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Insulin‐induced decrease in 5′‐nucleotidase activity in skeletal muscle membranes

FEBS LettersPublished 10 October 1988Open access
Amira Klip, Toolsie Ramlal, André G. Douen, Elena Burdett, Douglas A. Young, Gregory D. Cartee
Citations49
SJR quartileQ1
SJR score1.22
SNIP0.77
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TL;DR

It is proposed that insulin may activate an endogenous phospholipase C that cleavesospholipid‐glycan‐anchored proteins as well as 5′‐nucleotidase, which is anchored to the membrane through inositol‐containing phospholIPid glycans.

Abstract

Insulin releases inositol phosphoglycans from myocytes in culture [(1986) Science 233, 967-972], which display insulinomimetic activity. Because 5'-nucleotidase is anchored to the membrane through inositol-containing phospholipid glycans, we investigated whether insulin could release the enzyme from the membrane. Membranes prepared from hindquarter muscles of rats perfused with insulin showed a 23% decrease in 5'-nucleotidase activity. Isolated membranes from muscle exposed to insulin in vitro also showed a small but reproducible decrease (9%) in 5'-nucleotidase activity relative to unexposed controls. Phospholipase C from Staphylococcus aureus released 60% of the membrane-bound 5'-nucleotidase. We propose that insulin may activate an endogenous phospholipase C that cleaves phospholipid-glycan-anchored proteins.

Keywords

MedicineBiochemistry, Genetics and Molecular Biology