BIOMAT Database Logo BIOMAT Database Logo

Chromogranin A-processing proteinases in purified chromaffin granules: contaminants or endogenous enzymes? 1990

A Laslop, and R Fischer-Colbrie, and H Kirschke, and R Hogue-Angeletti, and H Winkler
Department of Pharmacology, University of Innsbruck, Austria.

It was the purpose of this study to define the chromogranin A-processing proteinases present in highly purified preparations of bovine chromaffin granules. The most active enzyme had a pH optimum of 5.0 and was inhibited by pepstatin. It could be identified immunologically as a cathepsin D-like enzyme and subcellular fractionation established its lysosomal origin. After removal of this enzyme the remaining activity at pH 5.0 was mainly due to a cathepsin B-like proteinase. The presence of this enzyme could also be attributed to lysosomal contamination. In the presence of calcium, a further proteolytic activity became apparent at pH 5.0. This enzyme which was inhibited by rho-chloromercuriphenylsulfonic acid was localized in chromaffin granules. A trypsin-like peptidase, most active at pH 8.2, was enriched in a membrane wash of chromaffin granules. Subcellular fractionation indicated that this enzyme is preferentially bound to the membranes of very dense particles probably representing a subpopulation of chromaffin granules. This study establishes that the most active chromogranin A-degrading proteinases present in highly purified chromaffin granules are attributable to lysosomal contamination. Two enzymes with low activity (a Ca2+ activated proteinase and a trypsin-like enzyme) are, apparently, true constituents of chromaffin granules.

UI MeSH Term Description Entries
D008247 Lysosomes A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured or undergoes MEMBRANE FUSION. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed). Autolysosome,Autolysosomes,Lysosome
D009419 Nerve Tissue Proteins Proteins, Nerve Tissue,Tissue Proteins, Nerve
D010436 Pepstatins N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.
D010447 Peptide Hydrolases Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES. Peptidase,Peptidases,Peptide Hydrolase,Protease,Proteases,Proteinase,Proteinases,Proteolytic Enzyme,Proteolytic Enzymes,Esteroproteases,Enzyme, Proteolytic,Hydrolase, Peptide
D011480 Protease Inhibitors Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES). Antiprotease,Endopeptidase Inhibitor,Endopeptidase Inhibitors,Peptidase Inhibitor,Peptidase Inhibitors,Peptide Hydrolase Inhibitor,Peptide Hydrolase Inhibitors,Peptide Peptidohydrolase Inhibitor,Peptide Peptidohydrolase Inhibitors,Protease Antagonist,Protease Antagonists,Antiproteases,Protease Inhibitor,Antagonist, Protease,Antagonists, Protease,Hydrolase Inhibitor, Peptide,Hydrolase Inhibitors, Peptide,Inhibitor, Endopeptidase,Inhibitor, Peptidase,Inhibitor, Peptide Hydrolase,Inhibitor, Peptide Peptidohydrolase,Inhibitor, Protease,Inhibitors, Endopeptidase,Inhibitors, Peptidase,Inhibitors, Peptide Hydrolase,Inhibitors, Peptide Peptidohydrolase,Inhibitors, Protease,Peptidohydrolase Inhibitor, Peptide,Peptidohydrolase Inhibitors, Peptide
D002118 Calcium A basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes. Coagulation Factor IV,Factor IV,Blood Coagulation Factor IV,Calcium-40,Calcium 40,Factor IV, Coagulation
D002401 Cathepsin B A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS. Cathepsin B-Like Proteinase,Cathepsin B1,Cathepsin B Like Proteinase,Proteinase, Cathepsin B-Like
D002402 Cathepsin D An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D002731 4-Chloromercuribenzenesulfonate A cytotoxic sulfhydryl reagent that inhibits several subcellular metabolic systems and is used as a tool in cellular physiology. Chloromercuriphenylsulfonate,PCMBS,Chloromercuribenzene-p-sulphonic Acid,Chloromercuribenzenesulfonate,PCMPS,p-Chloromercuriphenylsulphonate,4 Chloromercuribenzenesulfonate,Acid, Chloromercuribenzene-p-sulphonic,Chloromercuribenzene p sulphonic Acid,p Chloromercuriphenylsulphonate

Related Publications

A Laslop, and R Fischer-Colbrie, and H Kirschke, and R Hogue-Angeletti, and H Winkler
Proenkephalin-processing enzymes in chromaffin granules: model for neuropeptide biosynthesis.
March 1996, Annals of the New York Academy of Sciences,
A Laslop, and R Fischer-Colbrie, and H Kirschke, and R Hogue-Angeletti, and H Winkler
Processing of chromogranin A within chromaffin granules starts at C- and N-terminal cleavage sites.
April 1988, FEBS letters,
A Laslop, and R Fischer-Colbrie, and H Kirschke, and R Hogue-Angeletti, and H Winkler
Mitochondrial enzymes and chromaffin granules.
December 1957, The Journal of physiology,
A Laslop, and R Fischer-Colbrie, and H Kirschke, and R Hogue-Angeletti, and H Winkler
Proteolytic processing of chromogranin A in cultured chromaffin cells.
February 1990, Biochimica et biophysica acta,
A Laslop, and R Fischer-Colbrie, and H Kirschke, and R Hogue-Angeletti, and H Winkler
Chromogranin C: a third component of the acidic proteins in chromaffin granules.
July 1986, Journal of neurochemistry,
A Laslop, and R Fischer-Colbrie, and H Kirschke, and R Hogue-Angeletti, and H Winkler
Chromogranin A, the major lumenal protein in chromaffin granules, controls fusion pore expansion.
February 2019, The Journal of general physiology,
A Laslop, and R Fischer-Colbrie, and H Kirschke, and R Hogue-Angeletti, and H Winkler
Proenkephalin processing enzyme with specificity toward paired basic residues purified from bovine adrenal chromaffin granules.
February 1985, Neuropeptides,
A Laslop, and R Fischer-Colbrie, and H Kirschke, and R Hogue-Angeletti, and H Winkler
Rapid, high-yield isolation of human chromogranin A from chromaffin granules of pheochromocytomas.
August 1992, Neuropeptides,
A Laslop, and R Fischer-Colbrie, and H Kirschke, and R Hogue-Angeletti, and H Winkler
Reserpine-induced processing of chromogranin A in cultured bovine adrenal chromaffin cells.
March 1992, Journal of neurochemistry,
A Laslop, and R Fischer-Colbrie, and H Kirschke, and R Hogue-Angeletti, and H Winkler
A unique proenkephalin-converting enzyme purified from bovine adrenal chromaffin granules.
October 1982, Biochemical and biophysical research communications,
Copied contents to your clipboard!