STUDIES ON THE MECHANISM OF INSULIN ANTAGONISM BY ALBUMIN IN RAT DIAPHRAGM,

Abstract

Utilizing a modification of the rat diaphragm technique, studies of the mechanism of action of the albumin-associated antagonist were carried out using human fraction V. It was demonstrated that the antagonist could not be washed off of the diaphragm, that prior exposure of the diaphragm to insulin did not fully protect it from subsequent antagonism of the insulin effect and that although antagonism was proportional to albumin concentration, large excesses of insulin could not completely overcome small concentrations of the antagonist. The intracellular accumulation of AIB was inhibited by the antagonistic albumin but not by a non-antagonistic one (bovine fraction V). Both albumins depressed radioactive glycine incorporation into muscle protein. The antagonist was shown to inhibit glucose uptake much more than glycogen synthesis. These data indicate that the albumin-associated antagonist primarily blocks insulin effects on transport by either an extremely strong binding to the muscle cell or an irreversible alteration of the disphragm's response to insulin without binding. (Author)

Document Details

Document Type
Technical Report
Publication Date
Jan 01, 1964
Accession Number
AD0618508

Entities

People

  • Charles J. Goodner
  • Mayer B. Davidson

Organizations

  • University of Washington

Tags

DTIC Thesaurus Topics

  • Anatomy
  • Biological Sciences
  • Biomolecules
  • Biopolymers
  • Cells
  • Chemical Compounds
  • Glycogen
  • Macromolecules
  • Molecules
  • Muscle Cells
  • Muscle Proteins
  • Muscles
  • Proteins
  • Skeletal Muscle
  • Transport Ships

Fields of Study

  • Biology

Readers

  • Cardiovascular Physiology
  • Molecular and Cellular Biochemistry