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The FASEB Journal, Vol 1, 60-66, Copyright © 1987 by The Federation of American Societies for Experimental Biology

RESEARCH COMMUNICATIONS

Properties and function of caltrin, the calcium-transport inhibitor of bull seminal plasma

JT San Agustin, P Hughes and HA Lardy

Indirect immunofluorescence studies with polyclonal antibodies show that caltrin binds to the plasma membrane over the acrosome and principal tail regions of bovine spermatozoa but not to the postacrosomal area or the midpiece. Calcium influx into bovine epididymal spermatozoa maintained in a simple salt medium containing DL- beta-hydroxybutyrate is prevented by caltrin freshly prepared from bovine seminal plasma through a procedure employing only gel permeation columns. Older preparations, on the other hand, enhance calcium uptake into these cells. Caltrin freshly prepared through a purification scheme that includes a cation exchanger only induces enhancement of calcium uptake into bovine epididymal spermatozoa maintained under identical conditions. It is postulated that early during sperm transit through the female reproductive tract, caltrin bound to the sperm plasma membrane protects the sperm cells from calcium influx. As the cells enter the oviduct where meeting with the egg could take place, factors present in the surrounding milieu may cause caltrin to change from an inhibitor to an enhancer of calcium uptake. The acrosome reaction and possibly hyperactivation, two components of capacitation that require calcium influx as an initial event, then take place.


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Copyright © 1987 by The Federation of American Societies for Experimental Biology.