Chapter 3

Human Anatomy & Physiology

Eighth Edition

BIOLOGY 226 Professor McQuarters

amcquarters@ccc.edu

Cell Theory
The cell is the smallest structural and functional living unit  Organismal functions depend on individual and collective cell functions  Biochemical activities of cells are dictated by their specific subcellular structures  Continuity of life has a cellular basis


Cell Diversity
Over 200 different types of human cells  Types differ in size, shape, subcellular components, and functions


Erythrocytes Fibroblasts

Epithelial cells (a) Cells that connect body parts, form linings, or transport gases Skeletal Muscle cell Smooth muscle cells Nerve cell (e) Cell that gathers information and control body functions

(b) Cells that move organs and body parts Macrophage Fat cell

Sperm (f) Cell of reproduction

(c) Cell that stores (d) Cell that nutrients fights disease
Figure 3.1

Generalized Cell
All cells have some common structures and functions  Human cells have three basic parts:


Plasma membraneflexible outer boundary Cytoplasmintracellular fluid containing organelles Nucleuscontrol center

Chromatin Nucleolus Smooth endoplasmic reticulum Mitochondrion Cytosol Lysosome Centrioles Centrosome matrix

Nuclear envelope Nucleus Plasma membrane

Cytoskeletal elements Microtubule Intermediate filaments

Rough endoplasmic reticulum Ribosomes Golgi apparatus Secretion being released from cell by exocytosis Peroxisome
Figure 3.2

Plasma Membrane
Bimolecular layer of lipids and proteins in a constantly changing fluid mosaic  Plays a dynamic role in cellular activity  Separates intracellular fluid (ICF) from extracellular fluid (ECF)


Interstitial fluid (IF) = ECF that surrounds cells

Extracellular fluid (watery environment) Polar head of phospholipid molecule Cholesterol Glycolipid Glycoprotein

Carbohydrate of glycocalyx

Outwardfacing layer of phospholipids

Integral proteins Filament of cytoskeleton Peripheral Bimolecular Inward-facing proteins lipid layer layer of containing phospholipids Nonpolar proteins tail of phospholipid Cytoplasm molecule (watery environment)

Figure 3.3

Membrane Lipids


75% phospholipids (lipid bilayer)

Phosphate heads: polar and hydrophilic Fatty acid tails: nonpolar and hydrophobic (Review Fig. 2.16b)

5% glycolipids
Lipids with polar sugar groups on outer membrane surface

20% cholesterol
Increases membrane stability and fluidity

Lipid Rafts
~ 20% of the outer membrane surface  Contain phospholipids, sphingolipids, and cholesterol  May function as stable platforms for cellsignaling molecules


Membrane Proteins


Integral proteins
Firmly inserted into the membrane (most are transmembrane) Functions:


Transport proteins (channels and carriers), enzymes, or receptors

Membrane Proteins  Peripheral proteins

Loosely attached to integral proteins Include filaments on intracellular surface and glycoproteins on extracellular surface Functions:


Enzymes, motor proteins, cell-to-cell links, provide support on intracellular surface, and form part of glycocalyx

Extracellular fluid (watery environment) Polar head of phospholipid molecule Cholesterol Glycolipid Glycoprotein

Carbohydrate of glycocalyx

Outwardfacing layer of phospholipids

Integral proteins Filament of cytoskeleton Peripheral Bimolecular Inward-facing proteins lipid layer layer of containing phospholipids Nonpolar proteins tail of phospholipid Cytoplasm molecule (watery environment)

Figure 3.3

Functions of Membrane Proteins

1. 2. 3.

Transport Receptors for signal transduction Attachment to cytoskeleton and extracellular matrix

(a) Transport A protein (left) that spans the membrane may provide a hydrophilic channel across the membrane that is selective for a particular solute. Some transport proteins (right) hydrolyze ATP as an energy source to actively pump substances across the membrane.

Figure 3.4a

Signal

(b) Receptors for signal transduction A membrane protein exposed to the outside of the cell may have a binding site with a specific shape that fits the shape of a chemical messenger, such as a hormone. The external signal may cause a change in shape in the protein that initiates a chain of chemical reactions in the cell.

Receptor

Figure 3.4b

(c) Attachment to the cytoskeleton and extracellular matrix (ECM) Elements of the cytoskeleton (cells internal supports) and the extracellular matrix (fibers and other substances outside the cell) may be anchored to membrane proteins, which help maintain cell shape and fix the location of certain membrane proteins. Others play a role in cell movement or bind adjacent cells together.

Figure 3.4c

Functions of Membrane Proteins

4. 5. 6.

Enzymatic activity Intercellular joining Cell-cell recognition

(d) Enzymatic activity Enzymes A protein built into the membrane may be an enzyme with its active site exposed to substances in the adjacent solution. In some cases, several enzymes in a membrane act as a team that catalyzes sequential steps of a metabolic pathway as indicated (left to right) here.

Figure 3.4d

(e) Intercellular joining Membrane proteins of adjacent cells may be hooked together in various kinds of intercellular junctions. Some membrane proteins (CAMs) of this group provide temporary binding sites that guide cell migration and other cell-to-cell interactions. CAMs

Figure 3.4e

(f) Cell-cell recognition Some glycoproteins (proteins bonded to short chains of sugars) serve as identification tags that are specifically recognized by other cells.

Glycoprotein

Figure 3.4f

Membrane Junctions


Three types:
Tight junction Desmosome Gap junction

Membrane Junctions: Tight Junctions

Prevent fluids and most molecules from moving between cells  Where might these be useful in the body?


Plasma membranes of adjacent cells

Microvilli

Intercellular space

Basement membrane

Interlocking junctional proteins Intercellular space (a) Tight junctions: Impermeable junctions prevent molecules from passing through the intercellular space.
Figure 3.5a

Membrane Junctions: Desmosomes

Rivets or spot-welds that anchor cells together  Where might these be useful in the body?


Plasma membranes of adjacent cells

Microvilli

Intercellular space

Basement membrane Intercellular space Plaque

Linker glycoproteins (cadherins) (b) Desmosomes: Anchoring junctions bind adjacent cells together and help form an internal tension-reducing network of fibers.
Figure 3.5b

Intermediate filament (keratin)

Membrane Junctions: Gap Junctions



Transmembrane proteins form pores that allow small molecules to pass from cell to cell
For spread of ions between cardiac or smooth muscle cells

Plasma membranes of adjacent cells

Microvilli

Intercellular space

Basement membrane Intercellular space Channel between cells (connexon)

(c) Gap junctions: Communicating junctions allow ions and small molecules to pass from one cell to the next for intercellular communication.
Figure 3.5c

Membrane Transport
Plasma membranes are selectively permeable  Some molecules easily pass through the membrane; others do not


Types of Membrane Transport



Passive processes
No cellular energy (ATP) required Substance moves down its concentration gradient

Active processes
Energy (ATP) required Occurs only in living cell membranes

Passive Processes


What determines whether or not a substance can passively permeate a membrane?

1. 2. 3.

Lipid solubility of substance Channels of appropriate size Carrier proteins

Passive Processes
Simple diffusion  Carrier-mediated facilitated diffusion  Channel-mediated facilitated diffusion  Osmosis


Passive Processes: Simple Diffusion



Nonpolar lipid-soluble (hydrophobic) substances diffuse directly through the phospholipid bilayer

Extracellular fluid Lipidsoluble solutes

Cytoplasm (a) Simple diffusion of fat-soluble molecules directly through the phospholipid bilayer
Figure 3.7a

Passive Processes: Facilitated Diffusion



Certain lipophobic molecules (e.g., glucose, amino acids, and ions) use carrier proteins or channel proteins, both of which:
Exhibit specificity (selectivity) Are saturable; rate is determined by number of carriers or channels Can be regulated in terms of activity and quantity

Facilitated Diffusion Using Carrier Proteins

Transmembrane integral proteins transport specific polar molecules (e.g., sugars and amino acids)  Binding of substrate causes shape change in carrier


Lipid-insoluble solutes (such as sugars or amino acids)

(b) Carrier-mediated facilitated diffusion via a protein carrier specific for one chemical; binding of substrate causes shape change in transport protein
Figure 3.7b

Facilitated Diffusion Using Channel Proteins

Aqueous channels formed by transmembrane proteins selectively transport ions or water  Two types:


Leakage channels


Always open Controlled by chemical or electrical signals

Gated channels


Small lipidinsoluble solutes

(c) Channel-mediated facilitated diffusion through a channel protein; mostly ions selected on basis of size and charge
Figure 3.7c

Passive Processes: Osmosis

Movement of solvent (water) across a selectively permeable membrane  Water diffuses through plasma membranes:


Through the lipid bilayer Through water channels called aquaporins (AQPs)

Water molecules

Lipid billayer

Aquaporin (d) Osmosis, diffusion of a solvent such as water through a specific channel protein (aquaporin) or through the lipid bilayer
Figure 3.7d

Passive Processes: Osmosis

Water concentration is determined by solute concentration because solute particles displace water molecules  Osmolarity: The measure of total concentration of solute particles  When solutions of different osmolarity are separated by a membrane, osmosis occurs until equilibrium is reached


(a) Membrane permeable to both solutes and water Solute and water molecules move down their concentration gradients in opposite directions. Fluid volume remains the same in both compartments. Left compartment: Solution with lower osmolarity Right compartment: Solution with greater osmolarity Both solutions have the same osmolarity: volume unchanged

H2O Solute

Membrane

Solute molecules (sugar)

Figure 3.8a

(b) Membrane permeable to water, impermeable to solutes Solute molecules are prevented from moving but water moves by osmosis. Volume increases in the compartment with the higher osmolarity. Both solutions have identical osmolarity, but volume of the solution on the right is greater because only water is free to move

Left compartment

Right compartment

H2O

Membrane

Solute molecules (sugar)

Figure 3.8b

Importance of Osmosis
When osmosis occurs, water enters or leaves a cell  Change in cell volume disrupts cell function


Tonicity
Tonicity: The ability of a solution to cause a cell to shrink or swell  Isotonic: A solution with the same solute concentration as that of the cytosol  Hypertonic: A solution having greater solute concentration than that of the cytosol  Hypotonic: A solution having lesser solute concentration than that of the cytosol


(a)

Isotonic solutions

(b)

Hypertonic solutions

(c)

Hypotonic solutions

Cells retain their normal size and shape in isotonic solutions (same solute/water concentration as inside cells; water moves in and out).

Cells lose water by osmosis and shrink in a hypertonic solution (contains a higher concentration of solutes than are present inside the cells).

Cells take on water by osmosis until they become bloated and burst (lyse) in a hypotonic solution (contains a lower concentration of solutes than are present in cells).

Figure 3.9

Summary of Passive Processes

Process Simple diffusion Facilitated diffusion Osmosis Energy Source Kinetic energy Kinetic energy Kinetic energy Example Movement of O2 through phospholipid bilayer Movement of glucose into cells Movement of H2O through phospholipid bilayer or AQPs

Also see Table 3.1

Membrane Transport: Active Processes



Two types of active processes:

Active transport Vesicular transport

Both use ATP to move solutes across a living plasma membrane

Active Transport
Requires carrier proteins (solute pumps)  Moves solutes against a concentration gradient  Types of active transport:


Primary active transport Secondary active transport

Primary Active Transport



Energy from hydrolysis of ATP causes shape change in transport protein so that bound solutes (ions) are pumped across the membrane

Primary Active Transport



Sodium-potassium pump (Na+-K+ ATPase)

Located in all plasma membranes Involved in primary and secondary active transport of nutrients and ions Maintains electrochemical gradients essential for functions of muscle and nerve tissues

Extracellular fluid

Na+

Na+-K+ pump

ATP-binding site Cytoplasm

K+

Na+ bound

1 Cytoplasmic Na+ binds to pump protein. P ATP ADP

K+ released

6 K+ is released from the pump protein and Na+ sites are ready to bind Na+ again. The cycle repeats.

2 Binding of Na+ promotes phosphorylation of the protein by ATP.

Na+ released K+ bound

P Pi K+

5 K+ binding triggers release of the phosphate. Pump protein returns to its original conformation. P

3 Phosphorylation causes the protein to change shape, expelling Na+ to the outside.

4 Extracellular K+ binds to pump protein.

Figure 3.10

Extracellular fluid

Na+

Na+-K+ pump

ATP-binding site Cytoplasm

K+

1 Cytoplasmic Na+ binds to pump protein.

Figure 3.10 step 1

Na+ bound

P ATP ADP

2 Binding of Na+ promotes phosphorylation of the protein by ATP.

Figure 3.10 step 2

Na+ released

3 Phosphorylation causes the protein to change shape, expelling Na+ to the outside.
Figure 3.10 step 3

K+

4 Extracellular K+ binds to pump protein.

Figure 3.10 step 4

K+ bound

Pi

5 K+ binding triggers release of the phosphate. Pump protein returns to its original conformation.
Figure 3.10 step 5

K+ released

6 K+ is released from the pump protein

and Na+ sites are ready to bind Na+ again. The cycle repeats.
Figure 3.10 step 6

Extracellular fluid

Na+

Na+-K+ pump

ATP-binding site Cytoplasm

K+

Na+ bound

1 Cytoplasmic Na+ binds to pump protein. P ATP ADP

K+ released

6 K+ is released from the pump protein and Na+ sites are ready to bind Na+ again. The cycle repeats.

2 Binding of Na+ promotes phosphorylation of the protein by ATP.

Na+ released K+ bound

P Pi K+

5 K+ binding triggers release of the phosphate. Pump protein returns to its original conformation. P

3 Phosphorylation causes the protein to change shape, expelling Na+ to the outside.

4 Extracellular K+ binds to pump protein.

Figure 3.10

Secondary Active Transport

Depends on an ion gradient created by primary active transport  Energy stored in ionic gradients is used indirectly to drive transport of other solutes


Secondary Active Transport



Cotransportalways transports more than one substance at a time

Symport system: Two substances transported in same direction Antiport system: Two substances transported in opposite directions

Extracellular fluid Na+-glucose symport transporter loading glucose from ECF

Glucose Na+-glucose symport transporter releasing glucose into the cytoplasm

Na+-K+ pump

Cytoplasm
1 The ATP-driven Na+-K+ pump 2 As Na+ diffuses back across the

stores energy by creating a steep concentration gradient for Na+ entry into the cell.

membrane through a membrane cotransporter protein, it drives glucose against its concentration gradient into the cell. (ECF = extracellular fluid)
Figure 3.11

Extracellular fluid

Na+-K+ pump

Cytoplasm
1 The ATP-driven Na+-K+ pump

stores energy by creating a steep concentration gradient for Na+ entry into the cell.
Figure 3.11 step 1

Extracellular fluid Na+-glucose symport transporter loading glucose from ECF

Glucose Na+-glucose symport transporter releasing glucose into the cytoplasm

Na+-K+ pump

Cytoplasm
1 The ATP-driven Na+-K+ pump 2 As Na+ diffuses back across the

stores energy by creating a steep concentration gradient for Na+ entry into the cell.

membrane through a membrane cotransporter protein, it drives glucose against its concentration gradient into the cell. (ECF = extracellular fluid)
Figure 3.11 step 2

Vesicular Transport
Transport of large particles, macromolecules, and fluids across plasma membranes  Requires cellular energy (e.g., ATP)


Vesicular Transport


Functions:
Exocytosistransport out of cell Endocytosistransport into cell Transcytosistransport into, across, and then out of cell Substance (vesicular) traffickingtransport from one area or organelle in cell to another

Endocytosis and Transcytosis

Involve formation of protein-coated vesicles  Often receptor mediated, therefore very selective


1 Coated pit ingests

substance.

Extracellular fluid

Protein coat (typically clathrin) 2 Proteincoated vesicle detaches.

Plasma membrane

Cytoplasm
3 Coat proteins detach

and are recycled to plasma membrane. Transport vesicle Endosome

Uncoated endocytic vesicle 4 Uncoated vesicle fuses with a sorting vesicle called an endosome. Lysosome

5 Transport

vesicle containing membrane components moves to the plasma membrane for recycling.

6 Fused vesicle may (a) fuse

(a)

with lysosome for digestion of its contents, or (b) deliver its contents to the plasma membrane on the opposite side of the cell (transcytosis).

(b)

Figure 3.12

1 Coated pit ingests

substance.

Extracellular fluid

Protein coat (typically clathrin)

Plasma membrane

Cytoplasm

Figure 3.12 step 1

1 Coated pit ingests

substance.

Extracellular fluid

Protein coat (typically clathrin) 2 Proteincoated vesicle detaches.

Plasma membrane

Cytoplasm

Figure 3.12 step 2

1 Coated pit ingests

substance.

Extracellular fluid

Protein coat (typically clathrin) 2 Proteincoated vesicle detaches.

Plasma membrane

Cytoplasm
3 Coat proteins detach

and are recycled to plasma membrane.

Figure 3.12 step 3

1 Coated pit ingests

substance.

Extracellular fluid

Protein coat (typically clathrin) 2 Proteincoated vesicle detaches.

Plasma membrane

Cytoplasm
3 Coat proteins detach

and are recycled to plasma membrane.

Endosome Uncoated endocytic vesicle 4 Uncoated vesicle fuses with a sorting vesicle called an endosome.

Figure 3.12 step 4

1 Coated pit ingests

substance.

Extracellular fluid

Protein coat (typically clathrin) 2 Proteincoated vesicle detaches.

Plasma membrane

Cytoplasm
3 Coat proteins detach

and are recycled to plasma membrane. Transport vesicle Endosome

Uncoated endocytic vesicle 4 Uncoated vesicle fuses with a sorting vesicle called an endosome.

5 Transport

vesicle containing membrane components moves to the plasma membrane for recycling.

Figure 3.12 step 5

1 Coated pit ingests

substance.

Extracellular fluid

Protein coat (typically clathrin) 2 Proteincoated vesicle detaches.

Plasma membrane

Cytoplasm
3 Coat proteins detach

and are recycled to plasma membrane. Transport vesicle Endosome

Uncoated endocytic vesicle 4 Uncoated vesicle fuses with a sorting vesicle called an endosome. Lysosome

5 Transport

vesicle containing membrane components moves to the plasma membrane for recycling.

6 Fused vesicle may (a) fuse

(a)

with lysosome for digestion of its contents, or (b) deliver its contents to the plasma membrane on the opposite side of the cell (transcytosis).

(b)

Figure 3.12 step 6

Endocytosis


Phagocytosispseudopods engulf solids and bring them into cells interior

Macrophages and some white blood cells

Phagosome

(a) Phagocytosis The cell engulfs a large particle by forming projecting pseudopods (false feet) around it and enclosing it within a membrane sac called a phagosome. The phagosome is combined with a lysosome. Undigested contents remain in the vesicle (now called a residual body) or are ejected by exocytosis. Vesicle may or may not be proteincoated but has receptors capable of binding to microorganisms or solid particles.
Figure 3.13a

Endocytosis


Fluid-phase endocytosis (pinocytosis) plasma membrane infolds, bringing extracellular fluid and solutes into interior of the cell
Nutrient absorption in the small intestine

(b) Pinocytosis The cell gulps drops of extracellular fluid containing solutes into tiny vesicles. No receptors are used, so the process is nonspecific. Most vesicles are protein-coated.

Vesicle

Figure 3.13b

Endocytosis


Receptor-mediated endocytosisclathrincoated pits provide main route for endocytosis and transcytosis
Uptake of enzymes low-density lipoproteins, iron, and insulin

Vesicle

Receptor recycled to plasma membrane

(c) Receptor-mediated endocytosis Extracellular substances bind to specific receptor proteins in regions of coated pits, enabling the cell to ingest and concentrate specific substances (ligands) in protein-coated vesicles. Ligands may simply be released inside the cell, or combined with a lysosome to digest contents. Receptors are recycled to the plasma membrane in vesicles.

Figure 3.13c

Exocytosis


Examples:
Hormone secretion Neurotransmitter release Mucus secretion Ejection of wastes

Plasma membrane The process Extracellular of exocytosis SNARE (t-SNARE) fluid

Fusion pore formed

Secretory vesicle

The membraneVesicle bound vesicle SNARE (v-SNARE) migrates to the Molecule to plasma membrane. be secreted Cytoplasm

3 The vesicle

and plasma membrane fuse and a pore opens up.

2 There, proteins

at the vesicle Fused surface (v-SNAREs) v- and bind with t-SNAREs t-SNAREs (plasma membrane proteins).

4 Vesicle

contents are released to the cell exterior.

Figure 3.14a

Summary of Active Processes Process Energy Source Example

Primary active transport Secondary active transport Exocytosis Phagocytosis Pinocytosis Receptor-mediated endocytosis ATP Ion gradient ATP ATP ATP ATP Pumping of ions across membranes Movement of polar or charged solutes across membranes Secretion of hormones and neurotransmitters White blood cell phagocytosis Absorption by intestinal cells Hormone and cholesterol uptake

Also see Table 3.2

Membrane Potential
Separation of oppositely charged particles (ions) across a membrane creates a membrane potential (potential energy measured as voltage)  Resting membrane potential (RMP): Voltage measured in resting state in all cells


Ranges from 50 to 100 mV in different cells Results from diffusion and active transport of ions (mainly K+)

Generation and Maintenance of RMP

1.

2.

3.

The Na+ -K+ pump continuously ejects Na+ from cell and carries K+ back in Some K+ continually diffuses down its concentration gradient out of cell through K+ leakage channels Membrane interior becomes negative (relative to exterior) because of large anions trapped inside cell

Generation and Maintenance of RMP

4.

5.

6.

Electrochemical gradient begins to attract K+ back into cell RMP is established at the point where the electrical gradient balances the K+ concentration gradient A steady state is maintained because the rate of active transport is equal to and depends on the rate of Na+ diffusion into cell

Extracellular fluid

1 K+ diffuse down their steep

concentration gradient (out of the cell) via leakage channels. Loss of K+ results in a negative charge on the inner plasma membrane face.

2 K+ also move into the cell

because they are attracted to the negative charge established on the inner plasma membrane face.

3 A negative membrane potential

Potassium leakage channels (90 mV) is established when the movement of K+ out of the cell equals K+ movement into the cell. At this point, the concentration gradient promoting K+ exit exactly opposes the electrical gradient for K+ entry.

Cytoplasm

Protein anion (unable to follow K+ through the membrane)

Figure 3.15

Cell-Environment Interactions


Involves glycoproteins and proteins of glycocalyx

Cell adhesion molecules (CAMs) Membrane receptors

Roles of Cell Adhesion Molecules

Anchor cells to extracellular matrix or to each other  Assist in movement of cells past one another  CAMs of blood vessel lining attract white blood cells to injured or infected areas  Stimulate synthesis or degradation of adhesive membrane junctions  Transmit intracellular signals to direct cell migration, proliferation, and specialization


Roles of Membrane Receptors

 

Contact signalingtouching and recognition of cells; e.g., in normal development and immunity Chemical signalinginteraction between receptors and ligands (neurotransmitters, hormones and paracrines) to alter activity of cell proteins (e.g., enzymes or chemically gated ion channels) G proteinlinked receptorsligand binding activates a G protein, affecting an ion channel or enzyme or causing the release of an internal second messenger, such as cyclic AMP

1 Ligand (1st messenger) binds to the receptor.

2 The activated receptor binds to a G protein and activates it.

3 Activated G protein activates (or inactivates) effector protein (e.g., an enzyme) by causing its shape to change. Extracellular fluid Effector protein (e.g., an enzyme)

Ligand

Receptor

G protein GDP

Inactive 2nd messenger Active 2nd messenger Activated kinase enzymes Cascade of cellular responses (metabolic and structural changes)

4 Activated effector enzymes catalyze reactions that produce 2nd messengers in the cell 5 Second messengers activate other enzymes or ion channels 6 Kinase enzymes transfer phosphate groups from ATP to specific proteins and activate a series of other enzymes that trigger various cell responses. Intracellular fluid

Figure 3.16

1 Ligand (1st messenger) binds to the receptor. Extracellular fluid

Ligand

Receptor

Intracellular fluid

Figure 3.16 step 1

1 Ligand (1st messenger) binds to the receptor.

2 The activated receptor binds to a G protein and activates it. Extracellular fluid

Ligand

Receptor

G protein GDP

Intracellular fluid

Figure 3.16 step 2

1 Ligand (1st messenger) binds to the receptor.

2 The activated receptor binds to a G protein and activates it.

3 Activated G protein activates (or inactivates) effector protein (e.g., an enzyme) by causing its shape to change. Extracellular fluid Effector protein (e.g., an enzyme)

Ligand

Receptor

G protein GDP

Intracellular fluid

Figure 3.16 step 3

1 Ligand (1st messenger) binds to the receptor.

2 The activated receptor binds to a G protein and activates it.

3 Activated G protein activates (or inactivates) effector protein (e.g., an enzyme) by causing its shape to change. Extracellular fluid Effector protein (e.g., an enzyme)

Ligand

Receptor

G protein GDP

Inactive 2nd messenger Active 2nd messenger

4 Activated effector enzymes catalyze reactions that produce 2nd messengers in the cell

Intracellular fluid

Figure 3.16 step 4

1 Ligand (1st messenger) binds to the receptor.

2 The activated receptor binds to a G protein and activates it.

3 Activated G protein activates (or inactivates) effector protein (e.g., an enzyme) by causing its shape to change. Extracellular fluid Effector protein (e.g., an enzyme)

Ligand

Receptor

G protein GDP

Inactive 2nd messenger Active 2nd messenger Activated kinase enzymes

4 Activated effector enzymes catalyze reactions that produce 2nd messengers in the cell 5 Second messengers activate other enzymes or ion channels

Intracellular fluid

Figure 3.16 step 5

1 Ligand (1st messenger) binds to the receptor.

2 The activated receptor binds to a G protein and activates it.

3 Activated G protein activates (or inactivates) effector protein (e.g., an enzyme) by causing its shape to change. Extracellular fluid Effector protein (e.g., an enzyme)

Ligand

Receptor

G protein GDP

Inactive 2nd messenger Active 2nd messenger Activated kinase enzymes Cascade of cellular responses (metabolic and structural changes)

4 Activated effector enzymes catalyze reactions that produce 2nd messengers in the cell 5 Second messengers activate other enzymes or ion channels 6 Kinase enzymes transfer phosphate groups from ATP to specific proteins and activate a series of other enzymes that trigger various cell responses. Intracellular fluid

Figure 3.16 step 6

Cytoplasm

  

Located between plasma membrane and nucleus

Cytosol
Water with solutes (protein, salts, sugars, etc.)

Cytoplasmic organelles
Metabolic machinery of cell

Inclusions
Granules of glycogen or pigments, lipid droplets, vacuoles, and crystals

Cytoplasmic Organelles


Membranous
Mitochondria Peroxisomes Lysosomes Endoplasmic reticulum Golgi apparatus

Nonmembranous
Cytoskeleton Centrioles Ribosomes

Mitochondria
Double-membrane structure with shelflike cristae  Provide most of cells ATP via aerobic cellular respiration  Contain their own DNA and RNA


Outer mitochondrial membrane Ribosome

Mitochondrial DNA (a)

Inner mitochondrial membrane Cristae Matrix (c) Enzymes

(b)
Figure 3.17

Ribosomes
Granules containing protein and rRNA  Site of protein synthesis  Free ribosomes synthesize soluble proteins  Membrane-bound ribosomes (on rough ER) synthesize proteins to be incorporated into membranes or exported from the cell


Endoplasmic Reticulum (ER)

Interconnected tubes and parallel membranes enclosing cisternae  Continuous with nuclear membrane  Two varieties:


Rough ER Smooth ER

Smooth ER

Nuclear envelope Rough ER Ribosomes (a) Diagrammatic view of smooth and rough ER
Figure 3.18a

Rough ER
External surface studded with ribosomes  Manufactures all secreted proteins  Synthesizes membrane integral proteins and phospholipids


Smooth ER
 

Tubules arranged in a looping network Enzyme (integral protein) functions:

In the liverlipid and cholesterol metabolism, breakdown of glycogen, and, along with kidneys, detoxification of drugs, pesticides, and carcinogens Synthesis of steroid-based hormones In intestinal cellsabsorption, synthesis, and transport of fats In skeletal and cardiac musclestorage and release of calcium

Golgi Apparatus
Stacked and flattened membranous sacs  Modifies, concentrates, and packages proteins and lipids  Transport vessels from ER fuse with convex cis face of Golgi apparatus  Proteins then pass through Golgi apparatus to trans face  Secretory vesicles leave trans face of Golgi stack and move to designated parts of cell


1 Protein-

containing vesicles pinch off rough ER and migrate to fuse with membranes of Golgi apparatus.
2 Proteins are

Rough ER

Phagosome ER membrane Proteins in cisterna

Plasma membrane

modified within the Golgi compartments.

3 Proteins are

Pathway C: Lysosome containing acid hydrolase enzymes Vesicle becomes lysosome

then packaged within different vesicle types, depending on their ultimate destination.

Golgi apparatus Pathway A: Vesicle contents destined for exocytosis

Secretory vesicle

Secretion by exocytosis

Pathway B: Vesicle membrane to be incorporated into plasma membrane Extracellular fluid

Figure 3.20

Lysosomes
Spherical membranous bags containing digestive enzymes (acid hydrolases)  Digest ingested bacteria, viruses, and toxins  Degrade nonfunctional organelles  Break down and release glycogen  Break down bone to release Ca2+  Destroy cells in injured or nonuseful tissue (autolysis)


Endomembrane System


Overall function
Produce, store, and export biological molecules Degrade potentially harmful substances

Nucleus Smooth ER

Nuclear envelope

Rough ER Vesicle Plasma membrane Lysosome Golgi apparatus Transport vesicle

Figure 3.22

Endomembrane System

Peroxisomes
Membranous sacs containing powerful oxidases and catalases  Detoxify harmful or toxic substances  Neutralize dangerous free radicals (highly reactive chemicals with unpaired electrons)


Cytoskeleton


Elaborate series of rods throughout cytosol

Microtubules Microfilaments Intermediate filaments

Microfilaments
Dynamic actin strands attached to cytoplasmic side of plasma membrane  Involved in cell motility, change in shape, endocytosis and exocytosis


(a) Microfilaments Strands made of spherical protein subunits called actins Actin subunit 7 nm

Microfilaments form the blue network surrounding the pink nucleus in this photo.
Figure 3.23a

Intermediate Filaments
Tough, insoluble ropelike protein fibers  Resist pulling forces on the cell and attach to desmosomes


(b) Intermediate filaments Tough, insoluble protein fibers constructed like woven ropes Fibrous subunits 10 nm

Intermediate filaments form the purple batlike network in this photo.

Figure 3.23b

Microtubules
Dynamic hollow tubes  Most radiate from centrosome  Determine overall shape of cell and distribution of organelles


(c) Microtubules Hollow tubes of spherical protein subunits called tubulins Tubulin subunits 25 nm

Microtubules appear as gold networks surrounding the cells pink nuclei in this photo.
Figure 3.23c

Motor Molecules
Protein complexes that function in motility (e.g., movement of organelles and contraction)  Powered by ATP


Vesicle
ATP

Receptor for motor molecule Motor molecule (ATP powered)

Microtubule of cytoskeleton (a) Motor molecules can attach to receptors on vesicles or organelles, and walk the organelles along the microtubules of the cytoskeleton.

ATP

Motor molecule (ATP powered)

Cytoskeletal elements (microtubules or microfilaments) (b) In some types of cell motility, motor molecules attached to one element of the cytoskeleton can cause it to slide over another element, as in muscle contraction and cilia movement.
Figure 3.24

Centrosome
Cell center near nucleus  Generates microtubules; organizes mitotic spindle  Contains centrioles: Small tube formed by microtubules


Centrosome matrix Centrioles

(a)

Microtubules
Figure 3.25a

Cellular Extensions


Cilia and flagella

Whiplike, motile extensions on surfaces of certain cells Contain microtubules and motor molecules Cilia move substances across cell surfaces Longer flagella propel whole cells (tail of sperm)

Outer microtubule doublet Dynein arms Central microtubule Cross-linking proteins inside outer doublets Radial spoke TEM A cross section through the Microtubules cilium shows the 9 + 2 arrangement of microtubules. The doublets also have attached motor proteins, the dynein arms.

Cross-linking proteins inside outer doublets Radial spoke

The outer microtubule doublets and the two central microtubules are held together by cross-linking proteins and radial spokes. Cilium

Plasma membrane Basal body

Plasma membrane Triplet

TEM A longitudinal section of a cilium shows microtubules running the length of the structure.

TEM A cross section through the basal body. The nine outer doublets of a cilium extend into a basal body where each doublet joins another microtubule to form a ring of nine triplets. Basal body (centriole)

Figure 3.26

Power, or propulsive, stroke

Recovery stroke, when cilium is returning to its initial position

(a) Phases of ciliary motion. Layer of mucus

Cell surface

(b) Traveling wave created by the activity of many cilia acting together propels mucus across cell surfaces.

Figure 3.27

Cellular Extensions


Microvilli
Fingerlike extensions of plasma membrane Increase surface area for absorption Core of actin filaments for stiffening

Microvillus

Actin filaments Terminal web

Figure 3.28

Nucleus
Genetic library with blueprints for nearly all cellular proteins  Responds to signals and dictates kinds and amounts of proteins to be synthesized  Most cells are uninucleate  Red blood cells are anucleate  Skeletal muscle cells, bone destruction cells, and some liver cells are multinucleate


Nuclear pores Nuclear envelope Chromatin (condensed) Nucleolus Nucleus

Cisternae of rough ER (a)

Figure 3.29a

Nuclear Envelope
Double-membrane barrier containing pores  Outer layer is continuous with rough ER and bears ribosomes  Inner lining (nuclear lamina) maintains shape of nucleus  Pore complex regulates transport of large molecules into and out of nucleus


Surface of nuclear envelope.

Fracture line of outer membrane Nuclear pores Nucleus Nuclear lamina. The netlike lamina composed of intermediate filaments formed by lamins lines the inner surface of the nuclear envelope.

(b)

Nuclear pore complexes. Each pore is ringed by protein particles.

Figure 3.29b

Nucleoli
Dark-staining spherical bodies within nucleus  Involved in rRNA synthesis and ribosome subunit assembly


Chromatin
Threadlike strands of DNA (30%), histone proteins (60%), and RNA (10%)  Arranged in fundamental units called nucleosomes  Condense into barlike bodies called chromosomes when the cell starts to divide


1 DNA double
helix (2-nm diameter) Histones

2 Chromatin
(beads on a string) structure with nucleosomes

(a)

Linker DNA Nucleosome (10-nm diameter; eight histone proteins wrapped by two winds of the DNA double helix)

3 Tight helical fiber

(30-nm diameter)

4 Looped domain
structure (300-nm diameter)

5 Chromatid

(700-nm diameter) Metaphase chromosome (at midpoint of cell division) Figure 3.30

(b)

Cell Cycle
Defines changes from formation of the cell until it reproduces  Includes:


Interphase Cell division (mitotic phase)

Interphase
Period from cell formation to cell division  Nuclear material called chromatin  Four subphases:


G1 (gap 1)vigorous growth and metabolism G0gap phase in cells that permanently cease dividing S (synthetic)DNA replication G2 (gap 2)preparation for division

G1 checkpoint (restriction point) S Growth and DNA synthesis

G1 Growth

G2 Growth and final preparations for division

G2 checkpoint

Figure 3.31

Interphase

Centrosomes (each has 2 centrioles)

Plasma membrane

Nucleolus Interphase Nuclear envelope

Chromatin

Figure 3.33

DNA Replication
DNA helices begin unwinding from the nucleosomes  Helicase untwists the double helix and exposes complementary chains  The Y-shaped site of replication is the replication fork  Each nucleotide strand serves as a template for building a new complementary strand


DNA Replication


DNA polymerase only works in one direction

Continuous leading strand is synthesized Discontinuous lagging strand is synthesized in segments DNA ligase splices together short segments of discontinuous strand

DNA Replication
End result: two DNA molecules formed from the original  This process is called semiconservative replication


Chromosome

Free nucleotides

DNA polymerase

Old strand acts as a template for synthesis of new strand

Leading strand Two new strands (leading and lagging) synthesized in opposite directions Lagging strand

Old DNA Helicase unwinds the double helix and exposes the bases Replication fork Adenine
Thymine Cytosine Guanine

DNA polymerase Old (template) strand

Figure 3.32

Cell Division
Mitotic (M) phase of the cell cycle  Essential for body growth and tissue repair


Does not occur in most mature cells of nervous tissue, skeletal muscle, and cardiac muscle

Cell Division


Includes two distinct events:

1.

Mitosisfour stages of nuclear division:

   

Prophase Metaphase Anaphase Telophase

2.

Cytokinesisdivision of cytoplasm by cleavage furrow

G1 checkpoint (restriction point) S Growth and DNA synthesis

G1 Growth

G2 Growth and final preparations for division

G2 checkpoint

Figure 3.31

Prophase
Chromosomes become visible, each with two chromatids joined at a centromere  Centrosomes separate and migrate toward opposite poles  Mitotic spindles and asters form


Prophase
Nuclear envelope fragments  Kinetochore microtubules attach to kinetochore of centromeres and draw them toward the equator of the cell  Polar microtubules assist in forcing the poles apart


Early Prophase

Early mitotic spindle Aster

Early Prophase

Chromosome consisting of two sister chromatids

Centromere

Figure 3.33

Late Prophase

Polar microtubule Spindle pole Fragments of nuclear envelope

Kinetochore Late Prophase

Kinetochore microtubule

Figure 3.33

Metaphase
Centromeres of chromosomes are aligned at the equator  This plane midway between the poles is called the metaphase plate


Metaphase Spindle

Metaphase

Metaphase plate

Figure 3.33

Anaphase
Shortest phase  Centromeres of chromosomes split simultaneouslyeach chromatid now becomes a chromosome  Chromosomes (V shaped) are pulled toward poles by motor proteins of kinetochores  Polar microtubules continue forcing the poles apart


Anaphase

Daughter chromosomes Anaphase

Figure 3.33

Telophase
Begins when chromosome movement stops  The two sets of chromosomes uncoil to form chromatin  New nuclear membrane forms around each chromatin mass  Nucleoli reappear  Spindle disappears


Cytokinesis
Begins during late anaphase  Ring of actin microfilaments contracts to form a cleavage furrow  Two daughter cells are pinched apart, each containing a nucleus identical to the original


Nuclear envelope forming Telophase and Cytokinesis

Nucleolus forming

Contractile ring at cleavage furrow

Telophase

Figure 3.33

Control of Cell Division



Go signals:
Critical volume of cell when area of membrane is inadequate for exchange Chemicals (e.g., growth factors, hormones, cyclins, and cyclin-dependent kinases (Cdks))

Control of Cell Division



Stop signals:
Contact inhibition Growth-inhibiting factors produced by repressor genes

Protein Synthesis
DNA is the master blueprint for protein synthesis  Gene: Segment of DNA with blueprint for one polypeptide  Triplets of nucleotide bases form genetic library  Each triplet specifies coding for an amino acid


Nuclear envelope

Transcription

DNA

RNA Processing

Pre-mRNA

mRNA Nuclear pores Ribosome

Translation Polypeptide

Figure 3.34

Roles of the Three Main Types of RNA



Messenger RNA (mRNA)

Carries instructions for building a polypeptide, from gene in DNA to ribosomes in cytoplasm

Roles of the Three Main Types of RNA



Ribosomal RNA (rRNA)

A structural component of ribosomes that, along with tRNA, helps translate message from mRNA

Roles of the Three Main Types of RNA



Transfer RNAs (tRNAs)

Bind to amino acids and pair with bases of codons of mRNA at ribosome to begin process of protein synthesis

Transcription
Transfers DNA gene base sequence to a complementary base sequence of an mRNA  Transcription factor


Loosens histones from DNA in area to be transcribed Binds to promoter, a DNA sequence specifying start site of gene to be transcribed Mediates the binding of RNA polymerase to promoter

Transcription


RNA polymerase
Enzyme that oversees synthesis of mRNA Unwinds DNA template Adds complementary RNA nucleotides on DNA template and joins them together Stops when it reaches termination signal mRNA pulls off the DNA template, is further processed by enzymes, and enters cytosol

RNA polymerase Coding strand DNA

Promoter region

Template strand

Termination signal

1 Initiation: With the help of transcription factors, RNA polymerase binds to the promoter, pries apart the two DNA strands, and initiates mRNA synthesis at the start point on the template strand.

mRNA

Template strand Coding strand of DNA Rewinding of DNA RNA nucleotides Direction of transcription

2 Elongation: As the RNA polymerase moves along the template

strand, elongating the mRNA transcript one base at a time, it unwinds the DNA double helix before it and rewinds the double helix behind it.

Unwinding of DNA

mRNA transcript

mRNA

DNA-RNA hybrid region

Template strand RNA polymerase

3 Termination: mRNA synthesis ends when the termination signal

is reached. RNA polymerase and the completed mRNA transcript are released.

The DNA-RNA hybrid: At any given moment, 1618 base pairs of DNA are unwound and the most recently made RNA is still bound to DNA. This small region is called the DNA-RNA hybrid.

Completed mRNA transcript RNA polymerase

Figure 3.35

RNA polymerase Coding strand DNA

Promoter region

Template strand

Termination signal

1 Initiation: With the help of transcription factors, RNA

polymerase binds to the promoter, pries apart the two DNA strands, and initiates mRNA synthesis at the start point on the template strand.

Figure 3.35 step 1

mRNA

Template strand

2 Elongation: As the RNA polymerase moves along the template strand, elongating the mRNA transcript one base at a time, it unwinds the DNA double helix before it and rewinds the double helix behind it.

mRNA transcript
Figure 3.35 step 2

3 Termination: mRNA synthesis ends when the termination signal

is reached. RNA polymerase and the completed mRNA transcript are released.

Completed mRNA transcript

RNA polymerase

Figure 3.35 step 3

Coding strand of DNA Rewinding of DNA RNA nucleotides Direction of transcription Unwinding of DNA

mRNA

DNA-RNA hybrid region

Template strand RNA polymerase

The DNA-RNA hybrid: At any given moment, 1618 base pairs of DNA are unwound and the most recently made RNA is still bound to DNA. This small region is called the DNA-RNA hybrid.
Figure 3.35 step 4

RNA polymerase Coding strand DNA

Promoter region

Template strand

Termination signal

1 Initiation: With the help of transcription factors, RNA polymerase binds to the promoter, pries apart the two DNA strands, and initiates mRNA synthesis at the start point on the template strand.

mRNA

Template strand Coding strand of DNA Rewinding of DNA RNA nucleotides Direction of transcription

2 Elongation: As the RNA polymerase moves along the template

strand, elongating the mRNA transcript one base at a time, it unwinds the DNA double helix before it and rewinds the double helix behind it.

Unwinding of DNA

mRNA transcript

mRNA

DNA-RNA hybrid region

Template strand RNA polymerase

3 Termination: mRNA synthesis ends when the termination signal

is reached. RNA polymerase and the completed mRNA transcript are released.

The DNA-RNA hybrid: At any given moment, 1618 base pairs of DNA are unwound and the most recently made RNA is still bound to DNA. This small region is called the DNA-RNA hybrid.

Completed mRNA transcript RNA polymerase

Figure 3.35

Translation
Converts base sequence of nucleic acids into the amino acid sequence of proteins  Involves mRNAs, tRNAs, and rRNAs


Genetic Code


Each three-base sequence on DNA is represented by a codon

Codoncomplementary three-base sequence on mRNA

U UUU U UUC UUA UUG CUU C CUC CUA CUG AUU A AUC AUA Ile Leu Phe Leu

SECOND BASE C A UCU UCC UCA UCG CCU CCC CCA CCG ACU ACC ACA Thr Pro Ser UAU UAC UAA UAG CAU CAC CAA CAG AAU AAC AAA AAG GAU Ala GAC GAA GAG Tyr Stop Stop His Gln UGU UGC

G U Cys C

UGA Stop A Trp G UGG CGU CGC CGA CGG AGU AGC AGA AGG GGU GGC GGA GGG Gly Ser Arg Arg U C A G U C A G U C A G

Asn Lys

Met or AUG Start ACG GUU G GUC GUA GUG Val GCU GCC GCA GCG

Asp Glu

Figure 3.36

Translation
  

mRNA attaches to a small ribosomal subunit that moves along the mRNA to the start codon Large ribosomal unit attaches, forming a functional ribosome Anticodon of a tRNA binds to its complementary codon and adds its amino acid to the forming protein chain New amino acids are added by other tRNAs as ribosome moves along rRNA, until stop codon is reached

Nucleus

RNA polymerase

Energized by ATP, the correct amino acid is attached to each species of tRNA by aminoacyl-tRNA synthetase enzyme. Leu Amino acid

mRNA

Template strand of DNA

1 After mRNA synthesis in the nucleus, mRNA leaves the nucleus and attaches to a ribosome.

Nuclear pore tRNA Nuclear membrane G A A

2 Translation begins as incoming aminoacyl-tRNA recognizes the complementary codon calling for it at the A site on the ribosome. It hydrogen-bonds to the codon via its anticodon.

Released mRNA Aminoacyl-tRNA synthetase Leu

3 As the ribosome moves along the mRNA, and each codon is read in sequence, a new amino acid is added to the growing protein chain and the tRNA in the A site is translocated to the P site.

Ile Pro

tRNA head bearing anticodon

4 Once its amino acid is released from the P site, tRNA is ratcheted to the E site and then released to reenter the cytoplasmic pool, ready to be recharged with a new amino acid. The polypeptide is released when the stop codon is read.

E site

P site G G C

A site

Large ribosomal subunit

A U A C C G C U U Small ribosomal subunit

Codon 15

Codon 16

Codon 17

Direction of Portion of mRNA ribosome advance already translated

Figure 3.37

Nucleus

RNA polymerase

Energized by ATP, the correct amino acid is attached to each species of tRNA by aminoacyltRNA synthetase enzyme. Leu

mRNA

Template strand of DNA

Amino acid Nuclear pore

After mRNA synthesis in the nucleus, mRNA leaves the nucleus and attaches to a ribosome. Released mRNA

Nuclear membrane

tRNA GAA

Aminoacyl-tRNA synthetase

Figure 3.37 step 1

Leu 2 Translation begins as incoming aminoacyl-tRNA recognizes the complementary codon calling for it at the A site on the ribosome. It hydrogen-bonds to the codon via its anticodon.

Ile Pro

tRNA head bearing anticodon

E site

P site G G C

A site

Large ribosomal subunit Small ribosomal subunit

A U A C C G C U U

Codon Codon 15 16

Codon 17

Direction of Portion of ribosome advance mRNA already translated

Figure 3.37 step 2

Leu

3 As the ribosome moves

along the mRNA, and each codon is read in sequence, a new amino acid is added to the growing protein chain and the tRNA in the A site is translocated to the P site.

Ile Pro

tRNA head bearing anticodon

2 Translation begins as incoming aminoacyl-tRNA recognizes the complementary codon calling for it at the A site on the ribosome. It hydrogen-bonds to the codon via its anticodon.

E site

P site G G C

A site

Large ribosomal subunit Small ribosomal subunit

A U A C C G C U U

Codon Codon 15 16

Codon 17

Direction of Portion of ribosome advance mRNA already translated

Figure 3.37 step 3

Leu

3 As the ribosome moves

along the mRNA, and each codon is read in sequence, a new amino acid is added to the growing protein chain and the tRNA in the A site is translocated to the P site.

Ile Pro

tRNA head bearing anticodon

2 Translation begins as incoming aminoacyl-tRNA recognizes the complementary codon calling for it at the A site on the ribosome. It hydrogen-bonds to the codon via its anticodon.

4 Once its amino acid is

released from the P site, tRNA is ratcheted to the E site and then released to reenter the cytoplasmic pool, ready to be recharged with a new amino acid. The polypeptide is released when the stop codon is read.

E site

P site G G C

A site

Large ribosomal subunit Small ribosomal subunit

A U A C C G C U U

Codon Codon 15 16

Codon 17

Direction of Portion of ribosome advance mRNA already translated

Figure 3.37 step 4

Nucleus

RNA polymerase

Energized by ATP, the correct amino acid is attached to each species of tRNA by aminoacyl-tRNA synthetase enzyme. Leu Amino acid

mRNA

Template strand of DNA

1 After mRNA synthesis in the nucleus, mRNA leaves the nucleus and attaches to a ribosome.

Nuclear pore tRNA Nuclear membrane G A A

2 Translation begins as incoming aminoacyl-tRNA recognizes the complementary codon calling for it at the A site on the ribosome. It hydrogen-bonds to the codon via its anticodon.

Released mRNA Aminoacyl-tRNA synthetase Leu

3 As the ribosome moves along the mRNA, and each codon is read in sequence, a new amino acid is added to the growing protein chain and the tRNA in the A site is translocated to the P site.

Ile Pro

tRNA head bearing anticodon

4 Once its amino acid is released from the P site, tRNA is ratcheted to the E site and then released to reenter the cytoplasmic pool, ready to be recharged with a new amino acid. The polypeptide is released when the stop codon is read.

E site

P site G G C

A site

Large ribosomal subunit

A U A C C G C U U Small ribosomal subunit

Codon 15

Codon 16

Codon 17

Direction of Portion of mRNA ribosome advance already translated

Figure 3.37

Role of Rough ER in Protein Synthesis

mRNAribosome complex is directed to rough ER by a signal-recognition particle (SRP)  Forming protein enters the ER  Sugar groups may be added to the protein, and its shape may be altered  Protein is enclosed in a vesicle for transport to Golgi apparatus


1 The mRNA-ribosome complex is directed to the rough ER by the SRP. There the SRP binds to a receptor site.
ER signal sequence

2 Once attached to the ER, the SRP is released and the growing polypeptide snakes through the ER membrane pore into the cisterna. 3 The signal sequence is clipped off by an enzyme. As protein synthesis continues, sugar groups may be added to the protein. 4 In this example, the completed protein is released from the ribosome and folds into its 3-D conformation, a process aided by molecular chaperones. 5 The protein is enclosed within a protein (coatomer)-coated transport vesicle. The transport vesicles make their way to the Golgi apparatus, where further processing of the proteins occurs (see Figure 3.19).

Ribosome mRNA

Signal Signal recognition sequence particle Receptor site removed (SRP) Growing polypeptide

Sugar group

Released protein Rough ER cisterna

Cytoplasm

Transport vesicle pinching off

Coatomer-coated transport vesicle

Figure 3.39

1 The mRNA-ribosome complex is directed to the rough ER by the SRP. There the SRP binds to a receptor site.
ER signal sequence

Ribosome mRNA

Signal recognition particle Receptor site (SRP)

Rough ER cisterna

Cytoplasm

Figure 3.39 step 1

1 The mRNA-ribosome complex is directed to the rough ER by the SRP. There the SRP binds to a receptor site.
ER signal sequence

2 Once attached to the ER, the SRP is released and the growing polypeptide snakes through the ER membrane pore into the cisterna.

Ribosome mRNA

Signal recognition particle Receptor site (SRP) Growing polypeptide

Rough ER cisterna

Cytoplasm

Figure 3.39 step 2

1 The mRNA-ribosome complex is directed to the rough ER by the SRP. There the SRP binds to a receptor site.
ER signal sequence

2 Once attached to the ER, the SRP is released and the growing polypeptide snakes through the ER membrane pore into the cisterna. 3 The signal sequence is clipped off by an enzyme. As protein synthesis continues, sugar groups may be added to the protein.

Ribosome mRNA

Signal Signal recognition sequence particle Receptor site removed (SRP) Growing polypeptide

Sugar group

Rough ER cisterna

Cytoplasm

Figure 3.39 step 3

1 The mRNA-ribosome complex is directed to the rough ER by the SRP. There the SRP binds to a receptor site.
ER signal sequence

2 Once attached to the ER, the SRP is released and the growing polypeptide snakes through the ER membrane pore into the cisterna. 3 The signal sequence is clipped off by an enzyme. As protein synthesis continues, sugar groups may be added to the protein. 4 In this example, the completed protein is released from the ribosome and folds into its 3-D conformation, a process aided by molecular chaperones.

Ribosome mRNA

Signal Signal recognition sequence particle Receptor site removed (SRP) Growing polypeptide

Sugar group

Released protein Rough ER cisterna

Cytoplasm

Figure 3.39 step 4

1 The mRNA-ribosome complex is directed to the rough ER by the SRP. There the SRP binds to a receptor site.
ER signal sequence

2 Once attached to the ER, the SRP is released and the growing polypeptide snakes through the ER membrane pore into the cisterna. 3 The signal sequence is clipped off by an enzyme. As protein synthesis continues, sugar groups may be added to the protein. 4 In this example, the completed protein is released from the ribosome and folds into its 3-D conformation, a process aided by molecular chaperones. 5 The protein is enclosed within a protein (coatomer)-coated transport vesicle. The transport vesicles make their way to the Golgi apparatus, where further processing of the proteins occurs (see Figure 3.19).

Ribosome mRNA

Signal Signal recognition sequence particle Receptor site removed (SRP) Growing polypeptide

Sugar group

Released protein Rough ER cisterna

Cytoplasm

Transport vesicle pinching off

Coatomer-coated transport vesicle

Figure 3.39 step 5

Other Roles of DNA



Intron (junk) regions of DNA code for other types of RNA:

Antisense RNA


Prevents protein-coding RNA from being translated Small RNAs that interfere with mRNAs made by certain exons Folded RNAs that act as switches regulating protein synthesis in response to environmental conditions

MicroRNA


Riboswitches


Cytosolic Protein Degradation

Nonfunctional organelle proteins are degraded by lysosomes  Ubiquitin tags damaged or unneeded soluble proteins in cytosol; they are digested by enzymes of proteasomes


Extracellular Materials
Body fluids (interstitial fluid, blood plasma, and cerebrospinal fluid)  Cellular secretions (intestinal and gastric fluids, saliva, mucus, and serous fluids)  Extracellular matrix (abundant jellylike mesh containing proteins and polysaccharides in contact with cells)


Developmental Aspects of Cells

 

 

All cells of the body contain the same DNA but are not identical Chemical signals in the embryo channel cells into specific developmental pathways by turning some genes off Development of specific and distinctive features in cells is called cell differentiation Elimination of excess, injured, or aged cells occurs through programmed rapid cell death (apoptosis) followed by phagocytosis

Theories of Cell Aging

Wear and tear theory: Little chemical insults and free radicals have cumulative effects  Immune system disorders: Autoimmune responses and progressive weakening of the immune response  Genetic theory: Cessation of mitosis and cell aging are programmed into genes. Telomeres (strings of nucleotides on the ends of chromosomes) may determine the number of times a cell can divide.