Subcellular distribution of laminin and prolactin in stimulated and blocked prolactin cells in the pituitary of lactating rats

• Published in: Cell and tissue research 1988-01, Vol.254 (3), p.617-627
• Main Authors: VILA-PORCILE, E, PICART, R, OLIVIER, L, TIXIER-VIDAL, A, TOUGARD, C
• Format: Article
• Language: English
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Female; Fundamental and applied biological sciences. Psychology; Glycoproteins; Immunohistochemistry; Lactation - metabolism; Laminin - metabolism; Microscopy, Electron; Pituitary Gland, Anterior - metabolism; Pituitary Gland, Anterior - ultrastructure; Pregnancy; Prolactin - metabolism; Proteins; Rats; Rats, Inbred Strains; Subcellular Fractions - metabolism
• ISSN: 0302-766X; 1432-0878
• DOI: 10.1007/BF00226512

Laminin (LAM), a glycoprotein component of basement membranes, has been previously detected within several subcellular compartments of prolactin (PRL) cells in the pituitary gland. The present work was aimed at comparing the subcellular localization of PRL, a specific secretory product, with that of LAM, in relation to the secretory activity of PRL cells. LAM and PRL were located in parallel, by ultrastructural immunocytochemistry, in PRL cells of lactating female Wistar rats, either stimulated by suckling, or blocked by weaning, or reactivated by suckle following short-term weaning. Variations in physiological conditions were correlated with a redistribution of PRL immunoreactivity within morphologically modified compartments. The Golgi apparatus became hypertrophied, and PRL impressively accumulated within saccules of the Golgi stacks of blocked cells. On the contrary, no apparent changes occurred in LAM distribution, at least at the Golgi level. Only a slight increase of LAM immunoreactivity was observed in rough endoplasmic reticulum after a long weaning period. PRL could be detected in most of the secretory granules and particularly in forming elements, whereas LAM was observable at the peripheral edge of some mature granules. Such a labeling was not markedly influenced by the physiological state. The prominent structures, indicative of crinophagic activity, characteristic of blocked cells, contained masses of dense material, which were always immunopositive with antibodies to PRL, but never to LAM. These observations could suggest that, in PRL cells, intracellular transport and exportation of LAM are controlled by mechanisms independent from those involved in the regulation of PRL secretion.