Inhibition of lactate dehydrogenase C4 (LDH-C4) blocks capacitation of mouse sperm in vitro

@article{Duan2003InhibitionOL,
  title={Inhibition of lactate dehydrogenase C4 (LDH-C4) blocks capacitation of mouse sperm in vitro},
  author={Chenying Duan and Erwin Goldberg},
  journal={Cytogenetic and Genome Research},
  year={2003},
  volume={103},
  pages={352 - 359}
}
Lactate dehydrogenase C4 (LDH-C4) is a tissue-specific enzyme in the mammalian testis and the only lactate dehydrogenase isozyme of sperm. Inhibitors of LDH activity were used to determine whether this enzyme plays a role in sperm capacitation, the acrosome reaction and/or fertilization. Oxamate or its derivative was used to inhibit sperm LDH activity in a medium promoting capacitation. Complete inhibition of LDH activity blocked capacitation. This effect could be reversed partially by the… Expand
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References

SHOWING 1-10 OF 56 REFERENCES
Lactate dehydrogenase isoenzymes of sperm cells and testes
TLDR
The findings described are consistent with the idea that LDHx is different from other known lactate dehydrogenase isoenZymes, but that it has a metabolic function similar to that of the isoenzymes of other tissues. Expand
Preparation and characterization of monoclonal antibodies against sperm-specific lactate dehydrogenase C4.
TLDR
Results showed that all monoclonal antibodies were specific to LDH-C4 only: they did not react withLDH-1-5 from mice, nor from humans, and most of the antibodies belonged to the Ig G class. Expand
Intracellular localization of the testicular and sperm-specific lactate dehydrogenase isozyme C4 in mice.
TLDR
Postembedding immunocytochemistry at ultrastructural level was performed on testes, epididymal spermatozoa, and isolated testicular mitochondria, confirming previous findings, gathered by indirect methods, indicating a dual localization of LDH C4 in the cytosol of spermatocytes, sperMatids, and spermatozosa, as well as in the matrix of sperm-type mitochondria. Expand
Properties of pyruvate kinase and flagellar ATPase in rabbit spermatozoa: relation to metabolic strategy of the sperm cell.
TLDR
Rabbit spermatozoa have a metabolic strategy which is very similar to muscle cells, which suggests that the major use of the sperm cell's metabolic machinery is maintenance of energy for the contractile work of motility and that only minor amounts of metabolic energy appear to be consumed in other reactions, including those involved in fertilization. Expand
Functional Relationships between Capacitation-dependent Cell Signaling and Compartmentalized Metabolic Pathways in Murine Spermatozoa*
TLDR
The hypothesis that ATP specifically produced by a compartmentalized glycolytic pathway in the principal piece of the flagellum, as opposed to ATP generated by mitochondria in the mid-piece, is strictly required for protein tyrosine phosphorylation events that take place during sperm capacitation is supported. Expand
Epitopes of human testis-specific lactate dehydrogenase deduced from a cDNA sequence.
TLDR
The sequence and structure of human testis-specific L-lactate dehydrogenase has been derived from analysis of a complementary DNA (cDNA) clone comprising the complete protein coding region of the enzyme, and the deduced amino acid sequence is as different from rodent LDHC4 as it is from human LDHA4 and porcine LDHB4. Expand
Glyceraldehyde 3-phosphate dehydrogenase is bound to the fibrous sheath of mammalian spermatozoa.
TLDR
The inverse compartmentation of the glycolytic enzyme and mitochondria in the mammalian sperm flagella suggests that ATP-production in the principal piece mainly occurs by Glycolysis and in the midpiece by respiration. Expand
Regulation, localization, and anchoring of protein kinase A subunits during mouse sperm capacitation.
TLDR
It is demonstrated in this report that capacitation of cauda epididymal mouse sperm in vitro was accompanied by a time-dependent increase in PK-A activity, and cAMP is a key intermediary second messenger in regulating protein tyrosine phosphorylation and capacitation. Expand
Properties of the testicular lactate dehydrogenase isoenzyme.
TLDR
LDH isoenzyme X from all species showed greater ability than the other isoenzymes to catalyse the NAD+-linked interconversions of 2-oxobutanoate into 2-hydroxybutanoate and of 3-hydroxypentanoate, and a possible functional role for LDH isenzyme X could integrate a shuttle system transferring reducing equivalents from cytoplasm to mitochondria. Expand
Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway.
TLDR
Up-regulation of protein tyrosine phosphorylation by cAMP/PKA in sperm is, to the authors' knowledge, the first demonstration of such an interrelationship between tyrosin kinase/phosphatase and PKA signaling pathways. Expand
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