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Biomedical subjects

S M Arfin

Publications and source records attributed to S M Arfin.

8 recordsLinked to original sources
PubMed1992

Dipeptide inhibitors of ubiquitin-mediated protein turnover prevent growth factor-induced neurite outgrowth in rat pheochromocytoma PC12 cells.

Dipeptide inhibitors of the ubiquitin-dependent proteolysis pathway governed by N-terminal recognition (N-end rule) in reticulocyte lysates significantly suppress NGF- and bFGF-induced neurite outgrowth in rat pheochromocytoma PC12 cells, but do not cause retraction of already formed neurites. Peptides which do not inhibit proteolysis are also without effect on PC12 cell differentiation. Suppression of neurite outgrowth is readily reversible upon removal of the inhibitors. These data demonstrate a requirement for specific protein turnover in the process of neuron-like differentiation in PC12 cells and provide the first demonstration of a physiological role for the N-end rule.

Animals↗
PubMed1979

Aminoacyl-tRNA synthetase mutants degrade protein at a normal rate.

The stability of both rapidly and slowly degraded proteins in wild type CHO cells is similar to that in three ts aminoacyl-tRNA synthetase mutants at both permissive and non-permissive temperatures, although the degree of tRNA charging in the synthetase mutants differs considerably with temperature. These results indicate that the altered rate of protein breakdown seen under a variety of physiological conditions in eukaryotic systems is not mediated by uncharged tRNA.

Amino Acyl-tRNA Synthetases↗
PubMed1979

Assignment of histidase-regulating locus to chromosome 10 of the mouse.

Data from four sets of recombinant inbred strains confirm that variation at a single genetic locus is responsible for the previously observed differences in the rate of histidase synthesis in inbred mice. Linkage testing stocks were used to demonstrate linkage with steel (Sl) on chromosome 10.

Ammonia-Lyases↗
PubMed1978

Biochemical characterization of a mutant asparaginyl-tRNA synthetase from Chinese hamster ovary cells.

The biochemical and physical properties of asparaginyl-tRNA synthetase from wild type Chinese hamster ovary cells and a temperature sensitive mutant strain (lys 65a) are compared. The asparaginyl-tRNA synthetase in the mutant strain exhibits a greater temperature lability in vitro, a higher temperature-independent Km for asparagine, and a lower temperature-dependent catalytic capacity than the enzyme from the wild type strain. The mutant enzyme shows no differences in its molecular weight, its Km for tRNAAsn, or its ability to aminoacylate tRNAAsn isoacceptor species compared to the wild type enzyme. These observations, as well as the growth properties of the mutant cells as a function of temperature and exogenous asparagine concentrations, are consistent with their decreased ability to aminoacylate tRNAAsn in vivo.

Amino Acyl-tRNA Synthetases↗
PubMed1977

Genetic differences inthe te of histidase synthesis in inbred mice.

Inbred strains of mice fall into two groups with respect to their liver histidase activity levels, high strains having approximately twice as much activity as low strains. Analysis of the F1, F2, and backcross progeny of the mating of a high activity strain (C57BL/6J) and a low activity strain (C3H/HeJ) indicates that the difference between the strains is determined by a single genetic locus with two alleles exhibiting additive inheritance. No differences with respect to various physical and kinetic parameters were found in studies of partially purified histidase from both strains. Quantitation of the amount of enzyme present by immunotitration showed that the amount of enzyme antigen is proportional to the level of enzyme activity in the two strains. Measurements of the relative rates of histidase synthesis by combined radiochemical and immunological techniques showed that the relative rate of synthesis was closely correlated with the amount of enzyme present. Rates of enzyme degradation in the two strains, measured by recovery of activity after irreversible inhibition with nitromethane, were the same.

Ammonia-Lyases↗
PubMed1977

A role for asparaginyl-tRNA in the regulation of asparagine synthetase in a mammalian cell line.

The expression of asparagine synthetase activity [L-aspartate:ammonia ligase (AMP-forming), EC 6.3.1.1] in cultured Chinese hamster ovary (CHO) cells is regulated by asparagine. After transfer of CHO cells from an asparagine-supplemented medium to a medium lacking asparagine, activity increases 1.5- to 2-fold. If asparagine is added back to the medium, activity returns to control levels. To test the possible involvement of Asn-tRNAAsn in regulating the levels of asparagine synthetase, we have examined the levels of asparagine synthetase in a mutant of CHO cells containing a temperature-sensitive asparaginyl-tRNA synthetase [L-asparagine:tRNA ligase (AMP-forming), EC 6.1.1.22]. Under conditions of limited asparaginyl-tRNA synthetase activity in the mutant, there is a 2- to 3-fold increase in the level of asparagine synthetase activity. Under identical conditions, there is no change in asparagine synthetase activity in the wild type. This correlation between asparaginyl-tRNA synthetase activity and asparagine synthetase levels may be a consequence of a direct role of tRNAAsn in the regulation of the in vivo expression of the asparagine synthetase structural gene.

Asparagine↗