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Vol. 9, Issue 2, 263-276, February 1998
Center for Research on Reproduction and Women's Health, Department
of Obstetrics and Gynecology, University of Pennsylvania Medical
Center, Philadelphia, Pennsylvania 19104-6080
Multiple isoforms of type 1 hexokinase (HK1) are transcribed during
spermatogenesis in the mouse, including at least three that are
presumably germ cell specific: HK1-sa, HK1-sb, and HK1-sc. Each of
these predicted proteins contains a common, germ cell-specific sequence
that replaces the porin-binding domain found in somatic HK1. Although
HK1 protein is present in mature sperm and is tyrosine phosphorylated,
it is not known whether the various potential isoforms are
differentially translated and localized within the developing germ
cells and mature sperm. Using antipeptide antisera against unique
regions of HK1-sa and HK1-sb, it was demonstrated that these isoforms
were not found in pachytene spermatocytes, round spermatids, condensing
spermatids, or sperm, suggesting that HK1-sa and HK1-sb are not
translated during spermatogenesis. Immunoreactivity was detected in
protein from round spermatids, condensing spermatids, and mature sperm
using an antipeptide antiserum against the common, germ cell-specific
region, suggesting that HK1-sc was the only germ cell-specific isoform
present in these cells. Two-dimensional SDS-PAGE suggested that all of
the sperm HK1-sc was tyrosine phosphorylated, and that the somatic HK1
isoform was not present. Immunoelectron microscopy revealed that HK1-sc was associated with the mitochondria and with the fibrous sheath of the
flagellum and was found in discrete clusters in the region of the
membranes of the sperm head. The unusual distribution of HK1-sc in
sperm suggests novel functions, such as extramitochondrial energy
production, and also demonstrates that a hexokinase without a classical
porin-binding domain can localize to mitochondria.
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