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Journal of Histochemistry and Cytochemistry, Vol. 45, 805-814, Copyright © 1997 by The Histochemical Society, Inc.

ARTICLE

Modulation of Protein Kinases and Microtubule-associated Proteins and Changes in Ultrastructure in Female Rat Pituitary Cells: Effects of Estrogen and Bromocriptine

Akira Matsunoa,b, Susumu Takekoshib, Naoko Sannob,d, Hirotoshi Utsunomiyab, Yoshitaka Ohsugic, Nobuhito Saito, Hideaki Kanemitsue, Akira Tamurae, Tadashi Nagashimaa, R. Yoshiyuki Osamurab, and Keiichi Watanabeb
a Department of Neurosurgery, Teikyo University Ichihara Hospital, Ichihara City, Chiba, Japan
b Department of Pathology, Tokai University School of Medicine, Isehara City, Kanagawa, Japan
c Drug Safety Laboratory, Taiho Pharmaceutical Co., Ltd., Tokushima City, Tokushima, Japan
d Department of Neurosurgery, University of Tokyo Hospital, Tokyo, Japan
e Department of Neurosurgery, Teikyo University Hospital, Tokyo, Japan

Correspondence to: Akira Matsuno, Dept. of Neurosurgery, Teikyo Univ. Ichihara Hospital, 3426-3 Anegasaki, Ichihara City, Chiba 299-01, Japan.

This study focused on the intracellular signal transduction system and microtubule-associated proteins (MAPs), such as MAP-2 and Tau protein. The modulation of these proteins and their correlation with ultrastructural changes were investigated in rat pituitary prolactin (PRL) cells. Adult female Wistar rats were treated with estrogen and bromocriptine and their pituitary glands were removed for analysis of the expression of tubulin, MAP-2, Tau protein, protein kinase C (PKC), and calcium calmodulin (CaM) kinase. Western blot analysis showed that estrogen increased and bromocriptine decreased the expression of PKC{alpha}, ß1, ß2, CaM kinase {alpha}, ß, MAP-2, and Tau protein. MAP-2 and Tau protein, which are cytosolic proteins, being translated on free ribosomes, were associated with the membrane of whirling rough endoplasmic reticulum (RER) in estrogen-treated cells and dissociated with vesiculated RER induced by bromocriptine. These results suggested that the modulation of MAP-2 and Tau protein may reflect changes of PKC and CaM kinase, and that the quantitative changes and intracellular modulation of MAPs induced by estrogen and bromocriptine, i.e., estrogen-induced association and bromocriptine-induced dissociation of MAP-2 and Tau protein with membrane of RER, may reflect the dynamics of microtubules and are associated with structural changes in the RER and changes in the synthesis and intracellular transport of PRL. (J Histochem Cytochem 45:805-813, 1997)

Key Words: MAP-2, Tau protein, prolactin, rough endoplasmic reticulum, pituitary cell


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