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胶原纤维组装:解决未决问题的新方法。

Collagen fibril assembly: New approaches to unanswered questions.

作者信息

Revell Christopher K, Jensen Oliver E, Shearer Tom, Lu Yinhui, Holmes David F, Kadler Karl E

机构信息

Department of Mathematics, University of Manchester, Alan Turing Building, Oxford Road, Manchester M13 9PL, UK.

Wellcome Centre for Cell-Matrix Research, Faculty of Biology, Medicine and Health, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, UK.

出版信息

Matrix Biol Plus. 2021 Jul 13;12:100079. doi: 10.1016/j.mbplus.2021.100079. eCollection 2021 Dec.

DOI:10.1016/j.mbplus.2021.100079
PMID:34381990
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8334717/
Abstract

Collagen fibrils are essential for metazoan life. They are the largest, most abundant, and most versatile protein polymers in animals, where they occur in the extracellular matrix to form the structural basis of tissues and organs. Collagen fibrils were first observed at the turn of the 20th century. During the last 40 years, the genes that encode the family of collagens have been identified, the structure of the collagen triple helix has been solved, the many enzymes involved in the post-translational modifications of collagens have been identified, mutations in the genes encoding collagen and collagen-associated proteins have been linked to heritable disorders, and changes in collagen levels have been associated with a wide range of diseases, including cancer. Yet despite extensive research, a full understanding of how cells assemble collagen fibrils remains elusive. Here, we review current models of collagen fibril self-assembly, and how cells might exert control over the self-assembly process to define the number, length and organisation of fibrils in tissues.

摘要

胶原纤维对于后生动物的生命至关重要。它们是动物体内最大、最丰富且最具多功能性的蛋白质聚合物,存在于细胞外基质中,构成组织和器官的结构基础。胶原纤维最早是在20世纪之交被观察到的。在过去的40年里,编码胶原家族的基因已被鉴定,胶原三螺旋的结构已被解析,参与胶原翻译后修饰的众多酶已被识别,编码胶原及胶原相关蛋白的基因突变已与遗传性疾病相关联,并且胶原水平的变化已与包括癌症在内的多种疾病相关。然而,尽管进行了广泛的研究,对细胞如何组装胶原纤维仍缺乏全面的了解。在此,我们综述了当前胶原纤维自组装的模型,以及细胞如何对自组装过程进行调控以确定组织中纤维的数量、长度和组织方式。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/110e/8334717/f962c491800a/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/110e/8334717/10ca9b9bf471/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/110e/8334717/465169887a28/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/110e/8334717/fb1b33fc9da2/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/110e/8334717/f962c491800a/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/110e/8334717/10ca9b9bf471/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/110e/8334717/465169887a28/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/110e/8334717/fb1b33fc9da2/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/110e/8334717/f962c491800a/gr4.jpg

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Preservation of collagen in the soft tissues of frozen mammoths.冷冻猛犸象软组织中胶原蛋白的保存。
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A Recruitment Model of Tendon Viscoelasticity That Incorporates Fibril Creep and Explains Strain-Dependent Relaxation.纳入原纤维蠕变并解释应变相关松弛的肌腱粘弹性募集模型。
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Giantin is required for intracellular N-terminal processing of type I procollagen.巨大多肽是Ⅰ型前胶原 N 端肽内加工所必需的。
在小鼠前肢形态发生过程中,细胞外基质沉积先于肌肉-肌腱整合。
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