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Enigmatic insight into collagen
Collagen is a unique, triple helical molecule which forms the major part of extracellular matrix. It is the most abundant protein in the human body, representing 30% of its dry weight. It is the fibrous structural protein that makes up the white fibers (collagen fibers) of skin, tendons, bones, cart...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Medknow Publications & Media Pvt Ltd
2016
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4989561/ https://www.ncbi.nlm.nih.gov/pubmed/27601823 http://dx.doi.org/10.4103/0973-029X.185932 |
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author | Deshmukh, Shrutal Narendra Dive, Alka M Moharil, Rohit Munde, Prashant |
author_facet | Deshmukh, Shrutal Narendra Dive, Alka M Moharil, Rohit Munde, Prashant |
author_sort | Deshmukh, Shrutal Narendra |
collection | PubMed |
description | Collagen is a unique, triple helical molecule which forms the major part of extracellular matrix. It is the most abundant protein in the human body, representing 30% of its dry weight. It is the fibrous structural protein that makes up the white fibers (collagen fibers) of skin, tendons, bones, cartilage and all other connective tissues. Collagens are not only essential for the mechanical resistance and resilience of multicellular organisms, but are also signaling molecules defining cellular shape and behavior. The human body has at least 16 types of collagen, but the most prominent types are I, II and III. Collagens are produced by several cell types and are distinguishable by their molecular compositions, morphologic characteristics, distribution, functions and pathogenesis. This is the major fibrous glycoprotein present in the extracellular matrix and in connective tissue and helps in maintaining the structural integrity of these tissues. It has a triple helical structure. Various studies have proved that mutations that modify folding of the triple helix result in identifiable genetic disorders. Collagen diseases share certain similarities with autoimmune diseases, because autoantibodies specific to each collagen disease are produced. Therefore, this review highlights the role of collagen in normal health and also the disorders associated with structural and functional defects in collagen. |
format | Online Article Text |
id | pubmed-4989561 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Medknow Publications & Media Pvt Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-49895612016-09-06 Enigmatic insight into collagen Deshmukh, Shrutal Narendra Dive, Alka M Moharil, Rohit Munde, Prashant J Oral Maxillofac Pathol Review Article Collagen is a unique, triple helical molecule which forms the major part of extracellular matrix. It is the most abundant protein in the human body, representing 30% of its dry weight. It is the fibrous structural protein that makes up the white fibers (collagen fibers) of skin, tendons, bones, cartilage and all other connective tissues. Collagens are not only essential for the mechanical resistance and resilience of multicellular organisms, but are also signaling molecules defining cellular shape and behavior. The human body has at least 16 types of collagen, but the most prominent types are I, II and III. Collagens are produced by several cell types and are distinguishable by their molecular compositions, morphologic characteristics, distribution, functions and pathogenesis. This is the major fibrous glycoprotein present in the extracellular matrix and in connective tissue and helps in maintaining the structural integrity of these tissues. It has a triple helical structure. Various studies have proved that mutations that modify folding of the triple helix result in identifiable genetic disorders. Collagen diseases share certain similarities with autoimmune diseases, because autoantibodies specific to each collagen disease are produced. Therefore, this review highlights the role of collagen in normal health and also the disorders associated with structural and functional defects in collagen. Medknow Publications & Media Pvt Ltd 2016 /pmc/articles/PMC4989561/ /pubmed/27601823 http://dx.doi.org/10.4103/0973-029X.185932 Text en Copyright: © 2016 Journal of Oral and Maxillofacial Pathology http://creativecommons.org/licenses/by-nc-sa/3.0 This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 License, which allows others to remix, tweak, and build upon the work non-commercially, as long as the author is credited and the new creations are licensed under the identical terms. |
spellingShingle | Review Article Deshmukh, Shrutal Narendra Dive, Alka M Moharil, Rohit Munde, Prashant Enigmatic insight into collagen |
title | Enigmatic insight into collagen |
title_full | Enigmatic insight into collagen |
title_fullStr | Enigmatic insight into collagen |
title_full_unstemmed | Enigmatic insight into collagen |
title_short | Enigmatic insight into collagen |
title_sort | enigmatic insight into collagen |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4989561/ https://www.ncbi.nlm.nih.gov/pubmed/27601823 http://dx.doi.org/10.4103/0973-029X.185932 |
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