Insulin stimulates the acute release of adipsin from 3T3-L1 adipocytes.
Biochim Biophys Acta
; 1014(1): 83-9, 1989 Oct 30.
Article
em En
| MEDLINE
| ID: mdl-2679882
ABSTRACT
The release of adipsin, a serine proteinase with complement factor D activity, from 3T3-L1 adipocytes was measured by quantitative immunoblotting. This protein is secreted constitutively from 3T3-L1 adipocytes, and there is a 2-fold increase in the amount of adipsin released from cells treated with insulin for 1 to 10 min. Longer exposure to insulin had no further effect on the rate of adipsin release. Adipsin does not appear to be anchored by a glycosylphosphatidylinositol moiety, since adipsin which was been released with Triton X-114 from an intracellular membrane fraction partitions into the aqueous phase. Using a previously described procedure for the isolation of vesicles containing the insulin-responsive intracellular glucose transporters (GT vesicles), we show here that these GT vesicles contain an insulin-responsive pool of adipsin. Thus, insulin stimulates the secretion of a soluble protein, adipsin, as well as translocation to the plasma membrane of integral membrane proteins, including the glucose transporter, the transferrin receptors, and the insulin-like growth factor II receptor.
Buscar no Google
Base de dados:
MEDLINE
Assunto principal:
Tecido Adiposo
/
Insulina
Limite:
Animals
Idioma:
En
Ano de publicação:
1989
Tipo de documento:
Article