Loading…
Conjugation of extracellular matrix proteins to basal lamina analogs enhances keratinocyte attachment
The dermal–epidermal junction of skin contains extracellular matrix proteins that are involved in initiating and controlling keratinocyte signaling events such as attachment, proliferation, and terminal differentiation. To characterize the relationship between extracellular matrix proteins and kerat...
Saved in:
Published in: | Journal of biomedical materials research. Part A 2007-02, Vol.80A (2), p.444-452 |
---|---|
Main Authors: | , , , |
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-c3673-837a99bdf79c8ef77d44ef460e46270bae2b541c68dd9e8702feef609e092f2c3 |
---|---|
cites | cdi_FETCH-LOGICAL-c3673-837a99bdf79c8ef77d44ef460e46270bae2b541c68dd9e8702feef609e092f2c3 |
container_end_page | 452 |
container_issue | 2 |
container_start_page | 444 |
container_title | Journal of biomedical materials research. Part A |
container_volume | 80A |
creator | Bush, Katie A. Downing, Brett R. Walsh, Sarah E. Pins, George D. |
description | The dermal–epidermal junction of skin contains extracellular matrix proteins that are involved in initiating and controlling keratinocyte signaling events such as attachment, proliferation, and terminal differentiation. To characterize the relationship between extracellular matrix proteins and keratinocyte attachment, a biomimetic design approach was used to precisely tailor the surface of basal lamina analogs with biochemistries that emulate the native biochemical composition found at the dermal–epidermal junction. A high‐throughput screening device was developed by our laboratory that allows for the simultaneous investigation of the conjugation of individual extracellular matrix proteins (e.g. collagen type I, collagen type IV, laminin, or fibronectin) as well as their effect on keratinocyte attachment, on the surface of an implantable collagen membrane. Fluorescence microscopy coupled with quantitative digital image analyses indicated that the extracellular matrix proteins adsorbed to the collagen‐GAG membranes in a dose‐dependent manner. To determine the relationship between extracellular matrix protein signaling cues and keratinocyte attachment, cells were seeded on protein‐conjugated collagen‐GAG membranes and a tetrazolium‐based colorimetric assay was used to quantify viable keratinocyte attachment. Our results indicate that keratinocyte attachment was significantly enhanced on the surfaces of collagen membranes that were conjugated with fibronectin and type IV collagen. These findings define a set of design parameters that will enhance keratinocyte binding efficiency on the surface of collagen membranes and ultimately improve the rate of epithelialization for dermal equivalents. © 2006 Wiley Periodicals, Inc. J Biomed Mater Res, 2007 |
doi_str_mv | 10.1002/jbm.a.30933 |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_68389497</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>68389497</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3673-837a99bdf79c8ef77d44ef460e46270bae2b541c68dd9e8702feef609e092f2c3</originalsourceid><addsrcrecordid>eNp9kEFv0zAUgC0EYmNw4o584oJSHNux4yOtoIC2gRBoR-vFed7SJc6wHdH--6W0sNtOfofvfXr-CHldskXJGH-_aYYFLAQzQjwhp2VV8UIaVT3dz9IUght1Ql6ktJlhxSr-nJyUmpWiVvKU4GoMm-kacjcGOnqK2xzBYd9PPUQ6QI7dlt7FMWMXEs0jbSBBT3sYugAUAvTjdaIYbiA4TPQW46wKo9tlpJAzuJsBQ35JnnnoE746vmfk16ePP1efi_Nv6y-rD-eFE0qLohYajGlar42r0WvdSoleKoZScc0aQN5UsnSqbluDtWbcI3rFDDLDPXfijLw9eOeLf0-Ysh26tP8NBBynZFUtaiONnsF3B9DFMaWI3t7FboC4syWz-6p2rmrB_q0602-O2qkZsH1gjxlnoDwAf7oed4-57NflxT9pcdjpUsbt_x2It3ZuoSt7dbm26x_L5fLi-5WtxD0nrZRD</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>68389497</pqid></control><display><type>article</type><title>Conjugation of extracellular matrix proteins to basal lamina analogs enhances keratinocyte attachment</title><source>Wiley</source><creator>Bush, Katie A. ; Downing, Brett R. ; Walsh, Sarah E. ; Pins, George D.</creator><creatorcontrib>Bush, Katie A. ; Downing, Brett R. ; Walsh, Sarah E. ; Pins, George D.</creatorcontrib><description>The dermal–epidermal junction of skin contains extracellular matrix proteins that are involved in initiating and controlling keratinocyte signaling events such as attachment, proliferation, and terminal differentiation. To characterize the relationship between extracellular matrix proteins and keratinocyte attachment, a biomimetic design approach was used to precisely tailor the surface of basal lamina analogs with biochemistries that emulate the native biochemical composition found at the dermal–epidermal junction. A high‐throughput screening device was developed by our laboratory that allows for the simultaneous investigation of the conjugation of individual extracellular matrix proteins (e.g. collagen type I, collagen type IV, laminin, or fibronectin) as well as their effect on keratinocyte attachment, on the surface of an implantable collagen membrane. Fluorescence microscopy coupled with quantitative digital image analyses indicated that the extracellular matrix proteins adsorbed to the collagen‐GAG membranes in a dose‐dependent manner. To determine the relationship between extracellular matrix protein signaling cues and keratinocyte attachment, cells were seeded on protein‐conjugated collagen‐GAG membranes and a tetrazolium‐based colorimetric assay was used to quantify viable keratinocyte attachment. Our results indicate that keratinocyte attachment was significantly enhanced on the surfaces of collagen membranes that were conjugated with fibronectin and type IV collagen. These findings define a set of design parameters that will enhance keratinocyte binding efficiency on the surface of collagen membranes and ultimately improve the rate of epithelialization for dermal equivalents. © 2006 Wiley Periodicals, Inc. J Biomed Mater Res, 2007</description><identifier>ISSN: 1549-3296</identifier><identifier>EISSN: 1552-4965</identifier><identifier>DOI: 10.1002/jbm.a.30933</identifier><identifier>PMID: 17013864</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>basal lamina ; Basement Membrane - chemistry ; Basement Membrane - metabolism ; bioengineered skin substitutes ; Biomimetic Materials - chemistry ; Collagen Type IV - chemistry ; Dermis ; Epidermis ; extracellular matrix ; Extracellular Matrix Proteins - chemistry ; Extracellular Matrix Proteins - metabolism ; Fibronectins - chemistry ; Humans ; keratinocytes ; Keratinocytes - cytology ; Keratinocytes - metabolism ; Prostheses and Implants ; Protein Binding ; Signal Transduction</subject><ispartof>Journal of biomedical materials research. Part A, 2007-02, Vol.80A (2), p.444-452</ispartof><rights>Copyright © 2006 Wiley Periodicals, Inc.</rights><rights>Copyright 2006 Wiley Periodicals, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3673-837a99bdf79c8ef77d44ef460e46270bae2b541c68dd9e8702feef609e092f2c3</citedby><cites>FETCH-LOGICAL-c3673-837a99bdf79c8ef77d44ef460e46270bae2b541c68dd9e8702feef609e092f2c3</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/17013864$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bush, Katie A.</creatorcontrib><creatorcontrib>Downing, Brett R.</creatorcontrib><creatorcontrib>Walsh, Sarah E.</creatorcontrib><creatorcontrib>Pins, George D.</creatorcontrib><title>Conjugation of extracellular matrix proteins to basal lamina analogs enhances keratinocyte attachment</title><title>Journal of biomedical materials research. Part A</title><addtitle>J. Biomed. Mater. Res</addtitle><description>The dermal–epidermal junction of skin contains extracellular matrix proteins that are involved in initiating and controlling keratinocyte signaling events such as attachment, proliferation, and terminal differentiation. To characterize the relationship between extracellular matrix proteins and keratinocyte attachment, a biomimetic design approach was used to precisely tailor the surface of basal lamina analogs with biochemistries that emulate the native biochemical composition found at the dermal–epidermal junction. A high‐throughput screening device was developed by our laboratory that allows for the simultaneous investigation of the conjugation of individual extracellular matrix proteins (e.g. collagen type I, collagen type IV, laminin, or fibronectin) as well as their effect on keratinocyte attachment, on the surface of an implantable collagen membrane. Fluorescence microscopy coupled with quantitative digital image analyses indicated that the extracellular matrix proteins adsorbed to the collagen‐GAG membranes in a dose‐dependent manner. To determine the relationship between extracellular matrix protein signaling cues and keratinocyte attachment, cells were seeded on protein‐conjugated collagen‐GAG membranes and a tetrazolium‐based colorimetric assay was used to quantify viable keratinocyte attachment. Our results indicate that keratinocyte attachment was significantly enhanced on the surfaces of collagen membranes that were conjugated with fibronectin and type IV collagen. These findings define a set of design parameters that will enhance keratinocyte binding efficiency on the surface of collagen membranes and ultimately improve the rate of epithelialization for dermal equivalents. © 2006 Wiley Periodicals, Inc. J Biomed Mater Res, 2007</description><subject>basal lamina</subject><subject>Basement Membrane - chemistry</subject><subject>Basement Membrane - metabolism</subject><subject>bioengineered skin substitutes</subject><subject>Biomimetic Materials - chemistry</subject><subject>Collagen Type IV - chemistry</subject><subject>Dermis</subject><subject>Epidermis</subject><subject>extracellular matrix</subject><subject>Extracellular Matrix Proteins - chemistry</subject><subject>Extracellular Matrix Proteins - metabolism</subject><subject>Fibronectins - chemistry</subject><subject>Humans</subject><subject>keratinocytes</subject><subject>Keratinocytes - cytology</subject><subject>Keratinocytes - metabolism</subject><subject>Prostheses and Implants</subject><subject>Protein Binding</subject><subject>Signal Transduction</subject><issn>1549-3296</issn><issn>1552-4965</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNp9kEFv0zAUgC0EYmNw4o584oJSHNux4yOtoIC2gRBoR-vFed7SJc6wHdH--6W0sNtOfofvfXr-CHldskXJGH-_aYYFLAQzQjwhp2VV8UIaVT3dz9IUght1Ql6ktJlhxSr-nJyUmpWiVvKU4GoMm-kacjcGOnqK2xzBYd9PPUQ6QI7dlt7FMWMXEs0jbSBBT3sYugAUAvTjdaIYbiA4TPQW46wKo9tlpJAzuJsBQ35JnnnoE746vmfk16ePP1efi_Nv6y-rD-eFE0qLohYajGlar42r0WvdSoleKoZScc0aQN5UsnSqbluDtWbcI3rFDDLDPXfijLw9eOeLf0-Ysh26tP8NBBynZFUtaiONnsF3B9DFMaWI3t7FboC4syWz-6p2rmrB_q0602-O2qkZsH1gjxlnoDwAf7oed4-57NflxT9pcdjpUsbt_x2It3ZuoSt7dbm26x_L5fLi-5WtxD0nrZRD</recordid><startdate>200702</startdate><enddate>200702</enddate><creator>Bush, Katie A.</creator><creator>Downing, Brett R.</creator><creator>Walsh, Sarah E.</creator><creator>Pins, George D.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>BSCLL</scope><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>7X8</scope></search><sort><creationdate>200702</creationdate><title>Conjugation of extracellular matrix proteins to basal lamina analogs enhances keratinocyte attachment</title><author>Bush, Katie A. ; Downing, Brett R. ; Walsh, Sarah E. ; Pins, George D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3673-837a99bdf79c8ef77d44ef460e46270bae2b541c68dd9e8702feef609e092f2c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>basal lamina</topic><topic>Basement Membrane - chemistry</topic><topic>Basement Membrane - metabolism</topic><topic>bioengineered skin substitutes</topic><topic>Biomimetic Materials - chemistry</topic><topic>Collagen Type IV - chemistry</topic><topic>Dermis</topic><topic>Epidermis</topic><topic>extracellular matrix</topic><topic>Extracellular Matrix Proteins - chemistry</topic><topic>Extracellular Matrix Proteins - metabolism</topic><topic>Fibronectins - chemistry</topic><topic>Humans</topic><topic>keratinocytes</topic><topic>Keratinocytes - cytology</topic><topic>Keratinocytes - metabolism</topic><topic>Prostheses and Implants</topic><topic>Protein Binding</topic><topic>Signal Transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bush, Katie A.</creatorcontrib><creatorcontrib>Downing, Brett R.</creatorcontrib><creatorcontrib>Walsh, Sarah E.</creatorcontrib><creatorcontrib>Pins, George D.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biomedical materials research. Part A</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bush, Katie A.</au><au>Downing, Brett R.</au><au>Walsh, Sarah E.</au><au>Pins, George D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Conjugation of extracellular matrix proteins to basal lamina analogs enhances keratinocyte attachment</atitle><jtitle>Journal of biomedical materials research. Part A</jtitle><addtitle>J. Biomed. Mater. Res</addtitle><date>2007-02</date><risdate>2007</risdate><volume>80A</volume><issue>2</issue><spage>444</spage><epage>452</epage><pages>444-452</pages><issn>1549-3296</issn><eissn>1552-4965</eissn><abstract>The dermal–epidermal junction of skin contains extracellular matrix proteins that are involved in initiating and controlling keratinocyte signaling events such as attachment, proliferation, and terminal differentiation. To characterize the relationship between extracellular matrix proteins and keratinocyte attachment, a biomimetic design approach was used to precisely tailor the surface of basal lamina analogs with biochemistries that emulate the native biochemical composition found at the dermal–epidermal junction. A high‐throughput screening device was developed by our laboratory that allows for the simultaneous investigation of the conjugation of individual extracellular matrix proteins (e.g. collagen type I, collagen type IV, laminin, or fibronectin) as well as their effect on keratinocyte attachment, on the surface of an implantable collagen membrane. Fluorescence microscopy coupled with quantitative digital image analyses indicated that the extracellular matrix proteins adsorbed to the collagen‐GAG membranes in a dose‐dependent manner. To determine the relationship between extracellular matrix protein signaling cues and keratinocyte attachment, cells were seeded on protein‐conjugated collagen‐GAG membranes and a tetrazolium‐based colorimetric assay was used to quantify viable keratinocyte attachment. Our results indicate that keratinocyte attachment was significantly enhanced on the surfaces of collagen membranes that were conjugated with fibronectin and type IV collagen. These findings define a set of design parameters that will enhance keratinocyte binding efficiency on the surface of collagen membranes and ultimately improve the rate of epithelialization for dermal equivalents. © 2006 Wiley Periodicals, Inc. J Biomed Mater Res, 2007</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>17013864</pmid><doi>10.1002/jbm.a.30933</doi><tpages>9</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1549-3296 |
ispartof | Journal of biomedical materials research. Part A, 2007-02, Vol.80A (2), p.444-452 |
issn | 1549-3296 1552-4965 |
language | eng |
recordid | cdi_proquest_miscellaneous_68389497 |
source | Wiley |
subjects | basal lamina Basement Membrane - chemistry Basement Membrane - metabolism bioengineered skin substitutes Biomimetic Materials - chemistry Collagen Type IV - chemistry Dermis Epidermis extracellular matrix Extracellular Matrix Proteins - chemistry Extracellular Matrix Proteins - metabolism Fibronectins - chemistry Humans keratinocytes Keratinocytes - cytology Keratinocytes - metabolism Prostheses and Implants Protein Binding Signal Transduction |
title | Conjugation of extracellular matrix proteins to basal lamina analogs enhances keratinocyte attachment |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T23%3A06%3A13IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Conjugation%20of%20extracellular%20matrix%20proteins%20to%20basal%20lamina%20analogs%20enhances%20keratinocyte%20attachment&rft.jtitle=Journal%20of%20biomedical%20materials%20research.%20Part%20A&rft.au=Bush,%20Katie%20A.&rft.date=2007-02&rft.volume=80A&rft.issue=2&rft.spage=444&rft.epage=452&rft.pages=444-452&rft.issn=1549-3296&rft.eissn=1552-4965&rft_id=info:doi/10.1002/jbm.a.30933&rft_dat=%3Cproquest_cross%3E68389497%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c3673-837a99bdf79c8ef77d44ef460e46270bae2b541c68dd9e8702feef609e092f2c3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=68389497&rft_id=info:pmid/17013864&rfr_iscdi=true |