COL1A1 C-propeptide mutations cause ER mislocalization of procollagen and impair C-terminal procollagen processing
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چکیده
منابع مشابه
Procollagen C-proteinase Enhancer Stimulates Procollagen Processing by Binding to the C-propeptide Region Only*
Bone morphogenetic protein-1 (BMP-1) and the tolloid-like metalloproteinases control several aspects of embryonic development and tissue repair. Unlike other proteinases whose activities are regulated mainly by endogenous inhibitors, regulation of BMP-1/tolloid-like proteinases relies mostly on proteins that stimulate activity. Among these, procollagen C-proteinase enhancers (PCPEs) markedly in...
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Amino and carboxyl procollagen peptidases cleaved chick procollagen I to yield the intact amino propeptides and the disulfide-linked carboxyl propeptides, which were identified and partly characterized. The same products were released by these enzymes from the two separated fragments of procollagen produced by vertebrate collagenase, and this supports the concept that cleavage of amino and carb...
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BACKGROUND Sandwich enzyme-linked immunosorbent assay (ELISA) is one of the most frequently employed assays for clinical diagnosis, since this enables the investigator to identify specific protein biomarkers. However, the conventional assay using a 96-well microtitration plate is time- and sample-consuming, and therefore is not suitable for rapid diagnosis. To overcome these drawbacks, we perfo...
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The fate of the circulating C-terminal propeptide of type I procollagen (PICP) was studied. Trace amounts of 125I-PICP administered intravenously to rats disappeared from the blood with an initial t1/2 of 6.1 min. After 45 min the radioactivity was distributed as follows: liver, 36%; blood, 23%; kidneys, 18%; urine, 20%; spleen, 1%; lungs, 2%; heart, 0.4%. To prevent escape of label from the si...
متن کاملChondrocalcin is identical with the C-propeptide of type II procollagen.
The primary structure of the cartilage matrix molecule chondrocalcin has been found to be identical with that of the C-propeptide of type II procollagen by comparing sequence analyses of the N-terminal regions and of tryptic peptides derived from chondrocalcin. This implies that in type II collagen the C-propeptide of type II collagen is employed not only in the assembly of the triple helix of ...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
سال: 2019
ISSN: 0925-4439
DOI: 10.1016/j.bbadis.2019.04.018