Physiology exam – blood system

38. General characteristics of the blood system. Composition and functions of blood?

Blood functions:
1. Respiratory – carries oxygen and CO2
2. Thermoregulation
3. Help to from a clot
4. Immune function
5. Support of oncotic and osmotic pressure
6. Maintaining of acid-base balance of the tissues
7. Transport of nutrients and waste products

Blood system consist of:

1. Blood – which consists of 55% blood plasma and 45% formed elements which are cells and cell fragments
2. Blood forming organs – bone marrow
3. Blood destroying organs – liver, spleen
4. Storage of blood – f
5. Apparatus for regulation – Kidney regulates blood volume,

Blood composition: 6-8% of total body weight

55% Plasma 7% proteins Proteins include

91.5% water 54% Albumin
1% other solutes e.g. gases, 38% Globular protein
metabolic wastes and nutrients 7% fibrinogen
1% other
45% Blood formed elements Platelets 1.5-4*1011/L White blood cells
White blood cells 5-10*1010/L 60-70% Neutrophils
Erythrocytes 4.8-5.4G/L 20-25% Lymphocytes
3-8% Monocytes
2-4% Eosinophils
0.5-1% Basophils

Physical properties of Blood:

 pH: 7.35-7.45
 Viscosity: 3-4 centipoise
 Specific gravity: 1.056-1.066
Physiology of blood Systems

Unit Neutrophils Basophils Eosinophils Lymphocytes Monocyte

Young Stab/ Rod Segmental
Relative % 0-1% 1-6% 47-72% 0-1% 0.05-5% 18-37% 3-11%

0-0.01 0.01-0.06 0.47-0.72 0-0.01 0.005-0.05 0.18-0.37 0.03-0.11

Absolute 0.006 0.06-0.36 2.82-4.32 0-0.06 0.03-0.3 1.08-2.22 0.18-0.66
(i.e. *6)

39. Electrolytes in blood plasma?

Inorganic salts. Positively charged ions (cations) include Na+, K+, Ca2+, Mg2+; negatively charged ions
(anions) include Cl-, HPO42-, SO42-, and HCO3-. Help maintain osmotic pressure and play essential roles in
the function of cells. Less than 1% of blood plasma

40 The plasma proteins, their functional significance?

Albumin 54% Smallest and most numerous blood plasma proteins produced by the liver. Functions as transport
proteins for several steroid hormones and for fatty acids
Globulin 38% Produced by liver and plasma cells which develop from B-Lymphocytes. Immunoglobulins help to
attack virus and bacteria. Alpha and beta globulins transport iron, lipids and fat soluble vitamins
Fibrinogen 7% produced by liver, plays and important role in blood clotting

41. Erythrocyte sedimentation rate (ESR), factors that affect the ESR?

The erythrocyte sedimentation rate (ESR or sed rate) is the rate at which red blood cells sediment in a period of one
hour. It is a common hematology test, and is a non-specific measure of inflammation. To perform the test,
anticoagulated blood was traditionally placed in an upright tube, known as a Westergren tube, and the rate at which the
red blood cells fall was measured and reported in mm at the end of one hour.

In normal conditions, the red blood cells are negatively charged. Therefore, negatively charged red blood cells repel
each other and do not stack over each other. Besides, if the viscosity of blood is high, red blood cells would be slow to
fall to the base, thus lower the ESR.

Conditions that raises ESR:

 Anemia
 Renal failure
 Obesity
 Ageing
 ESR is also higher in women during menstruation and pregnancy

Conditions that reduces ESR:

 increased red blood cells (polycythemia) causes reduced ESR as blood viscosity increases
 Hemoglobinopathy such as sickle-cell disease can have low ESR due to improper shapes of red blood cells that
impairs stacking
The normal values of ESR in men is age (in years) divided by 2; for women, the normal value is age (in years) plus 10 then
divided by 2

Age 20 55 90
Men—5% exceed 12 14 19
Women—5% exceed 18 21 23

42. The acid-base status blood as a buffer systems of blood to maintain its sustainability?

Normal blood pH: 7.35-7.45

Buffer Systems in the Body

The buffer systems in the human body are extremely efficient, and different systems work at different rates. It takes
only seconds for the chemical buffers in the blood to make adjustments to pH. The respiratory tract can adjust the blood
pH upward in minutes by exhaling CO2 from the body. The renal system can also adjust blood pH through the excretion
of hydrogen ions (H+) and the conservation of bicarbonate, but this process takes hours to days to have an effect.

The buffer systems functioning in blood plasma include plasma proteins, phosphate, and bicarbonate and carbonic acid
buffers. The kidneys help control acid-base balance by excreting hydrogen ions and generating bicarbonate that helps
maintain blood plasma pH within a normal range. Protein buffer systems work predominantly inside cells.

Protein Buffers in Blood Plasma and Cells: Nearly all proteins can function as buffers. Proteins are made up of amino
acids, which contain positively charged amino groups and negatively charged carboxyl groups. The charged regions of
these molecules can bind hydrogen and hydroxyl ions, and thus function as buffers. Buffering by proteins accounts for
two-thirds of the buffering power of the blood and most of the buffering within cells.

Hemoglobin as a Buffer: Hemoglobin is the principal protein inside of red blood cells and accounts for one-third of the
mass of the cell. During the conversion of CO2 into bicarbonate, hydrogen ions liberated in the reaction are buffered by
hemoglobin, which is reduced by the dissociation of oxygen. This buffering helps maintain normal pH. The process is
reversed in the pulmonary capillaries to re-form CO2, which then can diffuse into the air sacs to be exhaled into the
atmosphere. This process is discussed in detail in the chapter on the respiratory system.

Phosphate Buffer: Phosphates are found in the blood in two forms: sodium dihydrogen phosphate ( Na 2 H 2 PO 4 − ),
which is a weak acid, and sodium monohydrogen phosphate ( Na 2 HPO 4 2- ), which is a weak base.

HCl + Na 2 HPO 4 → NaH 2 PO 4 + NaCl

(strong acid) + (weak base) → (weak acid) + (salt)

NaOH + NaH 2 PO 4 → Na 2 HPO 4 + H 2 O

(strong base) + (weak acid) → (weak base) + (water)

Bicarbonate-Carbonic Acid Buffer: The bicarbonate-carbonic acid buffer works in a fashion similar to phosphate buffers.
The bicarbonate is regulated in the blood by sodium, as are the phosphate ions. When sodium bicarbonate (NaHCO3),
comes into contact with a strong acid, such as HCl, carbonic acid (H2CO3), which is a weak acid, and NaCl are formed.
When carbonic acid comes into contact with a strong base, such as NaOH, bicarbonate and water are formed.
NaHCO 3 + HCl → H 2 CO 3 +NaCl

(sodium bicarbonate) + (strong acid) → (weak acid) + (salt)

H 2 CO 3 + NaOH→ HCO 3- + H 2 O

(weak acid) + (strong base)→(bicarbonate) + (water)

43. Red blood cells, their function?

Erythrocyte functions: erythrocytes are dedicated to respiratory gas transport. Hemoglobin reversibly binds with oxygen
and most oxygen in the blood is bound to hemoglobin. Erythrocytes do not contain nucleus and mitochondria Main
protein – hemoglobin (35 %) Energy – from glycolysis Life span – 120 days Formation is stimulated by erythropoetin

44. Types of hemoglobin and its compounds, their physiological role?

Normal level of hemoglobin (Hb) in blood in males is 14–16 g/dl and in females, 13–15 g/dl.

Hb is globular in shape

Hemoglobin type structure %

adult Hb (HbA) 2 alpha chains and 2 beta chains 97

Hb F (fetal Hb) of 2 alpha and 2 gamma chains 1

Hb A2 2 alpha and 2 delta chains. 2

Hemoglobin Derivatives:

Oxyhemoglobin oxy-Hb bright red substance formed by the combination of haemoglobin with oxygen,
present in oxygenated blood.
Deoxyhemoglobin Deoxy- Hb without oxygen
Hb
Methemoglobin Met-Hb Fe3+ instead of Fe2+ in heme group, can be due to congenital disease, drugs such as
benzocaine, aniline dyes
Carbonyl hemoglobin HbCO CO binds to Fe2+ in heme in the case of CO poisoning. CO has X200 the affinity to Fe2+
than oxygen
Carbaminohemoglobin CO2 is non covalently bound to globin chain of hemoglobin
HbCO2
Hemichromes Hemichromes are typically produced by the slow denaturation of methemoglobin
Ferritin High levels of ferritin can indicate an iron storage disorder, such as
hemochromatosis, or a chronic disease process. Low levels of ferritin are indicative of
iron deficiency, which causes anemia
Hemosidirin a yellowish brown granular pigment formed by breakdown of hemoglobin, found in
phagocytes and in tissues especially in disturbances of iron metabolism (as in
hemochromatosis, hemosiderosis, or some anemias)
45. White blood cells, their function?

46. Regulation development of leukocytes. Physiological leukocytosis?

Leukocytosis is white cells (the leukocyte count) above the normal range in the blood. It is frequently a sign of an
inflammatory response, most commonly the result of infection, but may also occur following certain parasitic infections
or bone tumors as well as leukemia. It may also occur after strenuous exercise, convulsions such as epilepsy, emotional
stress, pregnancy and labor, anesthesia, and epinephrine administration.

physiologic leukocytosis: any form of leukocytosis that is associated with apparently normal situations and that is not
directly related to a pathologic condition; for example, the temporary increase in the total number of white blood cells
that may occur during a single day, or from day to day, as well as in the newborn period, during childhood, after
strenuous exercise, during attacks of paroxysmal tachycardia, and in association with various other situations
47. Antigens and antibodies AB0 system and CDE?

ABO blood typing

There are four different types of blood A, B, AB, O They are determined by the protein (antigen) found on the RBC

Blood Type Blood Type Antigen on RBC Antibody in plasma

0(І)αβ 0 universal donor Neither A or B Both anti-A and anti-B
А(ІІ)β A A Anti B
В(ІІІ)α B B Anti A
АВ(ІV) AB universal recipient Both A and B Neither anti A or anti B
System СDЕ (rhesus).

There are 6 main аntigens of rhesus system: D, C, E; d, c, e.

48. Methods definitions of blood groups.

49. Samples of blood before transfusion.

50. The mechanism of Rh-conflict during pregnancy?

Rh incompatibility is a condition that occurs during pregnancy if a woman has Rh-negative blood and her baby has Rh-
positive blood.

"Rh-negative" and "Rh-positive" refer to whether your blood has Rh factor. Rh factor is a protein on red blood cells. If
you have Rh factor, you're Rh-positive. If you don't have it, you're Rh-negative. Rh factor is inherited (passed from
parents to children through the genes). Most people are Rh-positive.

When you're pregnant, blood from your baby can cross into your bloodstream, especially during delivery. If you're Rh-
negative and your baby is Rh-positive, your body will react to the baby's blood as a foreign substance.

Your body will create antibodies (proteins) against the baby's Rh-positive blood. These antibodies usually don't cause
problems during a first pregnancy. This is because the baby often is born before many of the antibodies develop.

However, the antibodies stay in your body once they have formed. Thus, Rh incompatibility is more likely to cause
problems in second or later pregnancies (if the baby is Rh-positive).

The Rh antibodies can cross the placenta and attack the baby's red blood cells. This can lead to hemolytic anemia

51. Platelets, their physiological role?

Platelets, also called thrombocytes are a component of blood whose function (along with the coagulation factors) is to
react to bleeding from blood vessel injury by clumping, thereby initiating a blood clot. Platelets have no cell nucleus:
they are fragments of cytoplasm that are derived from the megakaryocytes of the bone marrow, and then enter the
circulation. Circulating unactivated platelets are biconvex discoid (lens-shaped) structures, 2–3 µm in greatest diameter.
Platelets are found only in mammals.

Properties and function of platelets

 Quantity of platelets is 180-320 G/L.

 Diameter of platelets is 1-4 micrometers, thickness – 0,5-0,75 micrometers.
 They are the little piece of megakaryocytes cytoplasm (from one megacariocytes may develop few hundred of
platelets). Platelets circulates in blood from 5 to 11 days and then destroyed in liver, lungs, spleen by the cells of
macrophages system. Formation is regulated by thrombopoietin.
 Their granules contain serotonin, Ca2+, enzymes, ADP, and platelet-derived growth factor (PDGF)
 Platelets function in the clotting mechanism by forming a temporary plug that helps seal breaks in blood vessels
 Platelets not involved in clotting are kept inactive by Nitric Oxide (NO) and prostaglandins

Function of platelets

1. hemostatic function – platelets produce substances, which are secure the hemostasis.
2. Angiotrophic function – provide trophy of endotheliocytes of vessel wall, support structure and functions of
micro vessels. These function is realize by adhesion of platelets to endotheliocytes and injection the enzymes
into the endotheliocytes. For one day near 35 G/l of platelets do this function.
3. Transport function – transfer the enzymes, ADP, serotonin and other.
4. Phagocytes function – the contain of platelets help to kill viruses and antigens bodies.
 5. Regeneratory function – platelets have the growth factor, which help to grow the endothelial and muscles cells
which are present in the vessel wall.

The components of hemostasis are

1. wall of the vessels,

2. blood cells – platelets, erythrocytes, leukocytes,
3. enzymes and nonenzymes components of plasma – clotting and anticlotting substances, fibrinolytic
components.

There are 3 parts to coagulation: vasoconstriction, vessel-platelets (primary) and coagulative (secondary).

52. Vessel-platelet hemostasis, its mechanisms and physiological significance?

Stages of vessel-platelets hemostasis:

1. Shorting spasm of the vessels – vascular spasm duration to 1 minute is caused by catecholamines and other
enzymes. Diameter of vessels decrease on ½-⅓. Mechanism of it development determine by secretion of
serotonin and thromboxan A2 from platelets and epinephrine from ending of sympathetic nerves.
2. Adhesion of platelets – activation of platelets and stick it to the place of defect in vessel wall.
3. Reverse aggregation of platelets – the thrombus which are formed may make way for plasma.
4. Unreverse aggregation of platelets – the thrombus which are formed cannot may make way for plasma.
5. Retraction of platelets plug – decrease the size of plug, pack down the plug.
53. Coagulation hemostasis, its mechanisms and physiological significance?

The coagulation cascade of secondary hemostasis has two initial pathways which lead to fibrin formation. These are the
contact activation pathway (also known as the intrinsic pathway), and the tissue factor pathway (also known as the
extrinsic pathway), which both lead to the same fundamental reactions that produce fibrin

Characteristics of clotting factors

There are 12 clotting factors:

 I – fibrinogen;
 II – prothrombine;
 III – thromboplastin of tissue;
 IV – ions of calcium;
 V – proaccelerin;
 VII – proconvertin;
 VIII – antihemophylic factor A;
  IX – Christmas factor or antihemofilic factor B;
 X – Stuart-Prower factor or prothrombinase;
 XI – plasma thromboplastin antecedent;
 XII – Hageman factor;
 XIII – fibrin stabilizing factor

54. Coagulants and anticoagulants and their role in maintaining blood in the liquid state?

Anticoagulative mechanisms. Fibrinolysis

The primary anticoagulants are:

 antithrombin III (the most important anticoagulant in the blood);

 Heparin (originally found in the liver, by large basophilic cells in tissues of various organs. Heparin reduces the
ability of the blood to clot by blocking the change of prothrombin to thrombin. It can also be used to aid in
reducing clots in cases in which internal clotting has already occurred. Heparin form complex with antithrombin-
III. Activate nonenzyme fibrinolysis.);
  alpha-2-macroglobulin (Alpha-2-macroglobulin is a similar to antithrombin-heparin cofactor in that it combines
with the proteolytic coagulation factors. Its activity is not accelerated by heparin. Its function is mainly to act as
a binding agent for the coagulation factors and prevent their proteolytic action until they can be destroyed in
various ways. It a faint inhibitor of thrombin, connect with plasmin),
 alpha-1-antitripsin (Alpha-1-antitripsin inhibits thrombin activity, IXa, XIa, XIIa factors, plasmin and kallilrein),
 protein C (Protein C inhibits VIIIa, Va factors. It activity depend of thrombin and vitamin K concentration).

Primary anticoagulants are produce and present all time in plasma and secondary anticoagulants form in a case of blood
clotting. They are antithrombin-I or fibrin and products of fibrinolysis or products of fibrinogen degradation. Fibrin is
sorbs and inactivates thrombin and Xa factor. Products of fibrinolysis inactivate ending stage of clotting, IXa factor,
platelets' aggregation

Fibrinolysis: Clot dissolved by activity of plasmin, an enzyme which hydrolyzes fibrin

55. Mechanisms fibrinolysis, their physiological importance.

Fibrinolysis: Clot dissolved by activity of plasmin, an enzyme which hydrolyzes fibrin

Fibrinolysis is a process that prevents blood clots from growing and becoming problematic. This process has two types:
primary fibrinolysis and secondary fibrinolysis. The primary type is a normal body process, whereas secondary
fibrinolysis is the breakdown of clots due to a medicine, a medical disorder, or some other cause

In fibrinolysis, a fibrin clot, the product of coagulation, is broken down. Its main enzyme plasmin cuts the fibrin mesh at
various places, leading to the production of circulating fragments that are cleared by other proteases or by the kidney
and liver.
Plasmin is produced in an inactive form, plasminogen, in the liver. Although plasminogen cannot cleave fibrin, it still has
an affinity for it, and is incorporated into the clot when it is formed.

Tissue plasminogen activator (t-PA)[3] and urokinase are the agents that convert plasminogen to the active plasmin,
thus allowing fibrinolysis to occur. t-PA is released into the blood very slowly by the damaged endothelium of the blood
vessels, such that, after several days (when the bleeding has stopped), the clot is broken down. This occurs because
plasminogen became entrapped within the clot when it formed; as it is slowly activated, it breaks down the fibrin mesh.
t-PA and urokinase are themselves inhibited by plasminogen activator inhibitor-1 and plasminogen activator inhibitor-2
(PAI-1 and PAI-2). In contrast, plasmin further stimulates plasmin generation by producing more active forms of both
tissue plasminogen activator (tPA) and urokinase.

Alpha 2-antiplasmin and alpha 2-macroglobulin inactivate plasmin. Plasmin activity is also reduced by thrombin-
activatable fibrinolysis inhibitor (TAFI), which modifies fibrin to make it more resistant to the tPA-mediated
plasminogen.