IMMUNOHISTOCHEMICAL LOCALIZATION OF THE CALCIUM CALMODULIN-DEPENDENT PROTEIN PHOSPHATASE, CALCINEURIN, IN THE MOUSE TESTIS - ITS UNIQUE ACCUMULATION IN SPERMATID NUCLEI
M. Moriya et al., IMMUNOHISTOCHEMICAL LOCALIZATION OF THE CALCIUM CALMODULIN-DEPENDENT PROTEIN PHOSPHATASE, CALCINEURIN, IN THE MOUSE TESTIS - ITS UNIQUE ACCUMULATION IN SPERMATID NUCLEI, Cell and tissue research, 281(2), 1995, pp. 273-281
Immunohistochemical localization of a calmodulin-dependent protein pho
sphatase, calcineurin, was studied in the mouse testis in relation to
previous observations showing that calmodulin is unusually rich in spe
rmatogenic stages from mid-pachytene spermatocytes to elongating sperm
atids. The antibodies raised against calcineurin from scallop testis r
eacted with subunit B, but not subunit A, of calcineurin isoforms from
mouse brain and testis. Indirect immunofluorescence using these antib
odies on the mouse testis revealed positive reactions only in the nucl
ei of round or elongating spermatids: calcineurin started to accumulat
e in nuclei from the acrosomal cap phase, peaked at the initial stage
of nuclear elongation, and decreased thereafter. There was almost no s
ignal in the cytoplasm; spermatogenic cells at other stages, including
spermatogonia, spermatocytes, mature sperm, and other somatic cells i
n the seminiferous tubules were totally negative. Immune-electron micr
oscopy gave the same result, on the basis of measuring the density of
immunogold particles. These results suggest a role for calcineurin in
remodeling of the nuclear chromatin in metamorphosing spermatids.