Insulin stimulated protein phosphorylation in human plasma liver membranes: detection of endogenous or plasma membrane associated substrates for insulin receptor kinase.
The present work discloses a procedure for preparation of human liver plasma membranes containing catalytically competent insulin receptor kinase. In addition to insulin promoted phosphorylation of the beta-subunit of insulin receptor kinase, insulin promoted phosphorylation of pp 120 and two other new proteins was demonstrated. The new proteins with molecular weights of 50,000 and 120,000 do not bind to WGA, pp 120 antibody or insulin receptor antibody, but bind to the antiphosphotyrosyl antibody. The identity and physiological significance of these putative substrates for insulin receptor kinase remains to be established.
Caro
J F
JF
Department of Medicine, School of Medicine, East Carolina University, Greenville 27858-4354.
Shafer
J A
JA
Taylor
S I
SI
Raju
S M
SM
Perrotti
N
N
Sinha
M K
MK
D002462:Cell Membrane / Q000187:drug effects* / Q000378:metabolism; D003924:Diabetes Mellitus, Type 2 / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D006801:Humans; D007328:Insulin / Q000494:pharmacology*; D008565:Membrane Proteins / Q000302:isolation & purification* / Q000378:metabolism; D009765:Obesity / Q000378:metabolism; D010750:Phosphoproteins / Q000302:isolation & purification* / Q000378:metabolism; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D011972:Receptor, Insulin / Q000378:metabolism*
D007328:Insulin; D008565:Membrane Proteins; D010750:Phosphoproteins; D011505:Protein-Tyrosine Kinases; D011972:Receptor, Insulin