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From the * Department of Biochemistry, Molecular
Biology and Cell Biology, Northwestern University, Evanston, Illinois; and the
Laboratory of Reproductive and Developmental
Toxicology, National Institute of Environmental Health Sciences, National
Institutes of Health, Research Triangle Park, North Carolina.
| Correspondence to: Dr E. Goldberg, Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208 (e-mail: erv{at}northwestern.edu). |
Lactate dehydrogenase C (LDHC) was, to the best of our knowledge, the first
testis-specific isozyme discovered in male germ cells. In fact, this was
accomplished shortly before "isozymes or isoenzymes" became a
field of study. LDHC was detected initially in human spermatozoa and
spermatogenic cells of the testes by gel electrophoresis. Immunohistochemistry
was used to localize LDHC first in early-pachytene primary spermatocytes, with
an apparent increase in quantity after meiosis, to its final localization in
and on the principal piece of the sperm tail. After several decades of
biologic, biochemical, and genetic investigations, we now know that the
lactate dehydrogenase isozymes are ubiquitous in vertebrates, developmentally
regulated, tissue and cell specific, and multifunctional. Here, we will review
the history of LDHC and the work that demonstrates clearly that it is required
for sperm to accomplish their ultimate goal, fertilization.
Key words: Lactate dehydrogenase C, glycolysis, male fertility, sperm
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