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Rat vas deferens SERCA2 is modulated by Ca(2+)/calmodulin protein kinase II-mediated phosphorylation

Ca(2+) pumps are important players in smooth muscle contraction. Nevertheless, little information is available about these pumps in the vas deferens. We have determined which subtype of sarco(endo)plasmic reticulum Ca(2+)-ATPase isoform (SERCA) is expressed in rat vas deferens (RVD) and its modulati...

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Autores principales: Rodriguez, J.B.R., Muzi-Filho, H., Valverde, R.H.F., Quintas, L.E.M., Noel, F., Einicker-Lamas, M., Cunha, V.M.N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Associação Brasileira de Divulgação Científica 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3854380/
https://www.ncbi.nlm.nih.gov/pubmed/23558856
http://dx.doi.org/10.1590/1414-431X20122616
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author Rodriguez, J.B.R.
Muzi-Filho, H.
Valverde, R.H.F.
Quintas, L.E.M.
Noel, F.
Einicker-Lamas, M.
Cunha, V.M.N.
author_facet Rodriguez, J.B.R.
Muzi-Filho, H.
Valverde, R.H.F.
Quintas, L.E.M.
Noel, F.
Einicker-Lamas, M.
Cunha, V.M.N.
author_sort Rodriguez, J.B.R.
collection PubMed
description Ca(2+) pumps are important players in smooth muscle contraction. Nevertheless, little information is available about these pumps in the vas deferens. We have determined which subtype of sarco(endo)plasmic reticulum Ca(2+)-ATPase isoform (SERCA) is expressed in rat vas deferens (RVD) and its modulation by calmodulin (CaM)-dependent mechanisms. The thapsigargin-sensitive Ca(2+)-ATPase from a membrane fraction containing the highest SERCA levels in the RVD homogenate has the same molecular mass (∼115 kDa) as that of SERCA2 from the rat cerebellum. It has a very high affinity for Ca(2+) (Ca(0.5) = 780 nM) and a low sensitivity to vanadate (IC(50) = 41 µM). These facts indicate that SERCA2 is present in the RVD. Immunoblotting for CaM and Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) showed the expression of these two regulatory proteins. Ca(2+) and CaM increased serine-phosphorylated residues of the 115-kDa protein, indicating the involvement of CaMKII in the regulatory phosphorylation of SERCA2. Phosphorylation is accompanied by an 8-fold increase of thapsigargin-sensitive Ca(2+) accumulation in the lumen of vesicles derived from these membranes. These data establish that SERCA2 in the RVD is modulated by Ca(2+) and CaM, possibly via CaMKII, in a process that results in stimulation of Ca(2+) pumping activity.
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spelling pubmed-38543802013-12-16 Rat vas deferens SERCA2 is modulated by Ca(2+)/calmodulin protein kinase II-mediated phosphorylation Rodriguez, J.B.R. Muzi-Filho, H. Valverde, R.H.F. Quintas, L.E.M. Noel, F. Einicker-Lamas, M. Cunha, V.M.N. Braz J Med Biol Res Biomedical Sciences Ca(2+) pumps are important players in smooth muscle contraction. Nevertheless, little information is available about these pumps in the vas deferens. We have determined which subtype of sarco(endo)plasmic reticulum Ca(2+)-ATPase isoform (SERCA) is expressed in rat vas deferens (RVD) and its modulation by calmodulin (CaM)-dependent mechanisms. The thapsigargin-sensitive Ca(2+)-ATPase from a membrane fraction containing the highest SERCA levels in the RVD homogenate has the same molecular mass (∼115 kDa) as that of SERCA2 from the rat cerebellum. It has a very high affinity for Ca(2+) (Ca(0.5) = 780 nM) and a low sensitivity to vanadate (IC(50) = 41 µM). These facts indicate that SERCA2 is present in the RVD. Immunoblotting for CaM and Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) showed the expression of these two regulatory proteins. Ca(2+) and CaM increased serine-phosphorylated residues of the 115-kDa protein, indicating the involvement of CaMKII in the regulatory phosphorylation of SERCA2. Phosphorylation is accompanied by an 8-fold increase of thapsigargin-sensitive Ca(2+) accumulation in the lumen of vesicles derived from these membranes. These data establish that SERCA2 in the RVD is modulated by Ca(2+) and CaM, possibly via CaMKII, in a process that results in stimulation of Ca(2+) pumping activity. Associação Brasileira de Divulgação Científica 2013-03-19 /pmc/articles/PMC3854380/ /pubmed/23558856 http://dx.doi.org/10.1590/1414-431X20122616 Text en http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Biomedical Sciences
Rodriguez, J.B.R.
Muzi-Filho, H.
Valverde, R.H.F.
Quintas, L.E.M.
Noel, F.
Einicker-Lamas, M.
Cunha, V.M.N.
Rat vas deferens SERCA2 is modulated by Ca(2+)/calmodulin protein kinase II-mediated phosphorylation
title Rat vas deferens SERCA2 is modulated by Ca(2+)/calmodulin protein kinase II-mediated phosphorylation
title_full Rat vas deferens SERCA2 is modulated by Ca(2+)/calmodulin protein kinase II-mediated phosphorylation
title_fullStr Rat vas deferens SERCA2 is modulated by Ca(2+)/calmodulin protein kinase II-mediated phosphorylation
title_full_unstemmed Rat vas deferens SERCA2 is modulated by Ca(2+)/calmodulin protein kinase II-mediated phosphorylation
title_short Rat vas deferens SERCA2 is modulated by Ca(2+)/calmodulin protein kinase II-mediated phosphorylation
title_sort rat vas deferens serca2 is modulated by ca(2+)/calmodulin protein kinase ii-mediated phosphorylation
topic Biomedical Sciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3854380/
https://www.ncbi.nlm.nih.gov/pubmed/23558856
http://dx.doi.org/10.1590/1414-431X20122616
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