REGULATION OF MORPHOLOGY AND GENE EXPRESSION BY THREE-DIMENTIONAL STRUCTURE OF TYPE I COLLAGEN FIBRILS IN CULTURED HEPATIC STELLATE CELLS

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Hepatic stellate cells (HSCs), vitamin A-storing cells located in the perisinusoidal spaces between the sinusoidal endothelial cell lining and the parenchymal cell cord, extend long cellular processes and surround hepatic sinusoids in vivo. However, when isolated and cultured in polystyrene dishes or in type I collagen coated dishes, HSCs lost vitamin A-containing lipid droplets and altesed to myofibroblast-like phenotype with well-developed stress fibers and without cellular processes. In this study, we examined a moiphological change and a differential gene expression by histological and differential display studies in HSCs cultured using type I collagen gel as a substratum. When cultured on type I collagen gel, HSCs exhibited an in vivo morphology with long cellular processes. The results from these studies suggest that HSCs were recognizable two- or three-dimensional stmcture of extiacellular type I collagen fibrils and induced to elongate their procsesses via intracellular signaling and microtubule reorganization. The lability of the processes to cold-treatment at 4 ℃ suggested that the elongated processes of HSCs were composed of a dendrite-type of mierotubules. We demonstrated the involvement of microtubule-associated protein 2 (MAP2) in process elongation in cultured HSCs by immunofluorescence staining and immunoblofting. MAP2 mRNA levels were quantified by real-time RT-PCR, indicating no increase in MAP2 mRNA level in HSCs cultured using type I collagen gel. Therefore, the MAP2 activity appeared to be posttranscnptionally regulated in cultured HSCs. The results from differential display analysis indicated that several mRNA species including transcription factor SP1, breast cancer resistant protein (BCRP), dystonin, and KIF-associated protein 3 (KAP3) were differentially regulated by extracellular type I collagen. Dystonin and KAP3 are known to be involved in cytoskeleton organization and function. Taken together, cell surface binding to extracellular type I collagen fibrils may trigger an alteration in expression of cytoskeleton-related proteins such as MAP2, dystonin, and KAP3, in association with reorganization of microtubule for process elongation.
日本結合組織学会の論文

REGULATION OF MORPHOLOGY AND GENE EXPRESSION BY THREE-DIMENTIONAL STRUCTURE OF TYPE I COLLAGEN FIBRILS IN CULTURED HEPATIC STELLATE CELLS

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