Loading…

The application of recombinant human collagen in tissue engineering

Collagen is the main structural protein in vertebrates. It plays an essential role in providing a scaffold for cellular support and thereby affecting cell attachment, migration, proliferation, differentiation, and survival. As such, it also plays an important role in numerous approaches to the engin...

Full description

Saved in:
Bibliographic Details
Published in:BioDrugs : clinical immunotherapeutics, biopharmaceuticals, and gene therapy biopharmaceuticals, and gene therapy, 2004-01, Vol.18 (2), p.103-119
Main Authors: Yang, Chunlin, Hillas, Patrick J, Báez, Julio A, Nokelainen, Minna, Balan, Juliana, Tang, James, Spiro, Robert, Polarek, James W
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c475t-b4de075a63b53545e1f0cb2dcd47cf7ca705e945d298bd40bed6bb4fe3345d123
cites cdi_FETCH-LOGICAL-c475t-b4de075a63b53545e1f0cb2dcd47cf7ca705e945d298bd40bed6bb4fe3345d123
container_end_page 119
container_issue 2
container_start_page 103
container_title BioDrugs : clinical immunotherapeutics, biopharmaceuticals, and gene therapy
container_volume 18
creator Yang, Chunlin
Hillas, Patrick J
Báez, Julio A
Nokelainen, Minna
Balan, Juliana
Tang, James
Spiro, Robert
Polarek, James W
description Collagen is the main structural protein in vertebrates. It plays an essential role in providing a scaffold for cellular support and thereby affecting cell attachment, migration, proliferation, differentiation, and survival. As such, it also plays an important role in numerous approaches to the engineering of human tissues for medical applications related to tissue, bone, and skin repair and reconstruction. Currently, the collagen used in tissue engineering applications is derived from animal tissues, creating concerns related to the quality, purity, and predictability of its performance. It also carries the risk of transmission of infectious agents and precipitating immunological reactions. The recent development of recombinant sources of human collagen provides a reliable, predictable and chemically defined source of purified human collagens that is free of animal components. The triple-helical collagens made by recombinant technology have the same amino acid sequence as human tissue-derived collagen. Furthermore, by achieving the equivalent extent of proline hydroxylation via coexpression of genes encoding prolyl hydroxylase with the collagen genes, one can produce collagens with a similar degree of stability as naturally occurring material. The recombinant production process of collagen involves the generation of single triple-helical molecules that are then used to construct more complex three-dimensional structures. If one loosely defines tissue engineering as the use of a biocompatible scaffold combined with a biologically active agent (be it a gene or gene construct, growth factor or other biologically active agent) to induce tissue regeneration, then the production of recombinant human collagen enables the engineering of human tissue based on a human matrix or scaffold. Recombinant human collagens are an efficient scaffold for bone repair when combined with a recombinant bone morphogenetic protein in a porous, sponge-like format, and when presented as a membrane, sponge or gel can serve as a basis for the engineering of skin, cartilage and periodontal ligament, depending on the specific requirements of the chosen application.
doi_str_mv 10.2165/00063030-200418020-00004
format article
fullrecord <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_71766967</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A199865569</galeid><sourcerecordid>A199865569</sourcerecordid><originalsourceid>FETCH-LOGICAL-c475t-b4de075a63b53545e1f0cb2dcd47cf7ca705e945d298bd40bed6bb4fe3345d123</originalsourceid><addsrcrecordid>eNqFkU1r3DAQhnVISdJN_kIQBHpzMrK-rOOyJGlhoZfkLCR5vFGxpa1lH_rv681uUwqBMoeBl-cdBh5CKIO7mil5DwCKA4eqBhCsgRqqJQJxRi4Z07xqGhAX5HMpP95Io8_JBZMglKzVJdk8vyJ1-30fg5tiTjR3dMSQBx-TSxN9nQeXaMh973aYaEx0iqXMSDHtYkIcY9pdkU-d6wten_aKvDw-PG--VtvvT982620VhJZT5UWLoKVT3EsuhUTWQfB1G1qhQ6eD0yDRCNnWpvGtAI-t8l50yPkSspqvyJfj3f2Yf85YJjvEEnB5LWGei9VMK2WU_i_IjDLaGLWAt0dw53q0MXV5Gl04wHbNjGmUlMos1N0H1DItDjHkhF1c8n8KzbEQxlzKiJ3dj3Fw4y_LwB6k2T_S7Ls0-yZtqd6cXp_9gO3f4skY_w1BAZLf</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19697996</pqid></control><display><type>article</type><title>The application of recombinant human collagen in tissue engineering</title><source>Springer Nature</source><creator>Yang, Chunlin ; Hillas, Patrick J ; Báez, Julio A ; Nokelainen, Minna ; Balan, Juliana ; Tang, James ; Spiro, Robert ; Polarek, James W</creator><creatorcontrib>Yang, Chunlin ; Hillas, Patrick J ; Báez, Julio A ; Nokelainen, Minna ; Balan, Juliana ; Tang, James ; Spiro, Robert ; Polarek, James W</creatorcontrib><description>Collagen is the main structural protein in vertebrates. It plays an essential role in providing a scaffold for cellular support and thereby affecting cell attachment, migration, proliferation, differentiation, and survival. As such, it also plays an important role in numerous approaches to the engineering of human tissues for medical applications related to tissue, bone, and skin repair and reconstruction. Currently, the collagen used in tissue engineering applications is derived from animal tissues, creating concerns related to the quality, purity, and predictability of its performance. It also carries the risk of transmission of infectious agents and precipitating immunological reactions. The recent development of recombinant sources of human collagen provides a reliable, predictable and chemically defined source of purified human collagens that is free of animal components. The triple-helical collagens made by recombinant technology have the same amino acid sequence as human tissue-derived collagen. Furthermore, by achieving the equivalent extent of proline hydroxylation via coexpression of genes encoding prolyl hydroxylase with the collagen genes, one can produce collagens with a similar degree of stability as naturally occurring material. The recombinant production process of collagen involves the generation of single triple-helical molecules that are then used to construct more complex three-dimensional structures. If one loosely defines tissue engineering as the use of a biocompatible scaffold combined with a biologically active agent (be it a gene or gene construct, growth factor or other biologically active agent) to induce tissue regeneration, then the production of recombinant human collagen enables the engineering of human tissue based on a human matrix or scaffold. Recombinant human collagens are an efficient scaffold for bone repair when combined with a recombinant bone morphogenetic protein in a porous, sponge-like format, and when presented as a membrane, sponge or gel can serve as a basis for the engineering of skin, cartilage and periodontal ligament, depending on the specific requirements of the chosen application.</description><identifier>ISSN: 1173-8804</identifier><identifier>DOI: 10.2165/00063030-200418020-00004</identifier><identifier>PMID: 15046526</identifier><language>eng</language><publisher>New Zealand: Wolters Kluwer Health, Inc</publisher><subject>Animals ; Biocompatible Materials ; Collagen - chemistry ; Collagen - classification ; Collagen - physiology ; Humans ; Recombinant Proteins - chemistry ; Recombinant Proteins - classification ; Recombinant Proteins - pharmacology ; Tissue Engineering - methods ; Tissue Engineering - trends</subject><ispartof>BioDrugs : clinical immunotherapeutics, biopharmaceuticals, and gene therapy, 2004-01, Vol.18 (2), p.103-119</ispartof><rights>COPYRIGHT 2004 Wolters Kluwer Health, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c475t-b4de075a63b53545e1f0cb2dcd47cf7ca705e945d298bd40bed6bb4fe3345d123</citedby><cites>FETCH-LOGICAL-c475t-b4de075a63b53545e1f0cb2dcd47cf7ca705e945d298bd40bed6bb4fe3345d123</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15046526$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yang, Chunlin</creatorcontrib><creatorcontrib>Hillas, Patrick J</creatorcontrib><creatorcontrib>Báez, Julio A</creatorcontrib><creatorcontrib>Nokelainen, Minna</creatorcontrib><creatorcontrib>Balan, Juliana</creatorcontrib><creatorcontrib>Tang, James</creatorcontrib><creatorcontrib>Spiro, Robert</creatorcontrib><creatorcontrib>Polarek, James W</creatorcontrib><title>The application of recombinant human collagen in tissue engineering</title><title>BioDrugs : clinical immunotherapeutics, biopharmaceuticals, and gene therapy</title><addtitle>BioDrugs</addtitle><description>Collagen is the main structural protein in vertebrates. It plays an essential role in providing a scaffold for cellular support and thereby affecting cell attachment, migration, proliferation, differentiation, and survival. As such, it also plays an important role in numerous approaches to the engineering of human tissues for medical applications related to tissue, bone, and skin repair and reconstruction. Currently, the collagen used in tissue engineering applications is derived from animal tissues, creating concerns related to the quality, purity, and predictability of its performance. It also carries the risk of transmission of infectious agents and precipitating immunological reactions. The recent development of recombinant sources of human collagen provides a reliable, predictable and chemically defined source of purified human collagens that is free of animal components. The triple-helical collagens made by recombinant technology have the same amino acid sequence as human tissue-derived collagen. Furthermore, by achieving the equivalent extent of proline hydroxylation via coexpression of genes encoding prolyl hydroxylase with the collagen genes, one can produce collagens with a similar degree of stability as naturally occurring material. The recombinant production process of collagen involves the generation of single triple-helical molecules that are then used to construct more complex three-dimensional structures. If one loosely defines tissue engineering as the use of a biocompatible scaffold combined with a biologically active agent (be it a gene or gene construct, growth factor or other biologically active agent) to induce tissue regeneration, then the production of recombinant human collagen enables the engineering of human tissue based on a human matrix or scaffold. Recombinant human collagens are an efficient scaffold for bone repair when combined with a recombinant bone morphogenetic protein in a porous, sponge-like format, and when presented as a membrane, sponge or gel can serve as a basis for the engineering of skin, cartilage and periodontal ligament, depending on the specific requirements of the chosen application.</description><subject>Animals</subject><subject>Biocompatible Materials</subject><subject>Collagen - chemistry</subject><subject>Collagen - classification</subject><subject>Collagen - physiology</subject><subject>Humans</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - classification</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Tissue Engineering - methods</subject><subject>Tissue Engineering - trends</subject><issn>1173-8804</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNqFkU1r3DAQhnVISdJN_kIQBHpzMrK-rOOyJGlhoZfkLCR5vFGxpa1lH_rv681uUwqBMoeBl-cdBh5CKIO7mil5DwCKA4eqBhCsgRqqJQJxRi4Z07xqGhAX5HMpP95Io8_JBZMglKzVJdk8vyJ1-30fg5tiTjR3dMSQBx-TSxN9nQeXaMh973aYaEx0iqXMSDHtYkIcY9pdkU-d6wten_aKvDw-PG--VtvvT982620VhJZT5UWLoKVT3EsuhUTWQfB1G1qhQ6eD0yDRCNnWpvGtAI-t8l50yPkSspqvyJfj3f2Yf85YJjvEEnB5LWGei9VMK2WU_i_IjDLaGLWAt0dw53q0MXV5Gl04wHbNjGmUlMos1N0H1DItDjHkhF1c8n8KzbEQxlzKiJ3dj3Fw4y_LwB6k2T_S7Ls0-yZtqd6cXp_9gO3f4skY_w1BAZLf</recordid><startdate>20040101</startdate><enddate>20040101</enddate><creator>Yang, Chunlin</creator><creator>Hillas, Patrick J</creator><creator>Báez, Julio A</creator><creator>Nokelainen, Minna</creator><creator>Balan, Juliana</creator><creator>Tang, James</creator><creator>Spiro, Robert</creator><creator>Polarek, James W</creator><general>Wolters Kluwer Health, Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20040101</creationdate><title>The application of recombinant human collagen in tissue engineering</title><author>Yang, Chunlin ; Hillas, Patrick J ; Báez, Julio A ; Nokelainen, Minna ; Balan, Juliana ; Tang, James ; Spiro, Robert ; Polarek, James W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c475t-b4de075a63b53545e1f0cb2dcd47cf7ca705e945d298bd40bed6bb4fe3345d123</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Biocompatible Materials</topic><topic>Collagen - chemistry</topic><topic>Collagen - classification</topic><topic>Collagen - physiology</topic><topic>Humans</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - classification</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Tissue Engineering - methods</topic><topic>Tissue Engineering - trends</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yang, Chunlin</creatorcontrib><creatorcontrib>Hillas, Patrick J</creatorcontrib><creatorcontrib>Báez, Julio A</creatorcontrib><creatorcontrib>Nokelainen, Minna</creatorcontrib><creatorcontrib>Balan, Juliana</creatorcontrib><creatorcontrib>Tang, James</creatorcontrib><creatorcontrib>Spiro, Robert</creatorcontrib><creatorcontrib>Polarek, James W</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>BioDrugs : clinical immunotherapeutics, biopharmaceuticals, and gene therapy</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yang, Chunlin</au><au>Hillas, Patrick J</au><au>Báez, Julio A</au><au>Nokelainen, Minna</au><au>Balan, Juliana</au><au>Tang, James</au><au>Spiro, Robert</au><au>Polarek, James W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The application of recombinant human collagen in tissue engineering</atitle><jtitle>BioDrugs : clinical immunotherapeutics, biopharmaceuticals, and gene therapy</jtitle><addtitle>BioDrugs</addtitle><date>2004-01-01</date><risdate>2004</risdate><volume>18</volume><issue>2</issue><spage>103</spage><epage>119</epage><pages>103-119</pages><issn>1173-8804</issn><abstract>Collagen is the main structural protein in vertebrates. It plays an essential role in providing a scaffold for cellular support and thereby affecting cell attachment, migration, proliferation, differentiation, and survival. As such, it also plays an important role in numerous approaches to the engineering of human tissues for medical applications related to tissue, bone, and skin repair and reconstruction. Currently, the collagen used in tissue engineering applications is derived from animal tissues, creating concerns related to the quality, purity, and predictability of its performance. It also carries the risk of transmission of infectious agents and precipitating immunological reactions. The recent development of recombinant sources of human collagen provides a reliable, predictable and chemically defined source of purified human collagens that is free of animal components. The triple-helical collagens made by recombinant technology have the same amino acid sequence as human tissue-derived collagen. Furthermore, by achieving the equivalent extent of proline hydroxylation via coexpression of genes encoding prolyl hydroxylase with the collagen genes, one can produce collagens with a similar degree of stability as naturally occurring material. The recombinant production process of collagen involves the generation of single triple-helical molecules that are then used to construct more complex three-dimensional structures. If one loosely defines tissue engineering as the use of a biocompatible scaffold combined with a biologically active agent (be it a gene or gene construct, growth factor or other biologically active agent) to induce tissue regeneration, then the production of recombinant human collagen enables the engineering of human tissue based on a human matrix or scaffold. Recombinant human collagens are an efficient scaffold for bone repair when combined with a recombinant bone morphogenetic protein in a porous, sponge-like format, and when presented as a membrane, sponge or gel can serve as a basis for the engineering of skin, cartilage and periodontal ligament, depending on the specific requirements of the chosen application.</abstract><cop>New Zealand</cop><pub>Wolters Kluwer Health, Inc</pub><pmid>15046526</pmid><doi>10.2165/00063030-200418020-00004</doi><tpages>17</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1173-8804
ispartof BioDrugs : clinical immunotherapeutics, biopharmaceuticals, and gene therapy, 2004-01, Vol.18 (2), p.103-119
issn 1173-8804
language eng
recordid cdi_proquest_miscellaneous_71766967
source Springer Nature
subjects Animals
Biocompatible Materials
Collagen - chemistry
Collagen - classification
Collagen - physiology
Humans
Recombinant Proteins - chemistry
Recombinant Proteins - classification
Recombinant Proteins - pharmacology
Tissue Engineering - methods
Tissue Engineering - trends
title The application of recombinant human collagen in tissue engineering
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T03%3A41%3A04IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20application%20of%20recombinant%20human%20collagen%20in%20tissue%20engineering&rft.jtitle=BioDrugs%20:%20clinical%20immunotherapeutics,%20biopharmaceuticals,%20and%20gene%20therapy&rft.au=Yang,%20Chunlin&rft.date=2004-01-01&rft.volume=18&rft.issue=2&rft.spage=103&rft.epage=119&rft.pages=103-119&rft.issn=1173-8804&rft_id=info:doi/10.2165/00063030-200418020-00004&rft_dat=%3Cgale_proqu%3EA199865569%3C/gale_proqu%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c475t-b4de075a63b53545e1f0cb2dcd47cf7ca705e945d298bd40bed6bb4fe3345d123%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=19697996&rft_id=info:pmid/15046526&rft_galeid=A199865569&rfr_iscdi=true