Spontaneously hypertensive rats and platelet Ca2+-ATPases: Specific up-regulation of the 97 kDa isoform

B. Papp, E. Corvazier, C. Magnier, T. Kovács, N. Bourdeau, S. Levy-Toledano, R. Bredoux, B. Levy, P. Poitevin, A. M. Lompre, F. Wuytack, J. Enouf

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Abstract

The use of platelets instead of smooth muscle cells (SMC) to study the abnormal Ca2+ handling found in hypertension was investigated using spontaneously hypertensive rats (SHR). We studied the regulation of platelet Ca2+-ATPases, as we have recently demonstrated that human platelets, like SMC, contain the Ca2+-ATPase isoform termed SERCA(2-b) (sarco-endoplasmic reticulum Ca2+-ATPase). In mixed membranes isolated from platelets of normotensive Wistar-Kyoto (WKY) rats and SHR, total Ca2+-ATPase activity was found to be 43 % higher in SHR than in WKY rats. By the use of autophosphorylation of rat platelet Ca2+-ATPases with [γ-32P]ATP, followed by SDS/PAGE and Western blotting, we found that rat platelets express two distinct Ca2+-ATPases: a 100 kDa isoform, recognized by a SERCA(2-b)-specific anti-peptide antibody, and a 97 kDa isoform, specifically recognized by a polyclonal anti-SERCA antibody. Comparative analysis of platelet membrane Ca2+-ATPases from WKY rats and SHR demonstrated that the expression of the SERCA(2-b) isoform did not change significantly (128 ± 22%), whereas that of the 97 kDa isoform reached 300 ± 35 % in SHR when compared with WKY rats. We concluded that the upregulation of total platelet Ca2+-ATPases in SHR is not due to the 100 kDa SERCA(2-b) isoform found in SMC, but is specific to the 97 kDa Ca2+-ATPase isoform which is not present in SMC. Therefore platelets should be used with extreme caution as a surrogate model of vascular smooth muscle Ca2+ homoeostasis.

Original languageEnglish
Pages (from-to)685-690
Number of pages6
JournalBiochemical Journal
Volume295
Issue number3
Publication statusPublished - 1993

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Calcium-Transporting ATPases
Inbred SHR Rats
Platelets
Rats
Protein Isoforms
Up-Regulation
Blood Platelets
Inbred WKY Rats
Smooth Muscle Myocytes
Muscle
Anti-Idiotypic Antibodies
Sarcoplasmic Reticulum Calcium-Transporting ATPases
Membranes
Vascular Smooth Muscle
Antibodies
Polyacrylamide Gel Electrophoresis
Homeostasis
Adenosine Triphosphate
Western Blotting
Hypertension

ASJC Scopus subject areas

  • Biochemistry

Cite this

Papp, B., Corvazier, E., Magnier, C., Kovács, T., Bourdeau, N., Levy-Toledano, S., ... Enouf, J. (1993). Spontaneously hypertensive rats and platelet Ca2+-ATPases: Specific up-regulation of the 97 kDa isoform. Biochemical Journal, 295(3), 685-690.

Spontaneously hypertensive rats and platelet Ca2+-ATPases : Specific up-regulation of the 97 kDa isoform. / Papp, B.; Corvazier, E.; Magnier, C.; Kovács, T.; Bourdeau, N.; Levy-Toledano, S.; Bredoux, R.; Levy, B.; Poitevin, P.; Lompre, A. M.; Wuytack, F.; Enouf, J.

In: Biochemical Journal, Vol. 295, No. 3, 1993, p. 685-690.

Research output: Contribution to journalArticle

Papp, B, Corvazier, E, Magnier, C, Kovács, T, Bourdeau, N, Levy-Toledano, S, Bredoux, R, Levy, B, Poitevin, P, Lompre, AM, Wuytack, F & Enouf, J 1993, 'Spontaneously hypertensive rats and platelet Ca2+-ATPases: Specific up-regulation of the 97 kDa isoform', Biochemical Journal, vol. 295, no. 3, pp. 685-690.
Papp B, Corvazier E, Magnier C, Kovács T, Bourdeau N, Levy-Toledano S et al. Spontaneously hypertensive rats and platelet Ca2+-ATPases: Specific up-regulation of the 97 kDa isoform. Biochemical Journal. 1993;295(3):685-690.
Papp, B. ; Corvazier, E. ; Magnier, C. ; Kovács, T. ; Bourdeau, N. ; Levy-Toledano, S. ; Bredoux, R. ; Levy, B. ; Poitevin, P. ; Lompre, A. M. ; Wuytack, F. ; Enouf, J. / Spontaneously hypertensive rats and platelet Ca2+-ATPases : Specific up-regulation of the 97 kDa isoform. In: Biochemical Journal. 1993 ; Vol. 295, No. 3. pp. 685-690.
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abstract = "The use of platelets instead of smooth muscle cells (SMC) to study the abnormal Ca2+ handling found in hypertension was investigated using spontaneously hypertensive rats (SHR). We studied the regulation of platelet Ca2+-ATPases, as we have recently demonstrated that human platelets, like SMC, contain the Ca2+-ATPase isoform termed SERCA(2-b) (sarco-endoplasmic reticulum Ca2+-ATPase). In mixed membranes isolated from platelets of normotensive Wistar-Kyoto (WKY) rats and SHR, total Ca2+-ATPase activity was found to be 43 {\%} higher in SHR than in WKY rats. By the use of autophosphorylation of rat platelet Ca2+-ATPases with [γ-32P]ATP, followed by SDS/PAGE and Western blotting, we found that rat platelets express two distinct Ca2+-ATPases: a 100 kDa isoform, recognized by a SERCA(2-b)-specific anti-peptide antibody, and a 97 kDa isoform, specifically recognized by a polyclonal anti-SERCA antibody. Comparative analysis of platelet membrane Ca2+-ATPases from WKY rats and SHR demonstrated that the expression of the SERCA(2-b) isoform did not change significantly (128 ± 22{\%}), whereas that of the 97 kDa isoform reached 300 ± 35 {\%} in SHR when compared with WKY rats. We concluded that the upregulation of total platelet Ca2+-ATPases in SHR is not due to the 100 kDa SERCA(2-b) isoform found in SMC, but is specific to the 97 kDa Ca2+-ATPase isoform which is not present in SMC. Therefore platelets should be used with extreme caution as a surrogate model of vascular smooth muscle Ca2+ homoeostasis.",
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AU - Bredoux, R.

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