{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/20834"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/20834","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"H36-alpha7 is a novel integrin alpha chain that is developmentally regulated during skeletal myogenesis","abstract":"H36 is a 120,000 Da membrane glycoprotein that is expressed during the differentiation of skeletal muscle. H36 cDNA clones were isolated from a lambda UniZapXR rat myotube cDNA library and sequenced. The deduced amino acid sequence demonstrates that H36 is a novel integrin alpha chain that shares extensive homology with other alpha integrins that includes: (a) the GFFKR sequence found in all alpha integrins; (b) a single membrane spanning region; (c) conservation of 18 of 22 cysteines; and (d) a protease cleavage site found in the non-I region integrin alpha chains. The cytoplasmic domain of H36 is unique and additional regions of nonhomology further indicate H36 is distinct from all other alpha chains. In keeping with current nomenclature I designate this alpha chain $\\alpha$7. Northern blots demonstrate that expression of H36-$\\alpha$7 mRNA is regulated both early in the development of the myogenic lineage and later, during terminal differentiation. Detection of H36-$\\alpha$7 mRNA coincides with conversion of H36$\\sp-$ myogenic precursor cells to H36$\\sp+$ cells. H36-$\\alpha$7 mRNA is present in replicating myoblasts: expression increases upon terminal differentiation and is markedly reduced in developmentally defective myoblasts. In addition, H36-$\\alpha$7 mRNA is not detected in C3H10T1/2 cells. It is in myotubes derived from myoblasts obtained by treatment of 10T1/2 cells with azacytidine or transfection with MRF4. Immunoblots and immunofluorescence demonstrate that the H36-$\\alpha$7 chain is associated with integrin $\\beta$1. Affinity chromatography demonstrates that H36-$\\alpha$7$\\beta$1 selectively binds to laminin. The expression of H36-$\\alpha$7 on secondary myoblasts during the development of the limb in vivo corresponds with the appearance of laminin in the limb, with the responsiveness of secondary myoblast proliferation to laminin, and with the onset of increased muscle mass, suggesting that H36-$\\alpha$7 modulates this stage in limb development. I conclude that H36-$\\alpha$7 is a novel alpha integrin laminin binding protein whose expression is developmentally regulated during skeletal myogenesis.","abstract_html":"H36 is a 120,000 Da membrane glycoprotein that is expressed during the differentiation of skeletal muscle. H36 cDNA clones were isolated from a lambda UniZapXR rat myotube cDNA library and sequenced. The deduced amino acid sequence demonstrates that H36 is a novel integrin alpha chain that shares extensive homology with other alpha integrins that includes: (a) the GFFKR sequence found in all alpha integrins; (b) a single membrane spanning region; (c) conservation of 18 of 22 cysteines; and (d) a protease cleavage site found in the non-I region integrin alpha chains. The cytoplasmic domain of H36 is unique and additional regions of nonhomology further indicate H36 is distinct from all other alpha chains. In keeping with current nomenclature I designate this alpha chain <span class=\"etd-inline-math\">&alpha;</span>7. Northern blots demonstrate that expression of H36-<span class=\"etd-inline-math\">&alpha;</span>7 mRNA is regulated both early in the development of the myogenic lineage and later, during terminal differentiation. Detection of H36-<span class=\"etd-inline-math\">&alpha;</span>7 mRNA coincides with conversion of H36$\\sp-$ myogenic precursor cells to H36$\\sp+$ cells. H36-<span class=\"etd-inline-math\">&alpha;</span>7 mRNA is present in replicating myoblasts: expression increases upon terminal differentiation and is markedly reduced in developmentally defective myoblasts. In addition, H36-<span class=\"etd-inline-math\">&alpha;</span>7 mRNA is not detected in C3H10T1/2 cells. It is in myotubes derived from myoblasts obtained by treatment of 10T1/2 cells with azacytidine or transfection with MRF4. Immunoblots and immunofluorescence demonstrate that the H36-<span class=\"etd-inline-math\">&alpha;</span>7 chain is associated with integrin <span class=\"etd-inline-math\">&beta;</span>1. Affinity chromatography demonstrates that H36-<span class=\"etd-inline-math\">&alpha;</span>7<span class=\"etd-inline-math\">&beta;</span>1 selectively binds to laminin. The expression of H36-<span class=\"etd-inline-math\">&alpha;</span>7 on secondary myoblasts during the development of the limb in vivo corresponds with the appearance of laminin in the limb, with the responsiveness of secondary myoblast proliferation to laminin, and with the onset of increased muscle mass, suggesting that H36-<span class=\"etd-inline-math\">&alpha;</span>7 modulates this stage in limb development. I conclude that H36-<span class=\"etd-inline-math\">&alpha;</span>7 is a novel alpha integrin laminin binding protein whose expression is developmentally regulated during skeletal myogenesis.","abstract_has_math":true,"creators":["Song, Woo Keun"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Microbiology","degree_department":null,"school":null,"contributors":["Kaufman, Stephen J."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-05-07T12:50:40Z","date_published":"2011-05-07T12:50:40Z","updated_at":"2026-07-22T22:25:16Z","subjects":["Biology, Molecular","Biology, Genetics","Biology, Cell"],"languages":["eng"],"rights":["Copyright 1992 Song, Woo Keun"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9305701","(UMI)AAI9305701"],"render_values":[{"text":"AAI9305701","href":null,"code":true},{"text":"(UMI)AAI9305701","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/20834","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Kaufman, Stephen J."]},{"key":"dc:creator","label":"Author","values":["Song, Woo Keun"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-05-07T12:50:40Z","10000-01-01","1992"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Microbiology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biology, Molecular","Biology, Genetics","Biology, Cell"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 1992 Song, Woo Keun"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9305701","(UMI)AAI9305701","http://hdl.handle.net/2142/20834"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["H36 is a 120,000 Da membrane glycoprotein that is expressed during the differentiation of skeletal muscle. H36 cDNA clones were isolated from a lambda UniZapXR rat myotube cDNA library and sequenced. The deduced amino acid sequence demonstrates that H36 is a novel integrin alpha chain that shares extensive homology with other alpha integrins that includes: (a) the GFFKR sequence found in all alpha integrins; (b) a single membrane spanning region; (c) conservation of 18 of 22 cysteines; and (d) a protease cleavage site found in the non-I region integrin alpha chains. The cytoplasmic domain of H36 is unique and additional regions of nonhomology further indicate H36 is distinct from all other alpha chains. In keeping with current nomenclature I designate this alpha chain $\\alpha$7. Northern blots demonstrate that expression of H36-$\\alpha$7 mRNA is regulated both early in the development of the myogenic lineage and later, during terminal differentiation. Detection of H36-$\\alpha$7 mRNA coincides with conversion of H36$\\sp-$ myogenic precursor cells to H36$\\sp+$ cells. H36-$\\alpha$7 mRNA is present in replicating myoblasts: expression increases upon terminal differentiation and is markedly reduced in developmentally defective myoblasts. In addition, H36-$\\alpha$7 mRNA is not detected in C3H10T1/2 cells. It is in myotubes derived from myoblasts obtained by treatment of 10T1/2 cells with azacytidine or transfection with MRF4. Immunoblots and immunofluorescence demonstrate that the H36-$\\alpha$7 chain is associated with integrin $\\beta$1. Affinity chromatography demonstrates that H36-$\\alpha$7$\\beta$1 selectively binds to laminin. The expression of H36-$\\alpha$7 on secondary myoblasts during the development of the limb in vivo corresponds with the appearance of laminin in the limb, with the responsiveness of secondary myoblast proliferation to laminin, and with the onset of increased muscle mass, suggesting that H36-$\\alpha$7 modulates this stage in limb development. I conclude that H36-$\\alpha$7 is a novel alpha integrin laminin binding protein whose expression is developmentally regulated during skeletal myogenesis.","Made available in DSpace on 2011-05-07T12:50:40Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9305701.pdf: 5034250 bytes, checksum: 3a4649e5c68788f069367b346dfa93c5 (MD5) Previous issue date: 1992","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:46:37Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:20:55-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only"]},{"key":"dc:title","label":"Title","values":["H36-alpha7 is a novel integrin alpha chain that is developmentally regulated during skeletal myogenesis"]}]}],"canonical_facts":{"dc:contributor":["Kaufman, Stephen J."],"dc:creator":["Song, Woo Keun"],"dc:date":["2011-05-07T12:50:40Z","10000-01-01","1992"],"dc:description":["H36 is a 120,000 Da membrane glycoprotein that is expressed during the differentiation of skeletal muscle. H36 cDNA clones were isolated from a lambda UniZapXR rat myotube cDNA library and sequenced. The deduced amino acid sequence demonstrates that H36 is a novel integrin alpha chain that shares extensive homology with other alpha integrins that includes: (a) the GFFKR sequence found in all alpha integrins; (b) a single membrane spanning region; (c) conservation of 18 of 22 cysteines; and (d) a protease cleavage site found in the non-I region integrin alpha chains. The cytoplasmic domain of H36 is unique and additional regions of nonhomology further indicate H36 is distinct from all other alpha chains. In keeping with current nomenclature I designate this alpha chain $\\alpha$7. Northern blots demonstrate that expression of H36-$\\alpha$7 mRNA is regulated both early in the development of the myogenic lineage and later, during terminal differentiation. Detection of H36-$\\alpha$7 mRNA coincides with conversion of H36$\\sp-$ myogenic precursor cells to H36$\\sp+$ cells. H36-$\\alpha$7 mRNA is present in replicating myoblasts: expression increases upon terminal differentiation and is markedly reduced in developmentally defective myoblasts. In addition, H36-$\\alpha$7 mRNA is not detected in C3H10T1/2 cells. It is in myotubes derived from myoblasts obtained by treatment of 10T1/2 cells with azacytidine or transfection with MRF4. Immunoblots and immunofluorescence demonstrate that the H36-$\\alpha$7 chain is associated with integrin $\\beta$1. Affinity chromatography demonstrates that H36-$\\alpha$7$\\beta$1 selectively binds to laminin. The expression of H36-$\\alpha$7 on secondary myoblasts during the development of the limb in vivo corresponds with the appearance of laminin in the limb, with the responsiveness of secondary myoblast proliferation to laminin, and with the onset of increased muscle mass, suggesting that H36-$\\alpha$7 modulates this stage in limb development. I conclude that H36-$\\alpha$7 is a novel alpha integrin laminin binding protein whose expression is developmentally regulated during skeletal myogenesis.","Made available in DSpace on 2011-05-07T12:50:40Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9305701.pdf: 5034250 bytes, checksum: 3a4649e5c68788f069367b346dfa93c5 (MD5) Previous issue date: 1992","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:46:37Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:20:55-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only"],"dc:identifier":["AAI9305701","(UMI)AAI9305701","http://hdl.handle.net/2142/20834"],"dc:language":["eng"],"dc:rights":["Copyright 1992 Song, Woo Keun"],"dc:subject":["Biology, Molecular","Biology, Genetics","Biology, Cell"],"dc:title":["H36-alpha7 is a novel integrin alpha chain that is developmentally regulated during skeletal myogenesis"],"dc:type":["text"],"thesis:degree_discipline":["Microbiology"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:25:16Z"}