J. Biol. Chem., Vol. 255, Issue 19, 9005-9008, Oct, 1980
Formation of a receptor state from which insulin dissociates slowly in hepatic cells and plasma membranes
DB Donner and RE Corin
125I-insulin dissociated from rat hepatocytes and liver plasma membranes
with a time course suggestive of more than a single kinetic process.
Dissociation curves were resolved into rapidly and slowly dissociating
components. Increasing times of hormone-cell or hormone- membrane
incubation prior to the initiation of dissociation increased the proportion
of slowly dissociable 125I-insulin and decreased the proportion of rapidly
dissociating hormone. The rates of loss of rapidly and slowly dissociating
125I-insulin, 1 to 2 x 10(-3) and 2 to 7 x 10(-5) s-1, respectively, were
the same in cell and membrane incubates. The capacity of liver membranes
and hepatocytes to bind 125I- insulin in a slowly dissociable state was
saturable with respect to insulin concentration (approximately 10(-8) M).
The observation of the same physical process in both cells and plasma
membranes demonstrates a distinct role for receptors at the exterior
surface of target cells in the retention of insulin.