Abstract
As part of a study to elucidate the involvement of G proteins in signal transduction in testicular cells, we have examined the cellular localization of G q/11 within the seminiferous tubules. The somatic cells (Sertoli cells, peritubular cells) contain high amounts of both G q/11α mRNA and immunoreactive protein. In contrast, very low levels of these G proteins and the corresponding mRNAs are present in the germ cells (pachythene spermatocytes, round spermalids). Thus, in the germ cells, receptor-regulated inositol phospholipid hydrolysis is not likely to be regulated via G p/11, but rather through the G o protein, which has been previously shown to be abundant in rat germ cells. Since the somatic cells are nearly devoid of G o, the Gpp(NH)p-stimulated phospholipase C in these cells is probably regulated by G q and/or g 11.
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