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Example abstract:

Exit of nonglycosylated secretory proteins from the rough endoplasmic reticulum is asynchronous in the
exocrine pancreas

The path and synchrony of intracellular transport of 12 secretory proteins of the guinea pig exocrine
pancreas have been studied in pulse-chase amino acid labeling experiments by quantitative analysis of the
individual proteins recovered in subcellular fractions and extracellular samples. Protein fractionation was
accomplished by two-dimensional isoelectric focusing/SDS-gel electrophoresis. Use of a double-label protocol
allowed correction of the data on a protein-by-protein basis for leakage and adsorption artifacts which
accompany tissue homogenization. All the labeled secretory (pro)enzymes, including their isoenzymic forms,
were recovered in rough microsomal, Golgi-enriched and granule fractions during their transport to the cell
surface. However, major asynchrony was observed at four levels: exit from the rough endoplasmic reticulum;
transit through the Golgi complex; entry into granules; and discharge from the cell. Rapid transport rates were
observed for trypsinogen, chymotrypsinogen 2, procarboxypeptidase A2, and lipase 2. Slow transport rates were
observed for amylase and procarboxypeptidase B. In the presence of carbamylcholine or cholecystokinin
stimulation, the times required for 40% discharge of labeled chymotrypsinogen 2, trypsinogen, amylase, and
procarboxypeptidase B were 98, 102, 148, and 180 min, respectively. Transport rates did not correlate with
isoelectric point, molecular weight, or the presence of carbohydrate. These data suggest that interactions occur
within the rough endoplasmic reticulum, either between secretory (nonglyco)-proteins themselves or between
such proteins and the cisternal face of the rough endoplasmic reticulum.
Rough ER and Pancreatic Cells: Condensation-sorting events in the rough endoplasmic reticulum of
exocrine pancreatic cells.
In guinea pig exocrine pancreatic cells intracisternal granules (ICGs) occur at a low frequency within the
lumen of the RER. By starving and refeeding guinea pigs or injecting them in CoCl2 solution, the number of
these granules is greatly increased. We show here that ICGs contain the complete set of secreted pancreatic
digestive enzymes and proenzymes. Two other soluble proteins in the lumen of the RER, GRP 78/BiP and
protein disulphide isomerase (PDI), are specifically excluded from ICGs. The formation of ICGs, which occurs
without acidification of the RER cisternae, is therefore a sorting event involving the co-condensation of a
complete set of secretory enzymes and proenzymes, which for brevity we refer to collectively as the zymogens.
With the exception of approximately 50% of the RNase, the zymogens in ICGs are covalently cross-linked by
intermolecular disulphide bonds. The synthesis of all three resident ER cisternal proteins--PDI, GRP 78/BiP,
and GRP 94--with the carboxy-terminal sequence KDEL, is induced in response to the accumulation of massive
amounts of misfolded secretory protein in the ICGs in the lumen of the RER. After injection of rats with large
doses of parachlorophenylalanine-methylester, crystals form in the lumen of the RER. We show that these
crystals appear to be a lattice of amylase with the other zymogens incorporated between the layers. Both GRP
78/BiP and PDI are excluded from these crystals. The formation of these amylase crystals within the RER and
the inclusion of other zymogens is, therefore, also a sorting event. These data establish that in exocrine
pancreatic cells zymogens can co-condense in the RER into either amorphous aggregates or crystals that
exclude other soluble RER proteins. This demonstrates that co-condensation is a mechanism capable of sorting
zymogens within the secretory pathway.

Endoplasmic reticulum and Ca2+:Calcium binding proteins in the sarcoplasmic/endoplasmic reticulum


of muscle and nonmuscle cells
In this paper we review some of the large quantities of information currently available concerning the
identification, structure and function of Ca2+-binding proteins of endoplasmic and sarcoplasmic reticulum
membranes. The review places particular emphasis on identification and discussion of Ca2+ storage proteins
in these membranes. We believe that the evidence reviewed here supports the contention that the Ca2+-binding
capacity of both calsequestrin and calreticulin favor their contribution as the major Ca2+-binding proteins of
muscle and nonmuscle cells, respectively. Other Ca2+-binding proteins discovered in both endoplasmic
reticulum and sarcoplasmic reticulum membranes probably contribute to the overall Ca2+ storage capacity of
these membrane organelles, and they also play other important functional role such as posttranslational
modification of newly synthesized proteins, a cytoskeletal (structural) function, or movement of Ca2+ within
the lumen of the sarcoplasmic/endoplasmic reticulum towards the storage sites.
Golgi apparatus and alzheimer's: In Alzheimer's disease the Golgi apparatus of a population of neurons
without neurofibrillary tangles is fragmented and atrophic.
Recent immunocytochemical and morphometric studies in amyotrophic lateral sclerosis, Alzheimer's
disease (AD), and aging indicate that the neuronal Golgi apparatus is a reliable index of activity or
degeneration. To further evaluate a possible role of the Golgi apparatus in the pathogenesis of AD, we
examined by double labeling the neuronal Golgi apparatus, neurofibrillary tangles (NFTs), and senile plaques
(SPs) in the hippocampus of six cases of AD, and in 13 controls including three cases of a rare form of dementia
lacking distinctive histopathological features. The Golgi apparatus was visualized with a polyclonal antiserum
against MG-160, a membrane sialoglycoprotein of the organelle, and NFTs and SPs were visualized with
biotinylated basic fibroblast growth factor (bFGF). Only a rare SP contained a few small immunostained
elements of the Golgi apparatus. Neurons with intracellular NFTs, labeled with biotinylated bFGF, contained
intensely labeled but deformed Golgi apparatus, which was displaced by the NFTs and coalesced into larger
irregular granules. In contrast, a population of neurons without NFTs displayed fragmentation of the Golgi
apparatus, ie, the organelle appeared in the form of small round, disconnected, and dispersed elements instead
of the normal perinuclear network of irregular or linear profiles which often extended into the proximal
segments of dendrites. In addition, the fragmented neuronal Golgi apparatus was atrophic as the percentage of
the cell surface area occupied by the organelle was 4.4 +/- 0.6% SD, whereas in neurons with a normal Golgi
apparatus the percentage of the cell surface area occupied by the organelle was 10.3 +/- 0.3% SD. The results of
this study suggest that in AD the Golgi apparatus of a population of neurons without NFTs is involved in the
pathogenesis of the disease. Considering the role of the Golgi apparatus in the processing of polypeptides
destined for fast axoplasmic transports, the fragmentation of the organelle may be associated with functional
and structural impairments of axons and presynaptic terminals.

Golgi Apparatus and Epithelial Cells: THE FUNCTION OF THE GOLGI COMPLEX IN
TRANSITIONAL EPITHELIUM

The superficial squamous cells of rat transitional epithelium are limited, on their luminal face, by an
asymmetrically thickened membrane. Patches of similar thick membrane are found in the walls of the Golgi
cisternae and it is suggested that the Golgi system is the site of assembly of the thick plasma membrane. This
implies membrane flow from the Golgi apparatus to the cell surface, and there is indirect evidence that the
membrane is transported in the form of fusiform vacuoles, derived from the Golgi cisternae, which fuse with,
and become part of, the free cell membrane. Uptake of injected Imferon shows that similar, large, thick-walled
vacuoles may be formed by invagination of the free cell surface. Some of these vacuoles are subsequently
transformed into multivesicular bodies and autophagic vacuoles. The formation of other large heterogeneous
bodies is described, and some of these are shown to have acid phosphatase activity.

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