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Electrophoretic variants of cardiac myosin heavy chain‐α in Sprague Dawley rats
Author(s) -
Reiser Peter J.,
Wick Macdonald,
Pretzman Charles I.
Publication year - 2004
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200305709
Subject(s) - myosin , electrophoresis , chemistry , heavy chain , chromatography , biophysics , biochemistry , biology , gene
Analysis of cardiac myosin revealed differences in gel electrophoretic migration patterns of the α‐isoform of myosin heavy chain, but not the β‐isoform, in Sprague Dawley rats. No differences in the migration patterns of the α‐or β‐isoforms were observed in other rat strains. Three electrophoretic migration patterns of the α‐isoforms were observed in individual rats: a slower migrating isoform alone (4% of all rats tested), a faster migrating isoform alone (55%), and both isoforms (41%). The isoform expression pattern was identical in all myocardial regions in each rat. Frequency of expression patterns suggests multiple gene sequences for α‐cardiac myosin heavy chain in Sprague Dawley rats. Sequence analysis of amplified regions of the Sprague Dawley and Brown Norway rat α‐myosin genes, specifically the 5'‐untranslated region, exons 1–3, and associated introns, showed numerous single nucleotide polymorphisms in coding and noncoding regions, including putative regulatory sites in Sprague Dawley rats, but not in Brown Norway rats. All Sprague Dawley rats varied from Brown Norway rats and no heterogeneity was observed in Brown Norway rats. Several deletions and dimorphic positions were also observed. Dimorphic positions were evident on automated sequencing comparisons. The data indicate that at least two α‐myosin heavy chain isoforms exist in Sprague Dawley rats and these rats exhibit sequence diversity within that portion of the α‐myosin heavy chain gene reported in this study.