Hostname: page-component-6bf8c574d5-gr6zb Total loading time: 0 Render date: 2025-02-15T09:32:14.912Z Has data issue: false hasContentIssue false
  • English
  • Français

A Genetic Study of Erythrocyte Arginine-tRNA Synthetase Activity in Man

Published online by Cambridge University Press:  27 January 2025

Sylvia A. McCune ,
P. L. Yu  and
Walter E. Nance
Sylvia A. McCune
Affiliation:
Department of Medical Genetics, Indiana University School of Medicine, Indianapolis, Indiana, USA
P. L. Yu
Affiliation:
Department of Medical Genetics, Indiana University School of Medicine, Indianapolis, Indiana, USA
Walter E. Nance
Affiliation:
Department of Human Genetics, Medical College of Virginia, Richmond, Virginia, USA

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

To search for evidence of genetic variation among the aminoacyl-tRNA synthetases, a semi-automated assay procedure employing a Technicon Auto Analyzer was used to measure erythrocyte arginine-tRNA synthetase activity in samples obtained from normal human twins of various ages. Variation in enzyme activity within the older DZ twins was five times that of the MZ twins suggesting the existence of genetically determined variation in enzyme activity. Higher enzyme activity was observed in newborn DZ unlike-sexed twins than in like-sexed twins of either zygosity. Possible explanations for this observation are discussed.

Riassunto

RIASSUNTO

Al fine di valutare la variazione genetica fra aminoacil-tRNA sintetasi, è stato utilizzato un procedimento semiautomatizzato mediante impiego di un Technicon Auto-Analyzer, per misurare l'attività dell'arginina-tRNA sintetasi eritrocitaria in gemelli normali di varie età. La variazione nell'attività enzimatica nei gemelli DZ più anziani è risultata cinque volte superiore a quella dei gemelli MZ, indicando l'esistenza di un determinismo genetico dell'attività enzimatica. Una più elevata attività enzimatica è stata osservata in gemelli neonati di sesso opposto rispetto a gemelli dello stesso sesso e le possibili spiegazioni di tale reperto vengono discusse.

Résumé

RÉSUMÉ

Dans le but d'évaluer la variation génétique des amynoacyl-tRNA synthetases, un procédé d'essai sémiautomatisé, moyennant un Technicon Auto-Analyzer, a été utilisé pour mesurer l'activité de l'arginine tRNA synthétase érythrocytaire chez des jumeaux normaux de différents âges. La variation dans l'activité enzymatique chez les jumeaux DZ plus âgés a été cinq fois plus élevée par rapport aux jumeaux MZ, ce qui indique l'existence de facteurs génétiques dans l'activité enzymatique. Les jumeaux nouveaux-nés de sexe différent ont présenté une activité enzymatique plus élevée par rapport aux jumeaux du même sexe; les possibles interprétations de cette observation sont discutées.

Zusammenfassung

ZUSAMMENFASSUNG

Zur Beurteilung der Erbvariation unter den tRNS-Aminoazyl-Synthetasen wurde ein halbautomatisches Verfahren unter Benützung eines Technicon Auto-Analyzers angewandt, um die tRNS-Arginin-Synthetase-Aktivität in den Erythrozyten von normalen Zwillingen verschiedenen Alters zu messen. Bei den älteren ZZ war die Variation der Enzymtätigkeit fünfmal so hoch wie bei EZ, was dafür spricht, daß die Enzymtätigkeit erbbedingt ist. Es wurde auch die Beobachtung erörtert, daß die Enzymtätigkeit bei neugeborenen Pärchenzwillingen höher war als bei gleichgeschlechtlichen Zwillingspaaren, um die Bedeutung dieser Beobachtung zu verstehen.

Type
Research Article
Information
Acta geneticae medicae et gemellologiae: twin research , Volume 26 , Issue 1 , January 1977 , pp. 21 - 27
Copyright
Copyright © The International Society for Twin Studies 1977

References

REFERENCES

Anderson, W.F. 1969. Evolutionary conservation of the synthetase recognition site of alanine transfer ribonucleic acid. Biochemistry, 8: 3687–3691.CrossRefGoogle ScholarPubMed
Benirschke, K. 1970. Spontaneous chimerism in mammals - A critical review. Curr. Top. Pathol., 51: 1–61.Google Scholar
Benirschke, K., Kim, C.K. 1973. Multiple pregnancy. N. Engl. J. Med., 288:1276–1284, 1329–1336.CrossRefGoogle ScholarPubMed
Bick, M.D., Strehler, B.L. 1971. Leucyl transfer RNA synthetase changes during soybean cotyledon senescence. Proc. Natl. Acad. Sci. USA, 68: 224–228.CrossRefGoogle ScholarPubMed
Busby, W. F., Hele, P. 1970. Estrogen induced variation of lysine tRNA isoacceptors in chicken liver. Biochim. Biophys. Acta, 224: 413–422.CrossRefGoogle Scholar
Cameron, A.H. 1968. The Birmingham twin study. Proc. R. Soc. Med., 61: 229–236.Google Scholar
Christian, J.C., Kang, K.W., Norton, J.A. 1974. Choice of estimate of genetic variance from twin data. Am. J. Hum. Genet., 26: 154–161.Google ScholarPubMed
El-Alfi, O.S., and Hathout, H. 1969. Maternofetal transfusion: Immunologic and cytogenetic evidence. Am. J. Obstet. Gynecol., 103: 599–600.CrossRefGoogle ScholarPubMed
Elska, A., Matsuka, G., Matiash, V. et al. 1971. tRNA and aminoacyl-tRNA synthetases during differentiation and various functional states of the mammary gland. Biochim. Biophys. Acta, 247: 430–440.CrossRefGoogle ScholarPubMed
Gallo, R.C., Pestka, S. 1971. Transfer RNA species in normal and leukemic human lymphoblasts. J. Mol. Biol., 52: 195–219.CrossRefGoogle Scholar
Germanyuk, Y., Mironenko, V.I. 1969. Insulin and the attachment of amino acids to the liver transfer RNAs. Nature, 222: 486–487.CrossRefGoogle Scholar
Goldman, M., Johnston, W.M., Griffin, A.C. 1969. Comparison of transfer RNA and aminoacyl-tRNA synthetase of liver and ascites tumor cells. Cancer Res., 29: 1051–1055.Google Scholar
Marchin, G.L., Comer, M.M., Neidhardt, F.C. 1972. Viral modifications of the valyl transfer ribonucleic acid synthetase of Escherichia coli . J. Biol. Chem., 247: 5132–5145.CrossRefGoogle ScholarPubMed
Matthaei, J.H., Schoech, G.K. 1967. Human gene expression I: An aminoacyl-tRNA binding system from human placenta. Biochem. Biophys. Res. Commun., 27: 638–643.CrossRefGoogle Scholar
McCune, S.A., 1974. Genetic studies of human aminoacyl-transfer ribonucleic acid synthetases from erythrocytes and placentae of normal twins. Ph.D. thesis, Indiana Univeristy.Google Scholar
Nance, W.E. 1977. The relevance of twin studies in cancer research. In, Mulvihill, J.J. (ed.): The Genetics of Human Cancer (pp. 27–38). New York: Raven Press.Google Scholar
Neth, V.R., Heller, G., Matthaei, H. 1968. Menschliche Protein Synthese III: Preparation von Ribosomen, Transfer-RNA und Aminoacyl-transfer-RNA Synthetase aus Operations-und Biopsie Material. Hoppe-Seyler's, Z. Physiol. Chem., 349: 1514–1524.CrossRefGoogle Scholar
Newman, H.H., Freeman, F.N., Holzinger, K. 1937. Twins: Study of Heredity and Environment. Chicago: Univ. Chicago Press.Google Scholar
Ounsted, C., Taylor, D.C. 1972. Gender Differences: Their Ontogeny and Significance. Edinburgh: Churchill Livingstone.Google Scholar
Rennert, Q.M. 1969. Aminoacyl-tRNA synthetase reaction unique to early embryonic tissue of the mouse. Proc. Natl. Acad. Sci. USA, 63: 878–884.CrossRefGoogle ScholarPubMed
Sein, K.T., Becarevic, A., Kanazir, D. 1969. A simple modified method for the extraction of rat liver sRNA. Anal. Biochem., 28: 65–69.CrossRefGoogle ScholarPubMed
Smith, S.M., Penrose, L.S. 1955. Monozygotic and dizygotic twin diagnosis. Ann. Hum. Genet., 19: 273–289.CrossRefGoogle ScholarPubMed
Spadafora, C., Igo-Kemenes, T., Zachau, H.G. 1973. Changes in transfer RNA and aminoacyl-tRNA synthetases during sea urchin development. Biochim. Biophys. Acta, 312: 674–684.CrossRefGoogle ScholarPubMed
Strehler, B.L., Hendley, D.D., Hirsch, G.P. 1967. Evidence on a codon restriction hypothesis of cellular differentiation: Multiplicity of mammaHan leucyl-sRNA-specific synthetases and tissue specific deficiency in an alanyl-sRNA synthetase. Proc. Natl. Acad. Sci. USA, 57: 1751–1758.CrossRefGoogle Scholar
Tchou, H.P., Claflin, A.J., Muench, K.H. 1971. Tryptophanyl transfer RNA synthetase from lymphocytes of human chronic lymphocytic leukemia. Cancer Res., 31: 679–683.Google ScholarPubMed
Warburg, O., Christian, W. 1941. Isolurung and Kristallisation des Garungferments Enolase. Biochem, Z., 310: 384–421.Google Scholar