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Secretory leukocyte protease inhibitor in wound healing potential applications in.doc

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Secretory leukocyte protease inhibitor in wound healing potential applications in

 PAGE \* MERGEFORMAT 14 Secretory leukocyte protease inhibitor in wound healing potential applications in [Abstract] secretory leukocyte protease inhibitor (SLPI) is a serine protease activity can combat a variety of 12kDa cationic protein, and its carboxyl terminus to inhibit chymotrypsin, pancreatic elastase and other aspects of the activity of amino-terminal have anti-bacterial, anti- fungi, and many other anti-retroviral activity. Recent studies found that, SLPI by proliferation, apoptosis, tissue remodeling, and other ways to control invasive micro-environment, which affect the healing process. In this paper, SLPI in wound healing may be part of the process and role are summarized below. [Keywords:] secretory leukocyte protease inhibitor; wound healing; proliferation Abstract: Secretory leukocyte protease inhibitor (SLPI) is a 12 kDa mucosal secretory protein that is identified as a potent inhibitor of various serine proteases.The active inhibitory sites for leukocyte proteases and elastase are located in C terminal domain, whereas, the activities of antibacterial , antifungal and antiretrovirus are found in N terminal domain.Recent studies suggest that SLPI modulates wound healing via the activities of proliferation, apoptosis, tissue remodelling.This review focuses on the possible approaches and functions of SLPI in the process of wound healing. Keywords:: secretory leukocyte protease inhibitor; wound healing; proliferation A secretory leukocyte protease inhibitor (SLPI) the basic characteristics of SLPI is a 12kDa size of the cationic protein, are endogenous immune-related proteins, stable in the acidic environment. SLPI is a 107 amino acids containing a single chain polypeptide [1], the carboxyl terminal domain (also known as acidic protein domain) with Trappin family protease binding region shared by the amino-terminal domain mediates the binding of heparin to form a reversible complex after its anti microbial activity. SLPI gene was

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