Rat vas deferens SERCA2 is modulated by Ca2+/calmodulin protein kinase II-mediated phosphorylation
Ca2+ 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 Ca2+-ATPase isoform (SERCA) is expressed in rat vas deferens (RVD) and its modulation b...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Associação Brasileira de Divulgação Científica
2013-01-01
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| Series: | Brazilian Journal of Medical and Biological Research |
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| Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2013000300227 |
| _version_ | 1818985708209045504 |
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| author | J.B.R. Rodriguez H. Muzi-Filho R.H.F. Valverde L.E.M. Quintas F. Noel M. Einicker-Lamas V.M.N. Cunha |
| author_facet | J.B.R. Rodriguez H. Muzi-Filho R.H.F. Valverde L.E.M. Quintas F. Noel M. Einicker-Lamas V.M.N. Cunha |
| author_sort | J.B.R. Rodriguez |
| collection | DOAJ |
| description | Ca2+ 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 Ca2+-ATPase isoform (SERCA) is expressed in rat vas deferens (RVD) and its modulation by calmodulin (CaM)-dependent mechanisms. The thapsigargin-sensitive Ca2+-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 Ca2+ (Ca0.5 = 780 nM) and a low sensitivity to vanadate (IC50 = 41 µM). These facts indicate that SERCA2 is present in the RVD. Immunoblotting for CaM and Ca2+/calmodulin-dependent protein kinase II (CaMKII) showed the expression of these two regulatory proteins. Ca2+ 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 Ca2+ accumulation in the lumen of vesicles derived from these membranes. These data establish that SERCA2 in the RVD is modulated by Ca2+ and CaM, possibly via CaMKII, in a process that results in stimulation of Ca2+ pumping activity. |
| first_indexed | 2024-12-20T18:39:11Z |
| format | Article |
| id | doaj.art-c81620b6ef814a50a08178c367de3e45 |
| institution | Directory Open Access Journal |
| issn | 0100-879X 1414-431X |
| language | English |
| last_indexed | 2024-12-20T18:39:11Z |
| publishDate | 2013-01-01 |
| publisher | Associação Brasileira de Divulgação Científica |
| record_format | Article |
| series | Brazilian Journal of Medical and Biological Research |
| spelling | doaj.art-c81620b6ef814a50a08178c367de3e452022-12-21T19:29:51ZengAssociação Brasileira de Divulgação CientíficaBrazilian Journal of Medical and Biological Research0100-879X1414-431X2013-01-01463227234Rat vas deferens SERCA2 is modulated by Ca2+/calmodulin protein kinase II-mediated phosphorylationJ.B.R. RodriguezH. Muzi-FilhoR.H.F. ValverdeL.E.M. QuintasF. NoelM. Einicker-LamasV.M.N. CunhaCa2+ 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 Ca2+-ATPase isoform (SERCA) is expressed in rat vas deferens (RVD) and its modulation by calmodulin (CaM)-dependent mechanisms. The thapsigargin-sensitive Ca2+-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 Ca2+ (Ca0.5 = 780 nM) and a low sensitivity to vanadate (IC50 = 41 µM). These facts indicate that SERCA2 is present in the RVD. Immunoblotting for CaM and Ca2+/calmodulin-dependent protein kinase II (CaMKII) showed the expression of these two regulatory proteins. Ca2+ 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 Ca2+ accumulation in the lumen of vesicles derived from these membranes. These data establish that SERCA2 in the RVD is modulated by Ca2+ and CaM, possibly via CaMKII, in a process that results in stimulation of Ca2+ pumping activity.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2013000300227Ca2+/calmodulin-dependent kinase IICalcium homeostasisCalmodulinRat vas deferensSERCA2Thapsigargin |
| spellingShingle | J.B.R. Rodriguez H. Muzi-Filho R.H.F. Valverde L.E.M. Quintas F. Noel M. Einicker-Lamas V.M.N. Cunha Rat vas deferens SERCA2 is modulated by Ca2+/calmodulin protein kinase II-mediated phosphorylation Brazilian Journal of Medical and Biological Research Ca2+/calmodulin-dependent kinase II Calcium homeostasis Calmodulin Rat vas deferens SERCA2 Thapsigargin |
| title | Rat vas deferens SERCA2 is modulated by Ca2+/calmodulin protein kinase II-mediated phosphorylation |
| title_full | Rat vas deferens SERCA2 is modulated by Ca2+/calmodulin protein kinase II-mediated phosphorylation |
| title_fullStr | Rat vas deferens SERCA2 is modulated by Ca2+/calmodulin protein kinase II-mediated phosphorylation |
| title_full_unstemmed | Rat vas deferens SERCA2 is modulated by Ca2+/calmodulin protein kinase II-mediated phosphorylation |
| title_short | Rat vas deferens SERCA2 is modulated by Ca2+/calmodulin protein kinase II-mediated phosphorylation |
| title_sort | rat vas deferens serca2 is modulated by ca2 calmodulin protein kinase ii mediated phosphorylation |
| topic | Ca2+/calmodulin-dependent kinase II Calcium homeostasis Calmodulin Rat vas deferens SERCA2 Thapsigargin |
| url | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2013000300227 |
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