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Cathepsin D-mediated processing of procollagen: lysosomal enzyme involvement in secretory processing of procollagen.

作者信息

Helseth D L, Veis A

出版信息

Proc Natl Acad Sci U S A. 1984 Jun;81(11):3302-6. doi: 10.1073/pnas.81.11.3302.

DOI:10.1073/pnas.81.11.3302
PMID:6587351
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC345495/
Abstract

The proteolytic removal of the extension COOH-terminal propeptide from procollagen has been examined in vitro. A crude enzyme activity was identified in a whole-chicken-embryo extract that acted at acid pH and appeared to be similar to one identified previously [Davidson, J. M., McEneany , L. S. G. & Bornstein , P. (1979) Eur. J. Biochem. 100, 551-558]. This activity was inhibitable by pepstatin but not by leupeptin, suggesting that it might be cathepsin D. Cathepsin D was purified 907-fold from chicken livers by affinity chromatography on pepstatin-aminohexyl-Sepharose 4B and was found to remove the COOH propeptides from procollagen. At pH 6.0, the site of cleavage appeared to shift from the COOH telopeptide to the COOH telopeptide/propeptide junction, based upon the difference in electrophoretic migration of the cleavage products, although determining the actual cleavage site will require end-group analysis. A model for the involvement of cathepsin D in the in vivo processing of procollagen is presented.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df6/345495/c6a5e8ec33f3/pnas00612-0049-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df6/345495/d6a6a8e6fb56/pnas00612-0048-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df6/345495/988ea0d3b8e2/pnas00612-0048-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df6/345495/c6a5e8ec33f3/pnas00612-0049-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df6/345495/d6a6a8e6fb56/pnas00612-0048-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df6/345495/988ea0d3b8e2/pnas00612-0048-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9df6/345495/c6a5e8ec33f3/pnas00612-0049-a.jpg

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本文引用的文献

1
The heat precipitation of collagen from neutral salt solutions: some rate-regulating factors.胶原蛋白在中性盐溶液中的热沉淀：一些速率调节因素。
J Biol Chem. 1958 Aug;233(2):355-60.
2
Cathepsin D from porcine and bovine spleen.来自猪和牛脾脏的组织蛋白酶D。
Methods Enzymol. 1981;80 Pt C:565-81. doi: 10.1016/s0076-6879(81)80045-6.
3
Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor recycling.氯喹通过损害受体再循环抑制溶酶体酶的胞饮作用并增强溶酶体酶的分泌。
克尼斯发育不全的特征是II型软骨胶原蛋白C-前肽的加工过程明显异常，导致原纤维组装不完善。
J Clin Invest. 1988 Feb;81(2):579-89. doi: 10.1172/JCI113356.
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Cathepsin D-like activity in neutrophils and monocytes.中性粒细胞和单核细胞中的组织蛋白酶D样活性。
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Assessment of procollagen processing defects by fibroblasts cultured in the presence of dextran sulphate.在硫酸葡聚糖存在的情况下培养成纤维细胞，评估前胶原加工缺陷。
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The C-terminal extrahelical peptide of type I collagen and its role in fibrillogenesis in vitro.
Biopolymers. 1982 Nov;21(11):2291-313. doi: 10.1002/bip.360211115.
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Lysosomotropic agents ammonium chloride and chloroquine inhibit both the synthesis and secretion of procollagen by freshly isolated embryonic chick tendon cells.溶酶体亲和剂氯化铵和氯喹可抑制新鲜分离的鸡胚肌腱细胞中前胶原的合成与分泌。
Biochem Biophys Res Commun. 1982 Apr 14;105(3):902-8. doi: 10.1016/0006-291x(82)91055-5.
6
Conversion of type II procollagen to collagen in vitro: removal of the carboxy-terminal extension is inhibited by several naturally occurring amino acids, polyamines, and structurally related compounds.
Arch Biochem Biophys. 1982 Apr 15;215(1):230-6. doi: 10.1016/0003-9861(82)90299-5.
7
Biosynthesis of lysosomal hydrolases: their synthesis in bound polysomes and the role of co- and post-translational processing in determining their subcellular distribution.溶酶体水解酶的生物合成：它们在附着核糖体中的合成以及共翻译和翻译后加工在决定其亚细胞分布中的作用。
J Cell Biol. 1982 Apr;93(1):135-43. doi: 10.1083/jcb.93.1.135.
8
Cathepsin B, Cathepsin H, and cathepsin L.组织蛋白酶B、组织蛋白酶H和组织蛋白酶L。
Methods Enzymol. 1981;80 Pt C:535-61. doi: 10.1016/s0076-6879(81)80043-2.
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Partial purification of a procollagen C-proteinase. Inhibition by synthetic peptides and sequential cleavage of type I procollagen.原胶原C蛋白酶的部分纯化。合成肽的抑制作用及I型前胶原的顺序裂解
Biochemistry. 1982 Feb 16;21(4):757-64. doi: 10.1021/bi00533a028.
10
Ultrastructural identification of extension aminopropeptides of type I and III collagens in human skin.人类皮肤中I型和III型胶原蛋白延伸氨基端肽的超微结构鉴定
Proc Natl Acad Sci U S A. 1981 Dec;78(12):7360-4. doi: 10.1073/pnas.78.12.7360.