Processing of seminal plasma hCAP-18 to ALL-38 by gastricsin - A novel mechanism of generating antimicrobial peptides in vagina
Processing of seminal plasma hCAP-18 to ALL-38 by gastricsin - A novel mechanism of generating antimicrobial peptides in vagina
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DOI：
10.1074/jbc.m301608200
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发表时间：
2003-08-01
影响因子：
4.8
通讯作者：
Borregaard, N
中科院分区：
文献类型：
--
作者：
Sorensen, OE;Gram, L;Borregaard, N
人cathelicidin，hCAP-18，在中性粒细胞和上皮细胞中表达。hCAP-18在中性粒细胞中被蛋白酶3加工成抗菌肽LL-37。hCAP-18在附睾中高度表达，随后在精浆中高浓度，其中蛋白质以其未加工和抗微生物无活性的形式存在。我们在这里报告，hCAP-18在精浆中的处理，以产生一个38个氨基酸的抗菌肽ALL-38的前列腺衍生的蛋白酶胃泌素孵育时，在相应的pH值阴道pH值。根据这一点，精浆衍生的hCAP-18被发现在其处理后的形式在阴道性交。ALL-38对多种测试微生物的抗微生物活性与LL 37的抗微生物活性相等。在暴露于阴道环境后，精浆中的前抗菌物质的这种酶促活化代表了一种预防性交后感染的新机制。
The human cathelicidin, hCAP-18, is expressed both in neutrophils and in epithelial cells. hCAP-18 is processed to the antimicrobial peptide LL-37 by proteinase 3 in neutrophils. hCAP-18 is highly expressed in the epididymis with a subsequent high concentration in seminal plasma where the protein is present in its unprocessed and antimicrobially inactive form. We report here that hCAP-18 in seminal plasma is processed to generate a 38-amino acid antimicrobial peptide ALL-38 by the prostate-derived protease gastricsin when incubated at a pH corresponding to the vaginal pH. In accordance with this, seminal plasma derived hCAP-18 was found in its processed form in the vagina following sexual intercourse. The antimicrobial activity of ALL-38 against a variety of microorganisms tested is equal to that of LL37. This enzymatic activation of a proantimicrobial substance in seminal plasma following exposure to the vaginal milieu represents a novel mechanism to prevent infection following sexual intercourse.