Molecular cloning of rat cardiac troponin I and analysis of troponin I isoform expression in developing rat heart

AM Murphy, L Jones, HF Sims, AW Strauss - Biochemistry, 1991 - ACS Publications
AM Murphy, L Jones, HF Sims, AW Strauss
Biochemistry, 1991ACS Publications
Revised Manuscript Received October 2, 1990 abstract: We have isolated and sequenced a
cDNA encoding rat cardiac troponin I. The predicted amino acid sequence was highly
identical with previously reported chemically derived amino acid sequences for rabbit and
bovine cardiactroponin I. Clones for slow skeletal muscle troponin I were also obtained from
neonatal rat cardiac ventricle by the polymerase chain reaction. The nucleotide sequences
of these clones were determined to be more than 99% identical with a previously reported …
Revised Manuscript Received October 2, 1990 abstract: We have isolated and sequenced a cDNA encoding rat cardiac troponin I. The predicted amino acid sequence was highly identical with previously reported chemically derived amino acid sequences for rabbit and bovine cardiactroponin I. Clones for slow skeletal muscle troponin I were also obtained from neonatal rat cardiac ventricle by the polymerase chain reaction. The nucleotide sequences of these clones were determined to be more than 99% identical with a previously reported rat slow skeletal troponin I cDNA [Koppe et al.(1989) J. Biol. Chem. 264, 14327-14333]. The troponin I clones hybridized to RNA from the appropriate muscle from adult animals. However, RNA from fetal and neonatal rat heart also hybridized with the slow skeletal troponin I cDNA, demonstrating its expression in fetal and neonatal rat heart. Slow skeletal troponin I steady-state mRNA levels decreased with increasing age, but cardiac troponin I mRNA levels increased through fetal and early neonatal cardiac development. Thus, during fetal and neonatal development, slow skeletal and cardiac troponin I isoforms are coexpressed in therat heart and regulated in opposite directions. The degree of primary sequence differences in these isoforms, especially at phos-phorylation sites, mayresult in important functional differences in the neonatal myocardium.
ACS Publications
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