Molecular Human Reproduction, Vol 4, 215-226, Copyright © 1998 by Oxford University Press
LO Goodwin, NB Leeds, I Hurley, GW Cooper, RG Pergolizzi and S Benoff
Cell-specific isoforms of the alpha1 subunit of the L-type voltage-
dependent calcium channel (VDCC) have unique pharmacological reactivities.
Prior sequence analysis of nucleotide bases 3908-6077 of the VDCC alpha1
subunit expressed in rat testis differed from cardiac sequences only in a
84 base pair region corresponding to exons 31/32 encoding a putative
dihydropyridine binding region. We now report that sequence analysis of
bases 3048-3936 identifies a second difference between the rat testis and
rat cardiac alpha1 sequence in a 60 base pair region corresponding to exons
21/22 and encoding another putative dihydropyridine binding site. Variable
VDCC exons 21/22 and 31/32 and their linking introns were sequenced using
genomic DNA from rat lung as template, providing evidence that the rat
testis and cardiac alpha1 isoforms are products of the same gene. Reverse
transcription in-situ polymerase chain reaction (PCR) with frozen sections
of rat testis was carried out with primers identifying the testis-specific
exon 32 of the VDCC alpha1 subunit. PCR products were confined to
seminiferous tubules and were associated with the germ cell lineage from
Type A spermatogonia to mature spermatozoa. Close coupling of testis alpha1
VDCC gene transcription and translation was established by in-situ
immunolabelling of serial frozen sections with a monoclonal antibody (IIF7)
directed against epitopes on rabbit skeletal muscle L-type VDCC alpha1.
Western blot analysis of rat proteins extracted from heart, skeletal
muscle, testis and spermatozoa which were reactive with the IIF7 antibody
detected primarily 175-220 kDa proteins in the size range of VDCC. These
data unequivocally demonstrate that an L-type VDCC is expressed in rat
testis and that VDCC isoforms from rat testis and heart differ in deduced
amino acid composition in and around potential binding sites for calcium
channel blocking drugs such as the dihydropyridines.
JOURNAL ARTICLE
Alternative splicing of exons in the alpha1 subunit of the rat testis L- type voltage-dependent calcium channel generates germ line-specific dihydropyridine binding sites
Department of Research, North Shore University Hospital-New York University School of Medicine, Manhasset, USA.
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