Mikolajczyk-Pawlinska J, Travis J, Potempa J
Department of Microbiology and Immunology, Institute of Molecular Biology, Jagiellonian University, Krakow, Poland.
FEBS Lett. 1998 Dec 4;440(3):282-6. doi: 10.1016/s0014-5793(98)01461-6.
Gingipains are the major cysteine proteinases synthesized by Porphyromonas gingivalis which, in soluble form, are able to initially convert IL-8 (77 amino acid residues) to a more potent species truncated at the amino terminus, followed by slow degradation and destruction of chemokine biological activity. In contrast, the same enzymes when associated with bacterial outer-membrane blebs (vesicles), instantly degrade this chemokine. This division of enhancing and inactivating activity between soluble and membrane-bound gingipains can cause the compartmentalization of pro- and anti-inflammatory reactions to distal and proximal positions from bacterial plaque, respectively, which may explain why, despite the massive neutrophil accumulation at periodontitis sites, there is no elimination of infection.
牙龈蛋白酶是牙龈卟啉单胞菌合成的主要半胱氨酸蛋白酶，其可溶形式能够首先将白细胞介素-8（77个氨基酸残基）转化为在氨基末端截短的更具活性的形式，随后缓慢降解并破坏趋化因子的生物活性。相比之下，相同的酶与细菌外膜泡（囊泡）结合时，会立即降解这种趋化因子。可溶性和膜结合型牙龈蛋白酶之间增强和失活活性的这种区分，可能分别导致促炎和抗炎反应在细菌菌斑的远端和近端区域分隔开来，这或许可以解释为什么尽管牙周炎部位有大量中性粒细胞聚集，但感染却未被清除。
