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PROPROTEIN-PROCESSING ENDOPEPTIDASES OF THE INSULIN SECRETORY GRANULE

被引：30
作者：
BAILYES, EM
BENNETT, DL
HUTTON, JC
机构：
[1] Department of Clinical Biochemistry, University of Cambridge, Addenbrookes Hospital, Cambridge CB2 2QR, Hills Road
来源：
ENZYME | 1991年 / 45卷 / 5-6期
基金：
英国惠康基金;
关键词：
PROINSULIN; PROHORMONE CONVERTASE; ENDOPEPTIDASE; KEX-2; INSULIN GRANULE;
D O I：
10.1159/000468903
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Enzymological studies have implicated two Ca2+ dependent endopeptidases in the conversion of proinsulin to insulin: a type 1 activity and a type 2 activity which cleave on the C-terminal side of R31R32 and K64R65 in proinsulin, respectively. These activities were further characterized and their relationship to the mammalian family of subtilisin-like proteases was investigated. PC2 was expressed in neuroendocrine tissues and in insulinoma secretory granule fractions predominantly as a 65kDa protein. On anion-exchange chromatography of solubilized granules, PC1/3 immunoreactivity comigrated with a peak of type 1 activity whereas PC2 immunoreactivity coeluted with the peak of type 2 endopeptidase activity. PC2 antiserum gave a specific immunoprecipitation of type 2 activity from insulin granule extracts. It was concluded that the PC2 gene-product has type 2 endopeptidase activity.
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页码：301 / 313
页数：13
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