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Expression of lactate dehydrogenases A and B during chicken spermatogenesis: Characterization of testis specific transcripts
Author(s) -
Arias W. Martínez,
Mezquita C.,
Mezquita J.
Publication year - 2000
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/1097-4644(2000)79:1<15::aid-jcb30>3.0.co;2-4
Subject(s) - spermatogenesis , biology , messenger rna , lactate dehydrogenase , lactate dehydrogenase a , isozyme , microbiology and biotechnology , gene , meiosis , glycolysis , gene expression , spermatocyte , enzyme , biochemistry , endocrinology
The substrates required for glycolysis change markedly at successive stages of spermatogenesis suggesting a considerable plasticity in the expression of glycolytic enzymes. Lactate dehydrogenase (LDH) isoenzymes, LDH‐A and LDH‐B, are expressed in premeiotic, meiotic cells, and early spermatids, both in avian and mammalian spermatogenesis. Highly polyadenylated forms, particularly of LDH‐A, were detected in chicken testis. While mammals and columbid birds express the testis specific LDH‐C gene in meiotic and postmeiotic cells, several LDH‐B testis specific transcripts were detected in the corresponding cells during chicken spermatogenesis. These testis specific transcripts and the mRNA of mammalian LDH‐C show several properties in common, such as temporal correlation of expression, mRNA stability, and repression of premature translation. These observations suggest that the testis specific transcripts could perform during chicken spermatogenesis the functions of the LDH‐C mRNA in mammalian testis. J. Cell. Biochem. 79:15–27, 2000. © 2000 Wiley‐Liss, Inc.