Proinsulin C-peptide Regulates Ribosomal RNA Expression
نویسندگان
چکیده
منابع مشابه
Proinsulin C-peptide--biological activity?
Insulin—a hormone critical for the control of blood glucose—is first synthesized as a longer prohormone. During its maturation, a peptide, C-peptide, is cleaved from the protein, but has been thought to be biologically inert. [HN2], [HN3] Defying the rule that peptide hormones act only by binding to stereospecific receptors, Ido et al. (1) report on page 563 of this issue that C-peptide not onl...
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The C-peptide links the insulin A and B chains in proinsulin, providing thereby a means to promote their efficient folding and assembly in the endoplasmic reticulum during insulin biosynthesis. It then facilitates the intracellular transport, sorting, and proteolytic processing of proinsulin into biologically active insulin in the maturing secretory granules of the beta cells. These manifold fu...
متن کاملProinsulin C-peptide - A Consensus Statement
In recent years the physiological role of the proinsulin C-peptide has received increasing attention, focusing on the potential therapeutic value of C-peptide replacement in preventing and ameliorating type 1 diabetic complications. In order to consolidate these new data and to identify the immediate directions of C-peptide research and its clinical usefulness, an International Symposium was he...
متن کاملSpecific binding of proinsulin C-peptide to human cell membranes.
Recent reports have demonstrated beneficial effects of proinsulin C-peptide in the diabetic state, including improvements of kidney and nerve function. To examine the background to these effects, C-peptide binding to cell membranes has been studied by using fluorescence correlation spectroscopy. Measurements of ligand-membrane interactions at single-molecule detection sensitivity in 0.2-fl conf...
متن کاملIsolation and characterization of proinsulin C-peptide from bovine pancreas.
Although the enzymes that catalyze the transformation of proinsulin to insulin have not yet been identified, studies of intermediate forms of proinsulin isolated from bovine pancreas indicate the existence of a mechanism in which the interchain connecting peptide is cleaved with elimination of a pair of basic residues from each end to yield insulin and the intact remainder of the connecting pep...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2010
ISSN: 0021-9258
DOI: 10.1074/jbc.m109.053587