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Drug‐induced alterations in rat peritubular cell cytoskeleton result in proteoglycan synthesis modifications. Comparison with some intracellular signaling pathways
Author(s) -
Thiébot Bénédicte,
Bilinska Barbara,
Langris Monique,
Bocquet Jean,
Carreau Serge
Publication year - 1999
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1016/s0248-4900(99)80036-7
Subject(s) - cytoskeleton , biology , microbiology and biotechnology , proteoglycan , cytochalasin b , cytochalasin d , colchicine , protein kinase c , cytochalasin , microtubule , intracellular , nocodazole , cell , signal transduction , biochemistry , extracellular matrix , genetics
The influence of phorbol myristate acetate (PMA), dibutyryl cAMP and insulin‐like growth factor (IGF‐1) as well as cytoskeletal disrupting drugs on morphological changes has been studied in peritubular cells isolated from immature rat testis. Morphological studies were combined with immunofluorescence investigations of cytoskeletal elements and their rearrangements by various agents. The results were correlated with modulation of proteoglycan synthesis. Peritubular cells exposed to dibutyryl cAMP or cytochalasin D were transformed from flattened, fibroblast‐like into neuronal‐like morphology. In such cells, destruction of actin filaments was accompanied with a 50% decrease in cell‐associated proteoglycan synthesis as well as with oversulfation of total proteoglycans. On the contrary, peritubular cell shape has been slightly altered after addition of PMA, IGF‐1, vinblastine or colchicine. After these treatments, destruction or rearrangement of cytoskeletal elements was observed; cell‐layer proteoglycan synthesis remained either unchanged or increased while total proteoglycans were always undersulfated. IGF‐1, PMA and dibutyryl cAMP modified the peritubular cell morphology, cytoskeletal organization and proteoglycan production; the cytoskeleton disrupting drugs such as vinblastine, colchicine and cytochalasin D mimicked some of these effects. These observations suggest that alterations in proteoglycan biosynthesis, after activation of tyrosine kinase, protein kinase C and protein kinase A pathways might be mediated, at least in part, by the disorganization of the cytoskeleton structure.