Section 30
Chapter 29,613

A chemical and histochemical study on the significance of the nonspecific esterase activity in the adult rat testis

Niemi, M.; Härkönen, M.; Ikonen, M.

Endocrinology 79(2): 294-300


ISSN/ISBN: 0013-7227
PMID: 5950837
DOI: 10.1210/endo-79-2-294
Accession: 029612134

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In frozen sections of fresh and formol-calcium chloride fixed testes 2 functionally different types of nonspecific esterase activity can be demonstrated histochemically using various combinations of the substrates [alpha]-naphthyl acetate and indoxyl acetate and the inhibitor diethyl p-nitrophenyl phosphate (E600). The activity of the majority of interstitial cells (Leydig cells) can be visualized on fresh-frozen section with [alpha]-naphthyl acetate as substrate. This activity decreases markedly after hypophysectomy and is sensitive to 10-6 [image] concentration of the inhibitor. The Sertoli cells and a few of the interstitial cells (possibly macrophages), on the other hand, prefer indoxyl acetate as substrate and activity is demonstrable only in formalin-fixed frozen sections. It resists E600, and the number of cells exhibiting this E600-resistant activity increases greatly after hypophysectomy both in the seminiferous tubules and in the interstitium. In chemical quantitative determinations of testicular nonspecific esterase activity, a gonadotropin dependence is demonstrable only when p-nitrophenyl propionate is used as substrate. This activity is sensitive to E600 and can be only partly solubilized by homogenization and repeated freezing and thawing. On the other hand, when [beta]-naphthyl acetate is used as a substrate, stronger esterolytic activity is demonstrable. This is still increased by hypophysectomy due to an increased proportion of soluble lyoenzyme of the interstitial macrophages and the Sertoli cells.

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