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ID 253
Title Transcription
マトリセルラー タンパクシツ Matricellular proteins ノ キノウ : トロンボスポンジン オ チュウシン トシテ
Title Alternative
Functions of Matricellular Proteins in Cell-extracellular Matrix Interactions and Signaling : Focus on Thrombospondins
Author
Ueno, Akemichi Department of Hygiene Chemistry, School of Pharmaceutical Sciences, Ohu University
Keywords
細胞外マトリックス(ECM)
マトリセルラータンパク質
トロンボスポンジン(TSP)1,2
多機能タンパク質
細胞接着
マトリックス石灰化
Content Type
Departmental Bulletin Paper
Description
Matricellular proteins, components of the extracellular matrix (ECM) with no directly structural roles in the ECM, are expressed primarily during development and response to injury, but not abundant in the normal adults, except in tissues with continued turnover, such as bone. Members of this class including osteonectin, thrombospondin 1 (TSP1), thrombospondin 2 (TSP2), osteopontin, and tenascin-C serve as biological mediators of cell function by interacting directly with cells or by modulating the activity of growth factors, cytokines, proteases, and other extracellular macromolecules. In addition, matricellular proteins mediate cellular de-adhesion, which refers to a reversal of the adhesive process involving the transition from a strongly adherent state with focal adhesions and stress fibers to an intermediate state of adherence. The proteins stimulate reorganization of actin stress fibers and disassembly of focal adhesion complexes but maintain a spread cell shape, while employing each unique array of signaling. The adhesive state undergoes modulation in tissue remodeling during morphogenesis and wound healing, cellular metaplasia and proliferation, and tumor metastasis. Although matricellular protein-null mice are apparently normal possibly due to redundancy of these proteins, on more careful scrutiny they display some abnormalities in collagen fibril assembly, vascular morphology or density, and connective tissue organization that are often magnified under pathological conditions. In this review, TSP1 and TSP2 showing differential spatiotemporal expression in the developing skeleton will be mainly discussed in the context of mineralizing cell biology. TSP1 accumulates in both predentin and osteoid between mineralized and unmineralized tissues, whereas TSP2 acts an autocrine inhibitor of marrow stromal cell proliferation. In particular, it is clear that high levels of TSP1 inhibit pathophysiological mineralization and contribute to calcified tissue homeostasis in response to aging and remodeling as an interface molecule.
Journal Title
四国歯学会雑誌
ISSN
09146091
NCID
AN10050046
Volume
18
Issue
2
Start Page
203
End Page
210
Sort Key
203
Published Date
2006-01
Remark
公開日:2010年1月24日で登録したコンテンツは、国立情報学研究所において電子化したものです。
FullText File
language
jpn
Report Type
総説