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软骨钙素与II型前胶原的C-前肽相同。

Chondrocalcin is identical with the C-propeptide of type II procollagen.

作者信息

Van der Rest M, Rosenberg L C, Olsen B R, Poole A R

出版信息

Biochem J. 1986 Aug 1;237(3):923-5. doi: 10.1042/bj2370923.

DOI:10.1042/bj2370923
PMID:3800925
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1147077/
Abstract

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 type II collagen, as demonstrated previously, but in calcifying cartilage it may also be involved in those events leading to cartilage calcification, as earlier indicated.

摘要

通过比较软骨钙素N端区域和源自软骨钙素的胰蛋白酶肽段的序列分析,发现软骨基质分子软骨钙素的一级结构与II型前胶原的C-前肽相同。这意味着在II型胶原中,II型胶原的C-前肽不仅如先前所示参与II型胶原三螺旋的组装,而且在钙化软骨中,它也可能如早期所指出的那样参与导致软骨钙化的那些过程。

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Chondrocalcin is identical with the C-propeptide of type II procollagen.软骨钙素与II型前胶原的C-前肽相同。
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本文引用的文献

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A unique low molecular weight collagen secreted by cultured chick embryo chondrocytes.一种由培养的鸡胚软骨细胞分泌的独特的低分子量胶原蛋白。
J Biol Chem. 1982 Oct 25;257(20):12444-50.
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Effects of matrix macromolecules on chondrocyte gene expression: synthesis of a low molecular weight collagen species by cells cultured within collagen gels.基质大分子对软骨细胞基因表达的影响:在胶原凝胶中培养的细胞合成低分子量胶原种类
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Isolation and characterization of a 35,000 molecular weight subunit fetal cartilage matrix protein.一种分子量为35,000的亚基胎儿软骨基质蛋白的分离与特性鉴定
J Biol Chem. 1983 Jan 10;258(1):655-61.
5
Association of an extracellular protein (chondrocalcin) with the calcification of cartilage in endochondral bone formation.一种细胞外蛋白(软骨钙素)与软骨内骨形成过程中软骨钙化的关联。
J Cell Biol. 1984 Jan;98(1):54-65. doi: 10.1083/jcb.98.1.54.
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Primary structure determination of Escherichia coli heat-stable enterotoxin of porcine origin.猪源大肠杆菌热稳定肠毒素的一级结构测定
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Biosynthesis of cartilage procollagen. Influence of chain association and hydroxylation of prolyl residues on the folding of the polypeptides into the triple-helical conformation.软骨前胶原的生物合成。脯氨酰残基的链缔合和羟基化对多肽折叠成三螺旋构象的影响。
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Formation of interchain disulfide bonds and helical structure during biosynthesis of procollagen by embryonic tendon cells.胚胎肌腱细胞在原胶原蛋白生物合成过程中链间二硫键的形成及螺旋结构的形成。
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Proteoglycan Lt from chicken embryo sternum identified as type IX collagen.从鸡胚胸骨中鉴定出的蛋白聚糖Lt为IX型胶原蛋白。
J Biol Chem. 1985 Apr 25;260(8):4758-63.
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Enzymes converting procollagens to collagens.将前胶原转化为胶原的酶。
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