共 113 条
Current understanding of the thrombospondin-1 interactome
被引:204
作者:
Resovi, Andrea
[1
]
Pinessi, Denise
[1
]
Chiorino, Giovanna
[2
]
Taraboletti, Giulia
[1
]
机构:
[1] IRCCS Ist Ric Farmacol Mario Negri, Dept Oncol, Tumor Angiogenesis Unit, I-24126 Bergamo, Italy
[2] Fonda Edo & Elvo Tempia Valenta, Lab Canc Genom, I-13900 Biella, Italy
来源:
关键词:
Thrombospondin-1;
Protein-protein interaction;
Growth factors;
Angiogenesis;
Matricellular proteins;
Domains;
BINDING COMPETITIVE INHIBITOR;
HISTIDINE-RICH GLYCOPROTEIN;
PROTEIN DISULFIDE-ISOMERASE;
ENDOTHELIAL-CELL RESPONSES;
VON-WILLEBRAND-FACTOR;
N-TERMINAL DOMAIN;
GROWTH-FACTOR;
PLATELET THROMBOSPONDIN;
EXTRACELLULAR-MATRIX;
IN-VITRO;
D O I:
10.1016/j.matbio.2014.01.012
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
The multifaceted action of thrombospondin-1 (TSP-1) depends on its ability to physically interact with different ligands, including structural components of the extracellular matrix, other matricellular proteins, cell receptors, growth factors, cytokines and proteases. Through this network, TSP-1 regulates the ligand activity, availability and structure, ultimately tuning the cell response to environmental stimuli in a context-dependent manner, contributing to physiological and pathological processes. Complete mapping of the TSP-1 interactome is needed to understand its diverse functions and to lay the basis for the rational design of TSP-1-based therapeutic approaches. So far, large-scale approaches to identify TSP-1 ligands have been rarely used, but many interactions have been identified in small-scale studies in defined biological systems. This review, based on information from protein interaction databases and the literature, illustrates current knowledge of the TSP-1 interactome map. (C) 2014 The Authors. Published by Elsevier B.V.
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页码:83 / 91
页数:9
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