Kinetic characterization of a membrane-specific ATPase from rat osseous plate and its possible significance on endochondral ossification
Autor(a) principal: | |
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Data de Publicação: | 1998 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/S0005-2736(97)00174-0 http://hdl.handle.net/11449/3973 |
Resumo: | Treatment with phosphatidylinositol-specific phospholipase C of rat osseous plate membranes released up to 90-95% of alkaline phosphatase, but a specific ATPase activity (optimum pH = 7.5) remained bound to the membrane. The hydrolysis of ATP by this ATPase was negligible in the absence of magnesium or calcium ions. However, at millimolar concentrations of magnesium and calcium ions, the membrane-specific ATPase activity increased to about 560-600 U/mg, exhibiting two classes of ATP-hydrolysing sites, and site-site interactions. GTP, UTP, ITP, and CTP were also hydrolyzed by the membrane-specific ATPase. Oligomycin, ouabain, bafilomycin A(1), thapsigargin, omeprazole, ethacrynic acid and EDTA slightly affected membrane-specific ATPase activity while vanadate produced a 18% inhibition. The membrane-specific ATPase activity was insensitive to theophylline, but was inhibited 40% by levamisole. These data suggested that the membrane-specific ATPase activity present in osseous plate membranes, and alkaline phosphatase, were different proteins. (C) 1998 Elsevier B.V. B.V. |
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Kinetic characterization of a membrane-specific ATPase from rat osseous plate and its possible significance on endochondral ossificationATPaseOsseous platephosphatidylinositol-specific phospholipase Cendochondral ossificationAlkaline phosphataseTreatment with phosphatidylinositol-specific phospholipase C of rat osseous plate membranes released up to 90-95% of alkaline phosphatase, but a specific ATPase activity (optimum pH = 7.5) remained bound to the membrane. The hydrolysis of ATP by this ATPase was negligible in the absence of magnesium or calcium ions. However, at millimolar concentrations of magnesium and calcium ions, the membrane-specific ATPase activity increased to about 560-600 U/mg, exhibiting two classes of ATP-hydrolysing sites, and site-site interactions. GTP, UTP, ITP, and CTP were also hydrolyzed by the membrane-specific ATPase. Oligomycin, ouabain, bafilomycin A(1), thapsigargin, omeprazole, ethacrynic acid and EDTA slightly affected membrane-specific ATPase activity while vanadate produced a 18% inhibition. The membrane-specific ATPase activity was insensitive to theophylline, but was inhibited 40% by levamisole. These data suggested that the membrane-specific ATPase activity present in osseous plate membranes, and alkaline phosphatase, were different proteins. (C) 1998 Elsevier B.V. B.V.USP, Fac Filosofia Ciências & Letras Ribeirao Pret, Dept Quim, BR-14040901 Ribeirao Preto, SP, BrazilUNESP, Fac Ciências Agr & Vet, Dept Tecnol, Jaboticabal, SP, BrazilUNESP, Fac Ciências Agr & Vet, Dept Tecnol, Jaboticabal, SP, BrazilElsevier B.V.Universidade de São Paulo (USP)Universidade Estadual Paulista (Unesp)Pizauro, J. M.Demenis, M. A.Ciancaglini, P.Leone, F. A.2014-05-20T13:17:32Z2014-05-20T13:17:32Z1998-01-05info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article108-114application/pdfhttp://dx.doi.org/10.1016/S0005-2736(97)00174-0Biochimica Et Biophysica Acta-biomembranes. Amsterdam: Elsevier B.V., v. 1368, n. 1, p. 108-114, 1998.0005-2736http://hdl.handle.net/11449/397310.1016/S0005-2736(97)00174-0WOS:000071507700012WOS000071507700012.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBiochimica et Biophysica Acta: Biomembranes3.4381,495info:eu-repo/semantics/openAccess2023-12-07T06:20:38Zoai:repositorio.unesp.br:11449/3973Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-12-07T06:20:38Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Kinetic characterization of a membrane-specific ATPase from rat osseous plate and its possible significance on endochondral ossification |
title |
Kinetic characterization of a membrane-specific ATPase from rat osseous plate and its possible significance on endochondral ossification |
spellingShingle |
Kinetic characterization of a membrane-specific ATPase from rat osseous plate and its possible significance on endochondral ossification Pizauro, J. M. ATPase Osseous plate phosphatidylinositol-specific phospholipase C endochondral ossification Alkaline phosphatase |
title_short |
Kinetic characterization of a membrane-specific ATPase from rat osseous plate and its possible significance on endochondral ossification |
title_full |
Kinetic characterization of a membrane-specific ATPase from rat osseous plate and its possible significance on endochondral ossification |
title_fullStr |
Kinetic characterization of a membrane-specific ATPase from rat osseous plate and its possible significance on endochondral ossification |
title_full_unstemmed |
Kinetic characterization of a membrane-specific ATPase from rat osseous plate and its possible significance on endochondral ossification |
title_sort |
Kinetic characterization of a membrane-specific ATPase from rat osseous plate and its possible significance on endochondral ossification |
author |
Pizauro, J. M. |
author_facet |
Pizauro, J. M. Demenis, M. A. Ciancaglini, P. Leone, F. A. |
author_role |
author |
author2 |
Demenis, M. A. Ciancaglini, P. Leone, F. A. |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade de São Paulo (USP) Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Pizauro, J. M. Demenis, M. A. Ciancaglini, P. Leone, F. A. |
dc.subject.por.fl_str_mv |
ATPase Osseous plate phosphatidylinositol-specific phospholipase C endochondral ossification Alkaline phosphatase |
topic |
ATPase Osseous plate phosphatidylinositol-specific phospholipase C endochondral ossification Alkaline phosphatase |
description |
Treatment with phosphatidylinositol-specific phospholipase C of rat osseous plate membranes released up to 90-95% of alkaline phosphatase, but a specific ATPase activity (optimum pH = 7.5) remained bound to the membrane. The hydrolysis of ATP by this ATPase was negligible in the absence of magnesium or calcium ions. However, at millimolar concentrations of magnesium and calcium ions, the membrane-specific ATPase activity increased to about 560-600 U/mg, exhibiting two classes of ATP-hydrolysing sites, and site-site interactions. GTP, UTP, ITP, and CTP were also hydrolyzed by the membrane-specific ATPase. Oligomycin, ouabain, bafilomycin A(1), thapsigargin, omeprazole, ethacrynic acid and EDTA slightly affected membrane-specific ATPase activity while vanadate produced a 18% inhibition. The membrane-specific ATPase activity was insensitive to theophylline, but was inhibited 40% by levamisole. These data suggested that the membrane-specific ATPase activity present in osseous plate membranes, and alkaline phosphatase, were different proteins. (C) 1998 Elsevier B.V. B.V. |
publishDate |
1998 |
dc.date.none.fl_str_mv |
1998-01-05 2014-05-20T13:17:32Z 2014-05-20T13:17:32Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/S0005-2736(97)00174-0 Biochimica Et Biophysica Acta-biomembranes. Amsterdam: Elsevier B.V., v. 1368, n. 1, p. 108-114, 1998. 0005-2736 http://hdl.handle.net/11449/3973 10.1016/S0005-2736(97)00174-0 WOS:000071507700012 WOS000071507700012.pdf |
url |
http://dx.doi.org/10.1016/S0005-2736(97)00174-0 http://hdl.handle.net/11449/3973 |
identifier_str_mv |
Biochimica Et Biophysica Acta-biomembranes. Amsterdam: Elsevier B.V., v. 1368, n. 1, p. 108-114, 1998. 0005-2736 10.1016/S0005-2736(97)00174-0 WOS:000071507700012 WOS000071507700012.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Biochimica et Biophysica Acta: Biomembranes 3.438 1,495 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
108-114 application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier B.V. |
publisher.none.fl_str_mv |
Elsevier B.V. |
dc.source.none.fl_str_mv |
Web of Science reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1792962020969021440 |