Renin and cathepsin B in human pituitary lactotroph cells: an ultrastructural study

Renin, prorenin and cathepsin B were localized in human lactotrophs using immunoelectron microscopic techniques. Renin and prorenin were found in numerous cytoplasmic granules. Cathepsin B, a lysosomal enzyme known to be able to activate prorenin into renin, was also present in cytoplasmic granules...

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Bibliographic Details
Published in:Histochemistry 1989-01, Vol.91 (4), p.291-297
Main Authors: SAINT-ANDRE, J. P, ROHMER, V, PINET, F, ROUSSELET, M. C, BIGORGNE, J. C, CORVOL, P
Format: Article
Language:English
Subjects:
Adenoma - metabolism
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Cathepsins - metabolism
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Humans
Hydrolases
Immunohistochemistry
Pituitary Gland - metabolism
Pituitary Gland - pathology
Pituitary Neoplasms - metabolism
Renin - metabolism
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Summary:Renin, prorenin and cathepsin B were localized in human lactotrophs using immunoelectron microscopic techniques. Renin and prorenin were found in numerous cytoplasmic granules. Cathepsin B, a lysosomal enzyme known to be able to activate prorenin into renin, was also present in cytoplasmic granules of lactotrophs. The co-localization of renin and prolactin in the same secretory granules was demonstrated by double immunolabelling. Renin and cathepsin B were co-localized in some granules by the same technique. These results suggest a local activation of renin in the secretory granules of lactotrophs and support the hypothesis of a possible autocrine action of the renin-angiotensin system on prolactin release.
ISSN:0301-5564
1432-119X
DOI:10.1007/BF00493003