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A neurosecretory granule Lys-Arg Ca(2+)-dependent endopeptidase putatively involved in prooxytocin and provasopressin processing
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 156824
Author(s) Rouille, Y.; Spang, A.; Chauvet, J.; Acher, R.
Author(s) at UniBasel Spang, Anne
Year 1992
Title A neurosecretory granule Lys-Arg Ca(2+)-dependent endopeptidase putatively involved in prooxytocin and provasopressin processing
Journal Neuropeptides
Volume 22
Number 4
Pages / Article-Number 223-228
Keywords Amino Acid Sequence; Animals; Arginine/metabolism; Calcium/*pharmacology; Cytoplasmic Granules/*enzymology; Endopeptidases/*metabolism; Hydrogen-Ion Concentration; Lysine/metabolism; Molecular Sequence Data; Oxytocin/*metabolism; Pituitary Gland; Posterior/*enzymology/ultrastructure; Protein Precursors/*metabolism; Rats; Substrate Specificity; Vasopressins/*metabolism
Abstract A Ca(2+)-dependent endopeptidase cleaving at the carboxyl side of the paired Lys-Arg residues has been found in the neurosecretory granules of the rat neurointermediate pituitary. The specificity pattern on synthetic fluorogenic substrates, the inhibitor profile, the pH optimum of 5.0 and the Ca(2+)-dependence are compatible with an involvement of this enzyme in the prooxytocin and the provasopressin processing within the granules. The enzymatic features of the neurohypophysial granule endopeptidase resemble those of the insulinoma granule type II endopeptidase and suggest that the same Ca(2+)-dependent protease or closely related enzymes could be involved in processing Lys-Arg-containing prohormones in neuroendocrine cells.
Publisher Churchill Livingstone
ISSN/ISBN 0143-4179
edoc-URL http://edoc.unibas.ch/dok/A5259776
Full Text on edoc No
Digital Object Identifier DOI 10.1016/0143-4179(92)90050-7
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/1508325
ISI-Number WOS:A1992JG81400005
Document type (ISI) Article
 
   

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29/03/2024