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Expression of a Glyceraldehyde 3-Phosphate Dehydrogenase Gene Specific to Mouse Spermatogenic Cells1
Author(s) -
Jeffrey E. Welch,
E. C. Schatte,
Deborah A. O’Brien,
Edward M. Eddy
Publication year - 1992
Publication title -
biology of reproduction
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.366
H-Index - 180
eISSN - 1529-7268
pISSN - 0006-3363
DOI - 10.1095/biolreprod46.5.869
Subject(s) - biology , spermiogenesis , microbiology and biotechnology , glyceraldehyde 3 phosphate dehydrogenase , northern blot , complementary dna , spermatid , messenger rna , gene , gene expression , germ cell , somatic cell , start codon , spermatogenesis , genetics , endocrinology
A cDNA clone encoding a putative glyceraldehyde 3-phosphate dehydrogenase (GAPD-S) protein specific to spermatogenic cells was isolated from a mouse spermatogenic cell expression library. The Gapd-s cDNA contained 1451 bp of transcribed sequence, including an ATG initiation codon and a poly(A) addition signal. The location of the Gapd-s initiation codon differed from that of other Gapd sequences, resulting in a germ cell GAPD-S protein predicted to contain 105 additional residues at the amino terminus. While GAPD is constitutively expressed in somatic tissues, Northern blot analysis demonstrated that a Gapd-s probe hybridized to a 1.5-kb transcript present only in the testis. The Gapd-s mRNA was first detected during postnatal development in the testes of 20-day-old mice, suggesting that gene expression begins shortly after the appearance of haploid round spermatids. Northern analysis of RNA from isolated mouse pachytene spermatocytes and spermatids confirmed that Gapd-s expression is confined to post-meiotic germ cells. GAPD has been previously proposed to be the key enzyme regulating glycolysis in isolated round spermatids. We hypothesize that the GAPD-S enzyme plays an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon.

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