Gametes contain angiotensin converting enzyme (kininase II)

Summary The localization of angiotensin converting enzyme (ACE) in the gonads of the normal rabbit was studied by immunofluorescence and immunoelectron microscopy. The enzyme is present in the cytoplasm of testicular spermatids and of epididymal and ejaculated spermatozoa, and on the surface of follicular and tubal cocytes. These findings support the hypothesis that ACE has a role in gamete maturation and in fertilization.Acknowledgments. This study was supported by NIH grant AM36807 and by grants from the American Heart Association, the Joe and Emily Lowe Foundation, and the Dana Foundation. We thank L. Fernandez, B. Luders, I. Pawlowski, and K. Schwegler for technical assistance.     

Gametes contain angiotensin converting enzyme (kininase II)

The localization of angiotensin converting enzyme (ACE) in the gonads of the normal rabbit was studied by immunofluorescence and immunoelectron microscopy. The enzyme is present in the cytoplasm of testicular spermatids and of epididymal and ejaculated spermatozoa, and on the surface of follicular and tubal oocytes. These findings support the hypothesis that ACE has a role in gamete maturation and in fertilization.     

Levamisole inhibits mineral mobilisation,lactate production and lysosomal enzyme release from cultured bones

Summary Levamisole added to cultured calvarial bones inhibited spontaneous bone resorption, as indicated by reduced release of calcium and inorganic phosphate to the medium. In addition, levamisole reduced lactate production and release of lysosomal enzymes.     

Levamisole inhibits mineral mobilisation, lactate production and lysosomal enzyme release from cultured bones.

Levamisole added to cultured calvarial bones inhibited spontaneous bone resorption, as indicated by reduced release of calcium and inorganic phosphate to the medium. In addition, levamisole reduced lactate production and release of lysosomal enzymes.     

The bisphosphonates HEBP and AHPrBP but not AHBP inhibit mineral mobilization and lysosomal enzyme release from mouse calvarial bones in tissue culture

The effect of 3 bisphosphonates, 1-hydroxyethylidene-1, 1-bisphosphonate (HEBP), 3-amino-1-hydroxy-propylidene-1, 1-bisphosphonate (AHPrBP) and azacycloheptylidene-2, 2-bisphosphonate (AHBP), on the release of minerals (40Ca, 45Ca, Pi) and enzymes from cultured mouse calvaria was investigated in an organ culture system. HEBP and AHPrBP reduced PTH-stimulated mobilization of calcium and inorganic phosphate without affecting the release of lactate dehydrogenase. In contrast, no significant effect by AHBP on mineral mobilization and lysosomal enzyme release could be registered. In parallel with inhibited mineral mobilization, HEBP and AHPrBP inhibited the release of the lysosomal enzyme beta-glucuronidase. A possible cellular mechanism of action of bisphosphonates is discussed in the light of these data.     

The bisphosphonates HEBP and AHPrBP but not AHBP inhibit mineral mobilization and lysosomal enzyme release from mouse calvarial bones in tissue culture

Summary Mice injected with DSP-4 [N-(2-chloroethyl)-N-ethyl-2-bromobenzylamine], a selective noradrenergic neurotoxin, had marked depletions of central noradrenaline and an attenuated post-decapitation reflex. DSP-4-treated mice exhibited an increased sensitivity to the ₂-adrenoceptor agonist clonidine as measured by inhibition of the pinna reflex, but normal sensitivity as measured by hypothermia. This differential sensitivity may reflect the presence of supersensitive postsynaptic ₂-adrenoceptors in some, but not all, CNS regions after DSP-4 treatment.Acknowledgments. The authors gratefully acknowledge the excellent technical assistance of Mr P. E. Richards. DSP-4 hydrochloride and clonidine hydrochloride were synthesized by Beecham Pharmaceuticals Research Division.