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Inhibition of hepatocyte proliferation in vivo by a glycopeptide from rat serum
Author(s) -
Nadal C.
Publication year - 1987
Publication title -
cell proliferation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.647
H-Index - 74
eISSN - 1365-2184
pISSN - 0960-7722
DOI - 10.1111/j.1365-2184.1987.tb01315.x
Subject(s) - glycopeptide , in vivo , cell growth , hepatocyte , glycoprotein , dna synthesis , chemistry , biochemistry , biology , microbiology and biotechnology , medicine , in vitro , endocrinology , antibiotics
. The activity of a glycopeptide prepared from rat serum by treatment with trypsin and ultrafiltration was investigated in several in vivo proliferation systems. In baby rat hepatocytes synchronized by a subcutaneous injection of casein solution it caused a G 1 ‐S block, stopping cells at the end of the G 1 phase and sending them back to the G 0 phase. The glycopeptide also caused a G 1 ‐S block in young adult rats during the first semi‐synchronized wave of proliferation that followed partial hepatectomy. Inhibition of hepatocyte proliferation by the glycopeptide was suppressed by blood proteins from normal rats but not from acute phase rats. α 1 ‐acid glycoprotein, an acute phase protein, increased this inhibition and reversed the antagonistic effect of normal blood proteins. In normal baby rats a G 1 ‐S block of non‐synchronously proliferating hepatocytes was produced in two situations in which the antagonistic effect of normal blood proteins was eliminated: after treatment of the glycopeptide with leucine‐aminopeptidase, and after mixing it with α 1 ‐acid glycoprotein. The glycopeptide did not inhibit cell proliferation in kidney, submaxillary gland, or tongue epithelium. It seems to be the active component of a system that inhibits the proliferation of hepatocytes, probably by reducing their sensitivity to various mitogenic stimuli.

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