Identification of zymogen and mature forms of human carboxypeptidase H. A processing enzyme for the synthesis of peptide hormones.

Abstract:

:Carboxypeptidase H (CPH) is one of several processing enzymes required for the conversion of peptide hormone precursors into their smaller active forms. In this study, high levels of CPH activity was found in a liver metastasis of a human ileal carcinoid which expresses beta-preprotachykinin mRNA and the tachykinin neuropeptides, substance P and substance K. This human CPH showed properties of a zinc-metallopeptidase that is structurally similar to bovine and rat CPH. Immunoblots of the human ileal carcinoma with anti-bovine CPH showed that CPH activity is represented by two proteins of apparent molecular masses 57 and 55 kDa. Cell-free translation of poly(A)+ RNA followed by immunoprecipitation with anti-bovine CPH showed that human CPH mRNA encodes a precursor protein of apparent molecular mass 75 kDa. These data demonstrate that human CPH is synthesized as a zymogen, prepro-CPH, which must be cleaved to form catalytically active CPH.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Hook VY,Affolter HU

doi

10.1016/0014-5793(88)80508-8

subject

Has Abstract

pub_date

1988-10-10 00:00:00

pages

338-42

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(88)80508-8

journal_volume

238

pub_type

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