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 Lettjournal_title
FEBS lettersauthors
Hook VY,Affolter HUdoi
10.1016/0014-5793(88)80508-8subject
Has Abstractpub_date
1988-10-10 00:00:00pages
338-42issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(88)80508-8journal_volume
238pub_type
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