Glycosaminoglycans mediate the coacervation of human tropoelastin through dominant charge interactions involving lysine side chains
Glycosaminoglycans mediate the coacervation of human tropoelastin through dominant charge interactions involving lysine side chains
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DOI：
10.1074/jbc.274.31.21719
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发表时间：
1999-07-30
影响因子：
4.8
通讯作者：
Weiss, AS
中科院分区：
文献类型：
--
作者：
Wu, WJ;Vrhovski, B;Weiss, AS
Following cellular secretion into the extracellular matrix, tropoelastin is transported, deposited, and crosslinked to make elastin, Assembly by coacervation was examined for an isoform of tropoelastin that lacks the hydrophilic domain encoded by exon 26A It is equivalent to a naturally secreted form of tropoelastin and shows similar coacervation performance to its partner containing 26A, thereby generalizing the concept that splice form variants are able to coacervate under comparable conditions. This is optimal under physiological conditions of temperature, salt concentration, and pH, The proteins were examined for their ability to interact with extracellular matrix glycosaminoglycans. These negatively charged molecules interacted with positively charged lysine residues and promoted coacervation of tropoelastin in a temperature- and concentration-dependent manner. A testable model for elastin-glycosaminoglycan interactions is proposed, where tropoelastin deposition during elastogenesis is encouraged by local exposure to matrix glycosaminoglycans. Unmodified proteins are retained at similar to 3 mu M dissociation constant. Following lysyl oxidase modification of tropoelastin lysine residues, they are released from glycosaminoglycan interactions, thereby permitting those residues to contribute to elastin cross-links.
