scholarly journals Distribution of insulin receptor sites among liver plasma membrane subfractions

FEBS Letters ◽  
1973 ◽  
Vol 34 (2) ◽  
pp. 259-262 ◽  
Author(s):  
W.H. Evans ◽  
J.J.M. Bergeron ◽  
I.I. Geschwind
Keyword(s):  
Plasma Membrane ◽  
Insulin Receptor ◽  
Liver Plasma Membrane ◽  
Receptor Sites

scholarly journals The insulin-stimulated cyclic AMP phosphodiesterase binds to a single class of protein sites on the liver plasma membrane

1981 ◽  
Vol 198 (3) ◽  
pp. 703-706 ◽  
Author(s):  
M D Houslay ◽  
R J Marchmont
Keyword(s):  
Plasma Membrane ◽  
Cyclic Amp ◽  
Plasma Membranes ◽  
Receptor Site ◽  
Single Class ◽  
Liver Plasma Membrane ◽  
Cyclic Amp Phosphodiesterase ◽  
Receptor Sites ◽  
Rat Liver Plasma Membranes ◽  
Dependent Protein

The peripheral cycle AMP phosphodiesterase from rat liver plasma membranes binds with high affinity (2.4 nM) to a single class of receptor sites on the liver plasma membrane. These receptor sites appear to be proteins, as they are trypsin- and heat-labile. The sensitivity of these sites to denaturation by trypsin and heat is a first-order process. The presence of Ca2+ (5 mM) increases the affinity of these sites for the enzyme, but does not alter their total number. The receptor sites and the cyclic AMP phosphodiesterase occur in similar numbers, at around 2 pmol/mg of plasma-membrane protein. It is proposed that the peripheral, liver plasma-membrane cyclic AMP phosphodiesterase is attached to a specific site on the insulin receptor and that the binding of insulin to the receptor site triggers a conformational change in the enzyme such that the enzyme can be phosphorylated and activated by an endogenous cyclic AMP-dependent protein kinase.

Photoaffinity labeling of insulin receptor proteins of liver plasma membrane preparations

Biochemistry ◽  
1980 ◽  
Vol 19 (1) ◽  
pp. 70-76 ◽  
Author(s):  
Cecil C. Yip ◽  
Clement W. T. Yeung ◽  
Margaret L. Moule
Keyword(s):  
Plasma Membrane ◽  
Insulin Receptor ◽  
Photoaffinity Labeling ◽  
Receptor Proteins ◽  
Liver Plasma Membrane

Liver plasma membrane enzyme activities following glutaraldehyde fixation

Pathology ◽  
1976 ◽  
Vol 8 (1) ◽  
pp. 43-45 ◽  
Author(s):  
P.J. Hertzog ◽  
R.N. Le Page ◽  
P.S. Bhathal
Keyword(s):  
Plasma Membrane ◽  
Enzyme Activities ◽  
Glutaraldehyde Fixation ◽  
Liver Plasma Membrane ◽  
Membrane Enzyme

scholarly journals Revising Endosomal Trafficking under Insulin Receptor Activation

2021 ◽  
Vol 22 (13) ◽  
pp. 6978
Author(s):  
Maria J. Iraburu ◽  
Tommy Garner ◽  
Cristina Montiel-Duarte
Keyword(s):  
Plasma Membrane ◽  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Molecular Mechanisms ◽  
Receptor Activation ◽  
Small Gtpases ◽  
Early Endosome ◽  
Tyrosine Kinase Receptors ◽  
Endosomal Trafficking ◽  
Cell Functions

The endocytosis of ligand-bound receptors and their eventual recycling to the plasma membrane (PM) are processes that have an influence on signalling activity and therefore on many cell functions, including migration and proliferation. Like other tyrosine kinase receptors (TKR), the insulin receptor (INSR) has been shown to be endocytosed by clathrin-dependent and -independent mechanisms. Once at the early endosome (EE), the sorting of the receptor, either to the late endosome (LE) for degradation or back to the PM through slow or fast recycling pathways, will determine the intensity and duration of insulin effects. Both the endocytic and the endosomic pathways are regulated by many proteins, the Arf and Rab families of small GTPases being some of the most relevant. Here, we argue for a specific role for the slow recycling route, whilst we review the main molecular mechanisms involved in INSR endocytosis, sorting and recycling, as well as their possible role in cell functions.

Interaction between cortisol and arachidonic acid on the secretion of LH from ovine pituitary tissue

1991 ◽  
Vol 131 (1) ◽  
pp. 87-94 ◽  
Author(s):  
A. W. Nangalama ◽  
G. P. Moberg
Keyword(s):  
Arachidonic Acid ◽  
Plasma Membrane ◽  
Suppressive Effect ◽  
Inhibitory Effect ◽  
Adrenal Steroids ◽  
Membrane Phospholipids ◽  
Pituitary Tissue ◽  
Receptor Sites ◽  
Lh Release ◽  
Gonadotrophin Releasing Hormone

ABSTRACT In several species, glucocorticoids act directly on the pituitary gonadotroph to suppress the gonadotrophin-releasing hormone (GnRH)-induced secretion of the gonadotrophins, especially LH. A mechanism for this action of these adrenal steroids has not been established, but it appears that the glucocorticoids influence LH release by acting on one or more post-receptor sites. This study investigated whether glucocorticoids disrupt GnRH-induced LH release by altering the liberation of arachidonic acid from plasma membrane phospholipids, a component of GnRH-induced LH release. Using perifused ovine pituitary tissue, it was established that exposure of gonadotrophs to 1–1000 nmol cortisol/l for 4 h or longer significantly reduced GnRH-stimulated LH release with the maximal inhibitory effect being observed after 6 h of exposure to cortisol. This suppressive effect of cortisol could be reversed by administration of arachidonic acid, which in its own right could stimulate LH release from ovine pituitary tissue. Furthermore, the inhibitory effect of cortisol on GnRH-stimulated LH release could be directly correlated with decreased pituitary responsiveness to GnRH-stimulated arachidonic acid liberation, consistent with our hypothesis that glucocorticoids can suppress GnRH-induced secretion of LH by reducing the amount of arachidonic acid available for the exocytotic response of GnRH. Journal of Endocrinology (1991) 131, 87–94

scholarly journals Glucagon-(19-29), a Ca2+ pump inhibitory peptide, is processed from glucagon in the rat liver plasma membrane by a thiol endopeptidase.

1990 ◽  
Vol 265 (35) ◽  
pp. 21514-21519 ◽  
Author(s):  
P Blache ◽  
A Kervran ◽  
M Dufour ◽  
J Martinez ◽  
D Le-Nguyen ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Rat Liver ◽  
Inhibitory Peptide ◽  
Liver Plasma Membrane
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