High-affinity binding of the NC1 domain of collagen VII to laminin 5 and collagen IV
Anchoring functions of collagen VII depend on its ability to form homotypic fibrils and to bind to other macromolecules to form heterotypic complexes. Biosensor-based binding assays were employed to analyze the kinetics of the NC1 domain-mediated binding of collagen VII to laminin 5, collagen IV, an...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2006-05, Vol.343 (3), p.692-699 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Brittingham, Raymond Uitto, Jouni Fertala, Andrzej |
| description | Anchoring functions of collagen VII depend on its ability to form homotypic fibrils and to bind to other macromolecules to form heterotypic complexes. Biosensor-based binding assays were employed to analyze the kinetics of the NC1 domain-mediated binding of collagen VII to laminin 5, collagen IV, and collagen I. We showed that collagen VII interacts with laminin 5 and collagen IV with a
K
d value of 10
−9
M. In contrast, the NC1-mediated binding to collagen I was weak with a
K
d value of 10
−6
M. Binding assays also showed that the NC1 domain utilizes the same region to bind to both laminin 5 and collagen IV. We postulate that the ability of the NC1 domains to bind with high affinities to laminin 5 and collagen IV facilitates stabilization of the structure of the basement membrane itself and that the NC1-collagen I interaction may be less important for stabilization of the dermal–epidermal junction. |
| doi_str_mv | 10.1016/j.bbrc.2006.03.034 |
| format | Article |
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K
d value of 10
−9
M. In contrast, the NC1-mediated binding to collagen I was weak with a
K
d value of 10
−6
M. Binding assays also showed that the NC1 domain utilizes the same region to bind to both laminin 5 and collagen IV. We postulate that the ability of the NC1 domains to bind with high affinities to laminin 5 and collagen IV facilitates stabilization of the structure of the basement membrane itself and that the NC1-collagen I interaction may be less important for stabilization of the dermal–epidermal junction.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2006.03.034</identifier><identifier>PMID: 16563355</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Binding Sites ; Biosensing Techniques ; Biosensor ; Cell Adhesion Molecules - metabolism ; Collagen IV ; Collagen mutations ; Collagen Type IV - metabolism ; Collagen Type VII - chemistry ; Collagen Type VII - metabolism ; Collagen Type VII - ultrastructure ; Collagen VII ; Epidermolysis bullosa ; Extracellular matrix of connective tissue ; Humans ; Kalinin ; Laminin 5 ; Protein Structure, Tertiary</subject><ispartof>Biochemical and biophysical research communications, 2006-05, Vol.343 (3), p.692-699</ispartof><rights>2006 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c464t-56d354c1fd9664d688b353a480882f692f9005ccdc6b44f9b13667fe139162f73</citedby><cites>FETCH-LOGICAL-c464t-56d354c1fd9664d688b353a480882f692f9005ccdc6b44f9b13667fe139162f73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2006.03.034$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16563355$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brittingham, Raymond</creatorcontrib><creatorcontrib>Uitto, Jouni</creatorcontrib><creatorcontrib>Fertala, Andrzej</creatorcontrib><title>High-affinity binding of the NC1 domain of collagen VII to laminin 5 and collagen IV</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Anchoring functions of collagen VII depend on its ability to form homotypic fibrils and to bind to other macromolecules to form heterotypic complexes. Biosensor-based binding assays were employed to analyze the kinetics of the NC1 domain-mediated binding of collagen VII to laminin 5, collagen IV, and collagen I. We showed that collagen VII interacts with laminin 5 and collagen IV with a
K
d value of 10
−9
M. In contrast, the NC1-mediated binding to collagen I was weak with a
K
d value of 10
−6
M. Binding assays also showed that the NC1 domain utilizes the same region to bind to both laminin 5 and collagen IV. We postulate that the ability of the NC1 domains to bind with high affinities to laminin 5 and collagen IV facilitates stabilization of the structure of the basement membrane itself and that the NC1-collagen I interaction may be less important for stabilization of the dermal–epidermal junction.</description><subject>Binding Sites</subject><subject>Biosensing Techniques</subject><subject>Biosensor</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Collagen IV</subject><subject>Collagen mutations</subject><subject>Collagen Type IV - metabolism</subject><subject>Collagen Type VII - chemistry</subject><subject>Collagen Type VII - metabolism</subject><subject>Collagen Type VII - ultrastructure</subject><subject>Collagen VII</subject><subject>Epidermolysis bullosa</subject><subject>Extracellular matrix of connective tissue</subject><subject>Humans</subject><subject>Kalinin</subject><subject>Laminin 5</subject><subject>Protein Structure, Tertiary</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9UMtKw0AUHUSxtfoDLmRW7hJnMo9OwI0UtYGim1rcDck82inJpGZSoX_vhBa6Ew5cuOfBvQeAe4xSjDB_2qZV1ak0Q4iniETQCzDGKEdJhhG9BGMUmSTL8fcI3ISwRQhjyvNrMMKccUIYG4Pl3K03SWmt864_wMp57fwathb2GwM_ZhjqtimdHzaqretybTxcFQXsW1iXTXR5yGDp9ZktVrfgypZ1MHenOQFfb6_L2TxZfL4Xs5dFoiinfcK4JowqbHXOOdVciIowUlKBhMgszzObI8SU0opXlNq8woTzqTWY5Jhndkom4PGYu-van70JvWxcUCbe4U27D5JPBWGZEFGYHYWqa0PojJW7zjVld5AYyaFLuZVDl3LoUiISQaPp4ZS-rxqjz5ZTeVHwfBSY-OOvM50MyhmvjHadUb3Urfsv_w8y1IJv</recordid><startdate>20060512</startdate><enddate>20060512</enddate><creator>Brittingham, Raymond</creator><creator>Uitto, Jouni</creator><creator>Fertala, Andrzej</creator><general>Elsevier 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>7X8</scope></search><sort><creationdate>20060512</creationdate><title>High-affinity binding of the NC1 domain of collagen VII to laminin 5 and collagen IV</title><author>Brittingham, Raymond ; Uitto, Jouni ; Fertala, Andrzej</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c464t-56d354c1fd9664d688b353a480882f692f9005ccdc6b44f9b13667fe139162f73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Binding Sites</topic><topic>Biosensing Techniques</topic><topic>Biosensor</topic><topic>Cell Adhesion Molecules - metabolism</topic><topic>Collagen IV</topic><topic>Collagen mutations</topic><topic>Collagen Type IV - metabolism</topic><topic>Collagen Type VII - chemistry</topic><topic>Collagen Type VII - metabolism</topic><topic>Collagen Type VII - ultrastructure</topic><topic>Collagen VII</topic><topic>Epidermolysis bullosa</topic><topic>Extracellular matrix of connective tissue</topic><topic>Humans</topic><topic>Kalinin</topic><topic>Laminin 5</topic><topic>Protein Structure, Tertiary</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brittingham, Raymond</creatorcontrib><creatorcontrib>Uitto, Jouni</creatorcontrib><creatorcontrib>Fertala, Andrzej</creatorcontrib><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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brittingham, Raymond</au><au>Uitto, Jouni</au><au>Fertala, Andrzej</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>High-affinity binding of the NC1 domain of collagen VII to laminin 5 and collagen IV</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2006-05-12</date><risdate>2006</risdate><volume>343</volume><issue>3</issue><spage>692</spage><epage>699</epage><pages>692-699</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Anchoring functions of collagen VII depend on its ability to form homotypic fibrils and to bind to other macromolecules to form heterotypic complexes. Biosensor-based binding assays were employed to analyze the kinetics of the NC1 domain-mediated binding of collagen VII to laminin 5, collagen IV, and collagen I. We showed that collagen VII interacts with laminin 5 and collagen IV with a
K
d value of 10
−9
M. In contrast, the NC1-mediated binding to collagen I was weak with a
K
d value of 10
−6
M. Binding assays also showed that the NC1 domain utilizes the same region to bind to both laminin 5 and collagen IV. We postulate that the ability of the NC1 domains to bind with high affinities to laminin 5 and collagen IV facilitates stabilization of the structure of the basement membrane itself and that the NC1-collagen I interaction may be less important for stabilization of the dermal–epidermal junction.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16563355</pmid><doi>10.1016/j.bbrc.2006.03.034</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 2006-05, Vol.343 (3), p.692-699 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Binding Sites Biosensing Techniques Biosensor Cell Adhesion Molecules - metabolism Collagen IV Collagen mutations Collagen Type IV - metabolism Collagen Type VII - chemistry Collagen Type VII - metabolism Collagen Type VII - ultrastructure Collagen VII Epidermolysis bullosa Extracellular matrix of connective tissue Humans Kalinin Laminin 5 Protein Structure, Tertiary |
| title | High-affinity binding of the NC1 domain of collagen VII to laminin 5 and collagen IV |
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