| First Author | Bunch DO | Year | 1998 |
| Journal | Biol Reprod | Volume | 58 |
| Issue | 3 | Pages | 834-41 |
| PubMed ID | 9510974 | Mgi Jnum | J:46074 |
| Mgi Id | MGI:1197102 | Doi | 10.1095/biolreprod58.3.834 |
| Citation | Bunch DO, et al. (1998) Glyceraldehyde 3-phosphate dehydrogenase-S protein distribution during mouse spermatogenesis. Biol Reprod 58(3):834-41 |
| abstractText | The spermatogenic cell-specific isoform of glyceraldehyde 3-phosphate dehydro-genase (GAPD-S) may regulate glycolysis and energy production required for sperm motility. Although the steady-state level of Gapd-s mRNA is maximal at step 9 of mouse spermatogenesis, GAPD-S protein was not detected by immunohistochemistry until steps 12-13. This result suggests that Gapd-s is translationally regulated. Western blot analysis of isolated germ cells confirmed that GAPD-S is not detected in pachytene sperm-atocytes or round spermatids. A major immunoreactive protein migrating with a molecular weight (M(r)) of 69,200 was observed in condensing spermatids and cauda sperm. Addi-tional minor proteins that migrated at M(r) 55,200, 32,500, and 27,500 were detected in sperm. The molecular weight of GAPD-S is higher than the predicted molecular weight of 47,445, apparently due to a proline-rich 105-amino acid domain at the N-terminus. Recombinant GAPD-S protein lacking the proline-rich region migrated at M(r) 38,250, comparably to somatic GAPD, which also lacks the proline-rich domain. Indirect immuno-fluorescence demonstrated that GAPD-S is restricted to the principal piece in the sperm flagellum. Western blot analysis indicated that GAPD-S is tightly associated with the fibrous sheath of the flagellum, consistent with a potential role in regulating sperm motility. |
