Literature DB >> 3518805

Tryptophanyl-tRNA synthetase is a major soluble protein species in bovine pancreas.

M L Sallafranque, M Garret, J P Benedetto, M Fournier, B Labouesse, J Bonnet.   

Abstract

Besides their central role in protein synthesis, aminoacyl-tRNA synthetases have been found or thought to be involved in other processes. We present here a study showing that tryptophanyl-tRNA synthetase has a surprising tissular distribution. Indeed, immunochemical determinations showed that in several bovine organs such as liver, kidney and heart, tryptophanyl-tRNA synthetase constitutes, as expected, about 0.02% of soluble proteins. In spleen, brain cortex, stomach, cerebellum or duodenum, this amount is about 10-times higher, and in pancreas it is 100-fold. There is no correlation between these amounts and the RNA content of the organs. Moreover, the concentration of another aminoacyl-tRNA synthetase (methionyl-tRNA synthetase) is higher in liver than in pancreas, while the amount of tRNATrp is not higher in pancreas than in liver as compared to other tRNAs. Among several interpretations, it is possible that tryptophanyl-tRNA synthetase is involved in a function other than tRNA aminoacylation. This unknown function would be specific to the differentiated organs, since fetal cerebellum and fetal pancreas contain the same amount of tryptophanyl-tRNA synthetase as adult liver.

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Year:  1986        PMID: 3518805     DOI: 10.1016/0304-4165(86)90155-8

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  6 in total

1.  Aminoacyl-tRNA synthetases catalyze AMP----ADP----ATP exchange reactions, indicating labile covalent enzyme-amino-acid intermediates.

Authors:  E Rapaport; P Remy; H Kleinkauf; J Vater; P C Zamecnik
Journal:  Proc Natl Acad Sci U S A       Date:  1987-11       Impact factor: 11.205

2.  Tryptophanyl-tRNA synthetase-like immunoreactivity in the central nervous system and midgut of the migratory locust. Comparisons with gastrin-cholecystokinin-like and octopamine-like immunoreactivity.

Authors:  M Tamarelle; M L Sallafranque; J P Benedetto; J Bonnet; J Vieillemaringe; J Girardie
Journal:  Histochemistry       Date:  1990

3.  A human aminoacyl-tRNA synthetase as a regulator of angiogenesis.

Authors:  Keisuke Wakasugi; Bonnie M Slike; John Hood; Atsushi Otani; Karla L Ewalt; Martin Friedlander; David A Cheresh; Paul Schimmel
Journal:  Proc Natl Acad Sci U S A       Date:  2002-01-02       Impact factor: 11.205

Review 4.  Tryptophanyl-tRNA Synthetase as a Potential Therapeutic Target.

Authors:  Young Ha Ahn; Se-Chan Oh; Shengtao Zhou; Tae-Don Kim
Journal:  Int J Mol Sci       Date:  2021-04-26       Impact factor: 5.923

5.  An appended domain results in an unusual architecture for malaria parasite tryptophanyl-tRNA synthetase.

Authors:  Sameena Khan; Ankur Garg; Arvind Sharma; Noelia Camacho; Daria Picchioni; Adélaïde Saint-Léger; Lluís Ribas de Pouplana; Manickam Yogavel; Amit Sharma
Journal:  PLoS One       Date:  2013-06-12       Impact factor: 3.240

6.  Identification of a residue crucial for the angiostatic activity of human mini tryptophanyl-tRNA synthetase by focusing on its molecular evolution.

Authors:  Terumasa Nakamoto; Miki Miyanokoshi; Tomoaki Tanaka; Keisuke Wakasugi
Journal:  Sci Rep       Date:  2016-04-20       Impact factor: 4.379

  6 in total

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