Senior R M, Griffin G L, Mecham R P
J Clin Invest. 1980 Oct;66(4):859-62. doi: 10.1172/JCI109926.
Elastin-derived peptides, produced by digesting human aortic elastin and bovine ligament elastin with human neutrophil elastase, were tested for chemotactic activity. At 100 micrograms protein/ml, elastin digests were nearly as active for monocytes as saturating amounts of complement-derived chemotactic activity. Neutrophils and alveolar macrophages showed less response to elastin peptidces than did monocytes. Fractionation of the digests by gel filtration chromatography disclosed that maximal chemotactic activity eluted in fractions corresponding to 14,000-20,000 mol wt containing most of the desmosine cross-links in the digests. Whole human serum and rabbit anti-elastin immunoglobulin inhibited the chemotactic activity. Purified desmosine also showed chemotactic activity for monocytes, maximal at 10 nM. These findings suggest that elastin-degradation products enriched in cross-linking regions recruit inflammatory cells in vivo and that elastin proteolysis, characteristic of emphysema, may be a signal for recruitment of mononuclear phagocytes into the lungs.
用人类中性粒细胞弹性蛋白酶消化人主动脉弹性蛋白和牛韧带弹性蛋白所产生的弹性蛋白衍生肽，被检测了趋化活性。在蛋白质浓度为100微克/毫升时，弹性蛋白消化产物对单核细胞的趋化活性几乎与饱和量的补体衍生趋化活性相当。中性粒细胞和肺泡巨噬细胞对弹性蛋白肽的反应比单核细胞小。通过凝胶过滤色谱法对消化产物进行分级分离发现，最大趋化活性在对应于分子量为14,000 - 20,000的级分中洗脱出来，这些级分包含消化产物中的大部分锁链素交联结构。全人血清和兔抗弹性蛋白免疫球蛋白抑制了趋化活性。纯化的锁链素对单核细胞也显示出趋化活性，在10纳摩尔时活性最大。这些发现表明，富含交联区域的弹性蛋白降解产物在体内招募炎症细胞，并且肺气肿所特有的弹性蛋白蛋白水解可能是单核吞噬细胞被招募到肺部的一个信号。
