Protein Carboxyl-Methylation in Rat Testes: A Study of Inherited and X-Ray-Induced Seminiferous Tubule Failure*
- 1 December 1979
- journal article
- research article
- Published by The Endocrine Society in Endocrinology
- Vol. 105 (6) , 1440-1445
- https://doi.org/10.1210/endo-105-6-1440
Abstract
Protein carboxyl-methylase (PCM), the enzyme that transfers methyl groups from S-adenosyl-methionine to free carboxyl groups on proteins, is highly localized in testes. The cellular distribution of PCM and its substrates, the methyl acceptor proteins, was investigated. Separation of testicular cells on an albumin gravity gradient revealed the preferential localization of both enzyme and substrates in spermatids. In young rats, PCM activity increases with age coincidently with germ cell maturation. Rats which are heterozygous for the Hre gene (Hr7 +) are infertile as a result of germ cell depletion. In these animals, testicular PCM specific activity and total activity were, respectively, 4-6 and 40-50 times lower than in normal testes. Enzyme activity in testes from animals with x-ray-induced germ cell depletion was also very low. These observations suggest that PCM is located in germ cellsKeywords
This publication has 12 references indexed in Scilit:
- Enzymatic methylation of carboxyl groups of chromaffin granule membrane proteins.Journal of Biological Chemistry, 1978
- Chemotaxis in Escherichia coli : Methylation of che gene productsProceedings of the National Academy of Sciences, 1977
- Sensory transduction in Escherichia coli: two complementary pathways of information processing that involve methylated proteins.Proceedings of the National Academy of Sciences, 1977
- Spermatogenic cells of the prepuberal mouse: isolation and morphological characterizationThe Journal of cell biology, 1977
- Identification of a protein methyltransferase as the cheR gene product in the bacterial sensing system.Proceedings of the National Academy of Sciences, 1977
- Subcellualr distribution of protein carboxymethylase and its endogenous substrates in the adrenal medulla: possible role in excitation-secretion coupling.Proceedings of the National Academy of Sciences, 1976
- REGIONAL AND SUBCELLULAR DISTRIBUTION OF PROTEIN CARBOXYMETHYLASE IN BRAIN AND OTHER TISSUESJournal of Neurochemistry, 1976
- Separation of mouse spermatogenic cells by sedimentation velocityDevelopmental Biology, 1976
- Pituitary Gland: Enzymic Formation of Methanol from S -AdenosylmethionineScience, 1965
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951