Solution structure of human proinsulin C-peptide
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...
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 کاملThe Proinsulin C-peptide—A Multirole Model
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 کاملStudies on human proinsulin. Isolation and amino acid sequence of the human pancreatic C-peptide.
Human proinsulin C-peptide has been extracted from human pancreas with acid-ethanol and purified by means of gel filtration, carboxymethyl-cellulose chromatography, paper electrophoresis, and partition chromatography. The purified material was judged to be about 98% pure by compositional analysis. Amino acid sequence analysis was carried out on the intact C-peptide and fragments derived by hydr...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: FEBS Journal
سال: 2005
ISSN: 1742-464X
DOI: 10.1111/j.1742-4658.2005.04843.x