Discovery of type IV collagen non-collagenous domains as novel integrin ligands and endogenous inhibitors of angiogenesis
Discovery of type IV collagen non-collagenous domains as novel integrin ligands and endogenous inhibitors of angiogenesis
复制标题
DOI：
10.1101/sqb.2002.67.255
复制
发表时间：
2002-01-01
期刊：
影响因子：
--
通讯作者：
Kalluri, R
中科院分区：
文献类型：
--
作者：
Kalluri, R
《冷泉港定量生物学研讨会》第六卷。2002年冷泉港实验室出版社0-87969-678-8/02。255膜(BM)是细胞外基质(ECM)分子的特殊网络，对于后生动物的发展至关重要(Paulsson 1992；Yurchenco and O‘Rear 1994；Timpl 1996；Li等人)。2002年)。在提供结构支持的同时，VBM也被推测为调节细胞行为。它的重塑，如VBM合成和降解所定义的，向细胞产生不同的信号(Bergers等人。2000年；科罗拉多州等人。2000年；Egeblad和Werb 2002年)。在一般意义上，BM是专门的ECM的薄层，为上皮细胞和内皮细胞的生长和居住提供支撑结构。此外，它们与肌肉纤维、脂肪团和周围神经密切相关。BM由大约50个不同的大分子组成；最丰富的分子是IV型胶原、层粘连蛋白、硫酸乙酰肝素蛋白多糖(Perlecans)、纤维连接蛋白和Nidogen(图1a)。BM分子相当大，具有自聚集形成高阶结构的能力(Yurchenco和O‘Rear，1994；Li等人。2002年；Yurchenco等人。2002年)。IV型胶原原通过末端和中间的三螺旋区域自结合，形成蜘蛛网般的支架结构，与层粘连蛋白网络相互作用，层粘连蛋白网络本身也具有钙结合蛋白。
Cold Spring Harbor Symposia on Quantitative Biology, Volume LXVII.© 2002 Cold Spring Harbor Laboratory Press 0-87969-678-8/02. 255 membranes (BM) are a specialized meshwork of extracellular matrix (ECM) molecules, which are crucial for the development of metazoans (Paulsson 1992; Yurchenco and O’Rear 1994; Timpl 1996; Li et al. 2002). Along with providing structural support, VBM is also speculated to modulate cell behavior. Its remodeling, as defined by VBM synthesis and degradation, generates disparate signals to the cells (Bergers et al. 2000; Colorado et al. 2000; Egeblad and Werb 2002). In a general sense, BM are thin layers of a specialized ECM that provide the supporting structure on which epithelial and endothelial cells grow and reside. In addition, they are closely associated with muscle fibers, fat mass, and peripheral nerves. BM are composed of about 50 different macromolecules; the most abundant molecules are type IV collagen, laminin, heparan sulfate proteoglycans (perlecans), fibronectin, and nidogen (Fig. 1A). BM molecules are quite large in molecular size and have the capacity to self-aggregate to form higher-order structures (Yurchenco and O’Rear 1994; Li et al. 2002; Yurchenco et al. 2002). Type IV collagen protomers self-associate via their ends and their middle triple helical regions to form a spider web scaffold-like structure that interacts with the laminin network, which by itself also has the ca-