Biomedical subjects

Kasturi Mitra

Publications and source records attributed to Kasturi Mitra.

3 recordsLinked to original sources

PubMed2005

Novelty of the pyruvate metabolic enzyme dihydrolipoamide dehydrogenase in spermatozoa: correlation of its localization, tyrosine phosphorylation, and activity during sperm capacitation.

Spermatozoa are cells distinctly different from other somatic cells of the body, capacitation being one of the unique phenomena manifested by this gamete. We have shown earlier that dihydrolipoamide dehydrogenase, a post-pyruvate metabolic enzyme, undergoes capacitation-dependent tyrosine phosphorylation, and the functioning of the enzyme is required for hyperactivation (enhanced motility) and acrosome reaction of hamster spermatozoa (Mitra, K., and Shivaji, S. (2004) Biol. Reprod. 70, 887-899). In this report we have investigated the localization of this mitochondrial enzyme in spermatozoa revealing non-canonical extra-mitochondrial localization of the enzyme in mammalian spermatozoa. In hamster spermatozoa, dihydrolipoamide dehydrogenase along with its host complex, the pyruvate dehydrogenase complex, are localized in the acrosome and in the principal piece of the sperm flagella. The localization of dihydrolipoamide dehydrogenase, however, appears to be in the mitochondria in the spermatocytes, but in spermatids it appears to show a juxtanuclear localization (like Golgi). The capacitation-dependent time course of tyrosine phosphorylation of dihydrolipoamide dehydrogenase appears to be different in the principal piece of the flagella and the acrosome in hamster spermatozoa. Activity assays of this bi-directional enzyme suggest a strong correlation between the tyrosine phosphorylation and the bi-directional enzyme activity. This is the first report of a direct correlation of the localization, tyrosine phosphorylation, and activity of the important metabolic enzyme, dihydrolipoamide dehydrogenase, implicating dual involvement and regulation of the enzyme during sperm capacitation.

Acrosome↗

PubMed2005

Proteins implicated in sperm capacitation.

Spermatozoa after being deposited in the female reproductive tract spend a considerable time in this foreign environment prior to fertilization of the oocyte. Chang and Austin independently observed1,2 that this time spent by the spermatozoa in the female tract is not consequential but a necessary event in the life cycle of the male gamete, and Austin2 first called this maturation period of spermatozoa as 'Capacitation'. Ever since, attempts have been made to understand and unravel the molecular mechanism of capacitation. Based on the results obtained so far, it is clear that capacitation is guided by novel signal transduction pathways influencing varied aspects of spermatozoa. Capacitation could be, thus, defined as the cumulative molecular, cellular and physiological changes that occur in spermatozoa in the female reproductive tract to achieve the final competence to fertilize the oocyte. This review is structured so as to first understand the key features of capacitation and then to survey the players which bring about these changes during capacitation.

Animals↗

PubMed2003

Novel tyrosine-phosphorylated post-pyruvate metabolic enzyme, dihydrolipoamide dehydrogenase, involved in capacitation of hamster spermatozoa.

Capacitation is a process that confers fertilizing ability to spermatozoa and this critical event occurs in the development of mammalian spermatozoa during their transit through the female reproductive tract and precedes fertilization. Because spermatozoa are relatively silent in transcription and translation, posttranslational modifications perform the regulatory functions in these cells during capacitation. In this report, we identify a candidate protein, dihydrolipoamide dehydrogenase, which is a post-pyruvate metabolic enzyme, exhibiting tyrosine phosphorylation during hamster spermatozoal capacitation. This is the first report showing dihydrolipoamide dehydrogenase as a phosphoprotein. The cDNA sequence of hamster testes dihydrolipoamide dehydrogenase does not show any variation from the already reported mammalian dihydrolipoamide dehydrogenases. Downregulation of the activity of the hamster spermatozoal enzyme by its specific inhibitor, 5-methoxyindole-2-carboxylic acid, blocks acrosome reaction completely and hyperactivation partially, confirming the role of dihydrolipoamide dehydrogenase in hamster spermatozoal capacitation. We also delineate the temporal involvement of glucose and pyruvate-lactate, showing that the former is required in the earlier stages and the latter for the later stages of hamster spermatozoal capacitation. The essentiality of pyruvate-lactate during hyperactivation and acrosome reaction necessitates the involvement of the post-pyruvate-lactate enzyme, dihydrolipoamide dehydrogenase.

Acrosome Reaction↗