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N Shalitin

Publications and source records attributed to N Shalitin.

6 recordsLinked to original sources

The effect of angiotensin II on myosin heavy chain expression in cultured myocardial cells.

Angiotensin II (AII), the principal mediator of the renin-angiotensin system, is an important regulator of vascular and cardiac homeostasis. AII has also been shown to be a regulator of cardiac hypertrophy and of the corresponding changes in amount and composition of certain tissue proteins. We examined the trophic effects of AII on cultured myocytes derived from neonatal rat ventricles and followed, by Northern blot analysis and polyacrylamide gel electrophoresis, the expression of alpha- and beta-myosin heavy chain iso-mRNAs and isoproteins. Our findings show that a single administration of AII is sufficient to induce a trophic response in cultured beating myocytes and to enhance the expression of beta-myosin heavy chain iso-mRNA and isoprotein, having no effect on alpha-myosin heavy chain. Induction of alpha-myosin heavy chain expression by thyroid hormone before AII was administered showed that AII could not potentiate a shift from alpha- to beta-myosin heavy chain predominance. We suggest that the potency of AII to regulate the expression of myosin heavy chain isogenes is restricted to the beta isoform and is overridden by thyroid hormone.

Angiotensin II↗

4-Thiouridine, a built-in probe for structural changes in transfer RNA.

The luminescence of an aqueous solution of 4-thiouridine was compared with its emission when forming part of the polynucleotide chain of tRNA. In both cases excitation into the last absorption band at 335 nm yields a weak emission in the 520--550 nm region. However, while in aqueous solution this emission has a lifetime of approximately 240 ns, it increases in native tRNA to tau congruent to 6.6 mus. Oxygen and Cl- ions quench the thiouridine emission efficiently in aqueous solution while Na+ and Mg2+ ions have no influence on it. On the other hand thiouridine which forms part of a tRNA molecule is quite insensitive to Cl- ions and to O2 while its emission is greatly enhanced by Na+ and Mg2+ ions. From these salt effects as well as from data on the temperature dependence of the emission yield and the decay curve, it is concluded that the site of the thiouridine residue is very well protected within the tertiary structure of tRNA. Both permanent changes in the secondary and in the tertiary structures of the polynucleotide as well as dynamic conformation changes can be observed by following the emission characteristics of its thiouridine residue.

Binding Sites↗