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1 Department of Surgical Sciences, Section of Clinical Physiology, Karolinska Hospital, SE-171 76 Stockholm; and 2 Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 77 Stockholm, Sweden
The C-peptide of proinsulin is important
for the biosynthesis of insulin but has for a long time been considered
to be biologically inert. Data now indicate that C-peptide in the
nanomolar concentration range binds specifically to cell surfaces,
probably to a G protein-coupled surface receptor, with subsequent
activation of Ca2+-dependent intracellular signaling
pathways. The association rate constant, Kass, for
C-peptide binding to endothelial cells, renal tubular cells, and
fibroblasts is ~3 · 109
M
1. The binding is stereospecific, and
no cross-reaction is seen with insulin, proinsulin, insulin growth
factors I and II, or neuropeptide Y. C-peptide stimulates
Na+-K+-ATPase and endothelial nitric oxide
synthase activities. Data also indicate that C-peptide administration
is accompanied by augmented blood flow in skeletal muscle and skin,
diminished glomerular hyperfiltration, reduced urinary albumin
excretion, and improved nerve function, all in patients with type 1 diabetes who lack C-peptide, but not in healthy subjects. The
possibility exists that C-peptide replacement, together with insulin
administration, may prevent the development or retard the progression
of long-term complications in type 1 diabetes.
sodium-potassium-adenosine 5'-triphosphatase; endothelial nitric oxide synthase; renal function; autonomic nerve function; G protein
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