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Expression of sarcoplasmic‐endoplasmic reticulum Ca‐ ATP ase isoforms in masticatory muscles
Author(s) -
Sánchez Gabriel A.,
Trinks Pablo W.,
Richard Susana B.,
Di Croce Daniel E.,
Takara Delia
Publication year - 2014
Publication title -
european journal of oral sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.802
H-Index - 93
eISSN - 1600-0722
pISSN - 0909-8836
DOI - 10.1111/eos.12098
Subject(s) - serca , endoplasmic reticulum , gene isoform , chemistry , phospholamban , myocyte , endocrinology , medicine , biochemistry , biology , atpase , enzyme , gene
The aim of this study was to characterize the sarcoplasmic‐endoplasmic reticulum Ca‐ ATP ase ( SERCA ) isoforms in rabbit masticatory muscles compared with those in fast‐twitch muscle. It was hypothesized that combined expression of the SERCA isoforms in fast‐ and slow‐twitch muscles accounts for lower Ca‐ ATP ase activity. SERCA was isolated by differential centrifugation, the isoforms were determined by ELISA , and the activity of each isoform was measured using a colorimetric method. Activity was tested for significance by anova , and the distribution of isoforms was assessed using the chi‐square test ( P < 0.05) and correlated to SERCA activity using S pearman's rank correlation. SERCA 1 was predominant (90.5%) in fast‐twitch muscle, whereas a mixture of SERCA isoforms was found in masticatory muscles: 62–78% was SERCA 2 , 20–37% was SERCA 1 , and the SERCA 3 content was negligible. Depressor muscles showed a significantly higher content (77.8%) of SERCA 2 , and elevator muscles showed a higher content (35.4%) of SERCA 1 . Elevator muscles showed higher expression of SERCA 2a (58%), and depressor muscles showed higher expression of SERCA 2b (20%). The SERCA 1 content was mainly SERCA 1a and significantly higher for elevator muscles (33%), whereas depressor muscles showed a higher content of SERCA1 b (4%). The SERCA 1 content of fast‐twitch muscle was mainly SERCA 1a (88.5%). It is concluded that the mixture of different SERCA isoforms, along with a substantial content of SERCA 2b , in masticatory muscles would support lower Ca‐ ATP ase activity and calcium transport.