Hoffman M, Faulkner K A, Iannone M A, Church F C
Department of Pathology, University of North Carolina School of Medicine, Chapel Hill.
Biochim Biophys Acta. 1991 Oct 16;1095(1):78-82. doi: 10.1016/0167-4889(91)90047-2.
The serine proteinase inhibitor heparin cofactor II (HC) can be cleaved by polymorphonuclear leukocyte (PMN) elastase (LE) to yield potent chemotactic activity for PMN and monocytes. In contrast to the bacterially-derived chemotaxin formyl-Met-Leu-Phe (fMLP), the HC-derived chemotaxin does not stimulate PMN degranulation or oxidative burst activity. We compared the effects of HC-derived chemotaxins to the effects of fMLP on PMN actin conformation and on the cAMP levels. Both the HC chemotaxins and fMLP rapidly induced an increase in F-actin which was similar in magnitude and time-course. However, in contrast to fMLP, HC-derived chemotaxins did not elevate cAMP levels. HC-derived chemotaxins may be useful probes of chemotactic responses, since they do not have the mixed biological activities of fMLP.
丝氨酸蛋白酶抑制剂肝素辅因子II（HC）可被多形核白细胞（PMN）弹性蛋白酶（LE）裂解，从而产生对PMN和单核细胞具有强大趋化活性的物质。与细菌衍生的趋化因子甲酰甲硫氨酰亮氨酰苯丙氨酸（fMLP）不同，HC衍生的趋化因子不会刺激PMN脱颗粒或氧化爆发活性。我们比较了HC衍生的趋化因子与fMLP对PMN肌动蛋白构象和cAMP水平的影响。HC趋化因子和fMLP均迅速诱导F-肌动蛋白增加，其幅度和时间进程相似。然而，与fMLP不同，HC衍生的趋化因子不会提高cAMP水平。由于HC衍生的趋化因子不具有fMLP的混合生物学活性，因此它们可能是趋化反应的有用探针。
