Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1983-3-11
pubmed:abstractText
Addition of the chemically synthesized proalbumin hexapeptide in a concentration of 110 micro M to the medium of isolated rat hepatocytes decreased net albumin synthesis by 12%. The synthesis of other secretory proteins was not altered. A weaker inhibitory effect on albumin synthesis was found for a tetrapeptide, a possible degradation product of the proalbumin hexapeptide. For the uptake of the hexa- and tetrapeptide into the cells, bovine serum albumin is required. In a reticulocyte and in a wheat germ cell-free system a propeptide concentration of 600 micro M inhibited albumin synthesis by 50%, whereas total protein synthesis was inhibited by 19% only, and the synthesis of alpha 1-antitrypsin was not inhibited. These results suggest that the synthesis of preproalbumin is regulated by a feedback mechanism with its propeptide as inhibitor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6053-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Hexa- and pentapeptide extension of proalbumin: feedback inhibition of albumin synthesis by its propeptide in isolated hepatocytes and in the cell-free system.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't