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MODULATION IN NUCLEOSIDE DIPHOSPHATASE ACTIVITY OF MAMMOTROPHIC CELLS OF THE RAT ADENOHYPOPHYSIS DURING SECRETION

ROBERT E. SMITH 1 and MARILYN G. FARQUHAR 1

1 Department of Pathology, University of California School of Meaicine, San Francisco, California 94122 and Veterans Administration Hospital, Palo Alto, California 94304

The modulations in nucleoside diphosphatase (NDPase) activity which occur during protein secretion have been investigated in mammotrophic hormone-producing cells (MT) of the female rat adenohypophysis. Pituitaries were fixed by perfusion or immersion in glutaraldehyde, and nonfrozen sections were incubated for NDPase. Tissue was examined from lactating and estrogen-treated animals in which mammotrophic hormone secretion (MTH) is high and from postlactating rats in which secretion of MTH is suppressed. In all experimental groups, NDPase reaction product was found: (a) in Golgi cisternae, (b) around forming and mature secretion granules, (c) in pericapillary and intercellular spaces and (d) along the outer surface of endothelial and MT cell membranes. The staining intensity of both the intracellular and extracellular sites paralleled the level of MTH secretion; it was greatest after estrogen treatment, moderate during lactation and minimal in the postlactating animal. In animals given estrogen, the Golgi apparatus was increased in size and up to six successive cisternae along the concave Golgi face were filled with reaction product in virtually every cell. In postlactating animals, the Golgi apparatus was small, and there was only patchy staining of a few cisternae in some cells. From its location and fluctuations with secretion, it seems likely that NDPase activity may be associated with the condensation and/or discharge of secretory granules.

Submitted on September 16, 1969


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