The integrin specificity of human recombinant osteopontin
The ability of full-length human recombinant osteopontin (OPN) to support the adhesion of various α V integrin-expressing cell lines was determined in order to characterize its integrin selectivity. The identity of this protein was assessed by cDNA sequence and mass spectroscopic analysis, and confi...
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| Veröffentlicht in: | Biochemical pharmacology 1999-11, Vol.58 (10), p.1567-1578 |
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| creator | Caltabiano, Stephen Hum, Wah-Tung Attwell, Gwilym J. Gralnick, David N. Budman, Lori J. Cannistraci, AnnaMarie Bex, Frederick J. |
| description | The ability of full-length human recombinant osteopontin (OPN) to support the adhesion of various α
V integrin-expressing cell lines was determined in order to characterize its integrin selectivity. The identity of this protein was assessed by cDNA sequence and mass spectroscopic analysis, and confirmed as full-length OPN. Neither the human embryonic kidney 293 cell line, which expresses the α
Vβ
1 integrin, nor the human colonic adenocarcinoma HT-29 cell line, which expresses the α
Vβ
5 integrin, were able to adhere to OPN; both of these cell lines are deficient in the β
3 subunit. In contrast, an α
Vβ
3 integrin-expressing cell line, SK-MEL-24, was able to adhere to OPN in an arginine-glycine-aspartic acid dependent manner. In addition, this OPN-mediated cellular adhesion was completely blocked with an anti-α
Vβ
3 integrin antibody (LM609), confirming that only the α
Vβ
3 integrin mediated this cellular adhesion. These data demonstrate that, at least among the α
V integrins, only the α
Vβ
3 is able to support cellular adhesion to osteopontin. This finding may have implications for the design of therapeutics targeting OPN–integrin interactions. |
| doi_str_mv | 10.1016/S0006-2952(99)00251-8 |
| format | Article |
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V integrin-expressing cell lines was determined in order to characterize its integrin selectivity. The identity of this protein was assessed by cDNA sequence and mass spectroscopic analysis, and confirmed as full-length OPN. Neither the human embryonic kidney 293 cell line, which expresses the α
Vβ
1 integrin, nor the human colonic adenocarcinoma HT-29 cell line, which expresses the α
Vβ
5 integrin, were able to adhere to OPN; both of these cell lines are deficient in the β
3 subunit. In contrast, an α
Vβ
3 integrin-expressing cell line, SK-MEL-24, was able to adhere to OPN in an arginine-glycine-aspartic acid dependent manner. In addition, this OPN-mediated cellular adhesion was completely blocked with an anti-α
Vβ
3 integrin antibody (LM609), confirming that only the α
Vβ
3 integrin mediated this cellular adhesion. These data demonstrate that, at least among the α
V integrins, only the α
Vβ
3 is able to support cellular adhesion to osteopontin. This finding may have implications for the design of therapeutics targeting OPN–integrin interactions.</description><identifier>ISSN: 0006-2952</identifier><identifier>EISSN: 1873-2968</identifier><identifier>DOI: 10.1016/S0006-2952(99)00251-8</identifier><identifier>PMID: 10535747</identifier><identifier>CODEN: BCPCA6</identifier><language>eng</language><publisher>New York, NY: Elsevier Inc</publisher><subject>Biological and medical sciences ; Cell Adhesion - drug effects ; Cell interactions, adhesion ; Cell Line ; cellular adhesion ; Extracellular Matrix - physiology ; Fundamental and applied biological sciences. Psychology ; HT29 Cells ; Humans ; Molecular and cellular biology ; Oligopeptides - physiology ; Osteopontin ; Protein Conformation ; Receptors, Vitronectin - biosynthesis ; Receptors, Vitronectin - metabolism ; Recombinant Proteins - metabolism ; Recombinant Proteins - pharmacology ; RGD ; Sialoglycoproteins - metabolism ; Sialoglycoproteins - pharmacology ; Space life sciences ; Tumor Cells, Cultured ; α Vβ 1 ; α Vβ 3 ; α Vβ 5</subject><ispartof>Biochemical pharmacology, 1999-11, Vol.58 (10), p.1567-1578</ispartof><rights>1999 Elsevier Science Inc.</rights><rights>2000 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c456t-75573c9fc593ee55489bd64d6e1f6442697ab75396c4637a94e7b6a7212229d73</citedby><cites>FETCH-LOGICAL-c456t-75573c9fc593ee55489bd64d6e1f6442697ab75396c4637a94e7b6a7212229d73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006295299002518$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1178735$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10535747$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Caltabiano, Stephen</creatorcontrib><creatorcontrib>Hum, Wah-Tung</creatorcontrib><creatorcontrib>Attwell, Gwilym J.</creatorcontrib><creatorcontrib>Gralnick, David N.</creatorcontrib><creatorcontrib>Budman, Lori J.</creatorcontrib><creatorcontrib>Cannistraci, AnnaMarie</creatorcontrib><creatorcontrib>Bex, Frederick J.</creatorcontrib><title>The integrin specificity of human recombinant osteopontin</title><title>Biochemical pharmacology</title><addtitle>Biochem Pharmacol</addtitle><description>The ability of full-length human recombinant osteopontin (OPN) to support the adhesion of various α
V integrin-expressing cell lines was determined in order to characterize its integrin selectivity. The identity of this protein was assessed by cDNA sequence and mass spectroscopic analysis, and confirmed as full-length OPN. Neither the human embryonic kidney 293 cell line, which expresses the α
Vβ
1 integrin, nor the human colonic adenocarcinoma HT-29 cell line, which expresses the α
Vβ
5 integrin, were able to adhere to OPN; both of these cell lines are deficient in the β
3 subunit. In contrast, an α
Vβ
3 integrin-expressing cell line, SK-MEL-24, was able to adhere to OPN in an arginine-glycine-aspartic acid dependent manner. In addition, this OPN-mediated cellular adhesion was completely blocked with an anti-α
Vβ
3 integrin antibody (LM609), confirming that only the α
Vβ
3 integrin mediated this cellular adhesion. These data demonstrate that, at least among the α
V integrins, only the α
Vβ
3 is able to support cellular adhesion to osteopontin. This finding may have implications for the design of therapeutics targeting OPN–integrin interactions.</description><subject>Biological and medical sciences</subject><subject>Cell Adhesion - drug effects</subject><subject>Cell interactions, adhesion</subject><subject>Cell Line</subject><subject>cellular adhesion</subject><subject>Extracellular Matrix - physiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HT29 Cells</subject><subject>Humans</subject><subject>Molecular and cellular biology</subject><subject>Oligopeptides - physiology</subject><subject>Osteopontin</subject><subject>Protein Conformation</subject><subject>Receptors, Vitronectin - biosynthesis</subject><subject>Receptors, Vitronectin - metabolism</subject><subject>Recombinant Proteins - metabolism</subject><subject>Recombinant Proteins - pharmacology</subject><subject>RGD</subject><subject>Sialoglycoproteins - metabolism</subject><subject>Sialoglycoproteins - pharmacology</subject><subject>Space life sciences</subject><subject>Tumor Cells, Cultured</subject><subject>α Vβ 1</subject><subject>α Vβ 3</subject><subject>α Vβ 5</subject><issn>0006-2952</issn><issn>1873-2968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LAzEQhoMotlZ_grIHET2sJtl8bE4ixS8oeLCeQzY7ayPdpCZbof_e7QfqzdMww_PODA9CpwRfE0zEzSvGWORUcXqp1BXGlJO83ENDUsqiH4tyHw1_kAE6Sulj3ZaCHKIBwbzgkskhUtMZZM538B6dz9ICrGucdd0qC002W7bGZxFsaCvnje-ykDoIi-A754_RQWPmCU52dYTeHu6n46d88vL4PL6b5JZx0eWSc1lY1ViuCgDOWamqWrBaAGkEY1QoaSrJCyUsE4U0ioGshJGUUEpVLYsRutjuXcTwuYTU6dYlC_O58RCWSQtFCROY9SDfgjaGlCI0ehFda-JKE6zXzvTGmV4L0UrpjTNd9rmz3YFl1UL9J7WV1APnO8Aka-ZNNN669MsR2TvnPXa7xaC38eUg6mQdeAu16xV2ug7un0--Aa3mhwc</recordid><startdate>19991115</startdate><enddate>19991115</enddate><creator>Caltabiano, Stephen</creator><creator>Hum, Wah-Tung</creator><creator>Attwell, Gwilym J.</creator><creator>Gralnick, David N.</creator><creator>Budman, Lori J.</creator><creator>Cannistraci, AnnaMarie</creator><creator>Bex, Frederick J.</creator><general>Elsevier Inc</general><general>Elsevier Science</general><scope>IQODW</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>19991115</creationdate><title>The integrin specificity of human recombinant osteopontin</title><author>Caltabiano, Stephen ; Hum, Wah-Tung ; Attwell, Gwilym J. ; Gralnick, David N. ; Budman, Lori J. ; Cannistraci, AnnaMarie ; Bex, Frederick J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-75573c9fc593ee55489bd64d6e1f6442697ab75396c4637a94e7b6a7212229d73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Biological and medical sciences</topic><topic>Cell Adhesion - drug effects</topic><topic>Cell interactions, adhesion</topic><topic>Cell Line</topic><topic>cellular adhesion</topic><topic>Extracellular Matrix - physiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>HT29 Cells</topic><topic>Humans</topic><topic>Molecular and cellular biology</topic><topic>Oligopeptides - physiology</topic><topic>Osteopontin</topic><topic>Protein Conformation</topic><topic>Receptors, Vitronectin - biosynthesis</topic><topic>Receptors, Vitronectin - metabolism</topic><topic>Recombinant Proteins - metabolism</topic><topic>Recombinant Proteins - pharmacology</topic><topic>RGD</topic><topic>Sialoglycoproteins - metabolism</topic><topic>Sialoglycoproteins - pharmacology</topic><topic>Space life sciences</topic><topic>Tumor Cells, Cultured</topic><topic>α Vβ 1</topic><topic>α Vβ 3</topic><topic>α Vβ 5</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Caltabiano, Stephen</creatorcontrib><creatorcontrib>Hum, Wah-Tung</creatorcontrib><creatorcontrib>Attwell, Gwilym J.</creatorcontrib><creatorcontrib>Gralnick, David N.</creatorcontrib><creatorcontrib>Budman, Lori J.</creatorcontrib><creatorcontrib>Cannistraci, AnnaMarie</creatorcontrib><creatorcontrib>Bex, Frederick J.</creatorcontrib><collection>Pascal-Francis</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>Biochemical pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Caltabiano, Stephen</au><au>Hum, Wah-Tung</au><au>Attwell, Gwilym J.</au><au>Gralnick, David N.</au><au>Budman, Lori J.</au><au>Cannistraci, AnnaMarie</au><au>Bex, Frederick J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The integrin specificity of human recombinant osteopontin</atitle><jtitle>Biochemical pharmacology</jtitle><addtitle>Biochem Pharmacol</addtitle><date>1999-11-15</date><risdate>1999</risdate><volume>58</volume><issue>10</issue><spage>1567</spage><epage>1578</epage><pages>1567-1578</pages><issn>0006-2952</issn><eissn>1873-2968</eissn><coden>BCPCA6</coden><abstract>The ability of full-length human recombinant osteopontin (OPN) to support the adhesion of various α
V integrin-expressing cell lines was determined in order to characterize its integrin selectivity. The identity of this protein was assessed by cDNA sequence and mass spectroscopic analysis, and confirmed as full-length OPN. Neither the human embryonic kidney 293 cell line, which expresses the α
Vβ
1 integrin, nor the human colonic adenocarcinoma HT-29 cell line, which expresses the α
Vβ
5 integrin, were able to adhere to OPN; both of these cell lines are deficient in the β
3 subunit. In contrast, an α
Vβ
3 integrin-expressing cell line, SK-MEL-24, was able to adhere to OPN in an arginine-glycine-aspartic acid dependent manner. In addition, this OPN-mediated cellular adhesion was completely blocked with an anti-α
Vβ
3 integrin antibody (LM609), confirming that only the α
Vβ
3 integrin mediated this cellular adhesion. These data demonstrate that, at least among the α
V integrins, only the α
Vβ
3 is able to support cellular adhesion to osteopontin. This finding may have implications for the design of therapeutics targeting OPN–integrin interactions.</abstract><cop>New York, NY</cop><pub>Elsevier Inc</pub><pmid>10535747</pmid><doi>10.1016/S0006-2952(99)00251-8</doi><tpages>12</tpages></addata></record> |
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| subjects | Biological and medical sciences Cell Adhesion - drug effects Cell interactions, adhesion Cell Line cellular adhesion Extracellular Matrix - physiology Fundamental and applied biological sciences. Psychology HT29 Cells Humans Molecular and cellular biology Oligopeptides - physiology Osteopontin Protein Conformation Receptors, Vitronectin - biosynthesis Receptors, Vitronectin - metabolism Recombinant Proteins - metabolism Recombinant Proteins - pharmacology RGD Sialoglycoproteins - metabolism Sialoglycoproteins - pharmacology Space life sciences Tumor Cells, Cultured α Vβ 1 α Vβ 3 α Vβ 5 |
| title | The integrin specificity of human recombinant osteopontin |
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