Elastase Digestion of Fibronectin Releases an Epiviosamine Peptide with Fibroblast Growth and Survival Activity.
Elastase Digestion of Fibronectin Releases an Epiviosamine Peptide with Fibroblast Growth and Survival Activity.
复制标题
纤维连接蛋白的弹性蛋白酶消化释放出具有成纤维细胞生长和存活活性的表维维胺肽。
DOI:
10.1016/j.jid.2018.04.023
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发表时间:
2018
期刊:
影响因子:
--
通讯作者:
Clark,RichardA
中科院分区:
文献类型:
--
作者:
Lin,Kevin;Lin,Fubao;Clark,RichardA
Degradation of extracellular matrix with enzymes such as neutrophil elastase and matrix metalloproteinase play an important role in inflammation (Cox et al., 2008, Tester et al., 2007) and tissue repair (Wells et al., 2016). During proteolysis, extracellular matrix proteins often release peptides that have different biological functions compared with their parent protein (Norris et al., 1982, Payne et al., 2017, Yi and Ruoslahti, 2001). These peptides can be beneficial or detrimental to tissue repair (Wells et al., 2016).Fibronectin (FN), a 500-kDa protein, is deposited with fibrin at sites of injury as a provisional matrix (Pankov and Yamada, 2002, Yamada and Clark, 1996) and produced in situ by activated tissue cells (Kubo et al., 1984, Singer et al., 1984). During burn injury, FN is deposited in the burn at the time of initial wounding but subject to extensive degradation by neutrophil elastase (Grinnell and Zhu, 1994). Previously, we showed that such fragments have chemotactic activity for human blood monocytes (Doherty et al., 1990, Norris et al., 1982).