A novel human serum lectin with collagen- and fibrinogen-like domains that functions as an opsonin

被引:284
作者
Matsushita, M
Endo, Y
Taira, S
Sato, Y
Fujita, T
Ichikawa, N
Nakata, M
Mizuochi, T
机构
[1] FUKUSHIMA MED COLL,DEPT BIOCHEM,FUKUSHIMA 96012,JAPAN
[2] TOKAI UNIV,DEPT APPL CHEM,BIOMED CHEM LAB,HIRATSUKA,KANAGAWA 25912,JAPAN
关键词
D O I
10.1074/jbc.271.5.2448
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Collectins are C-type animal lectins with both collagenous and carbohydrate recognition domains and are involved in the first line host defense against pathogens, We report here a novel Ca2+-dependent and GlcNAc-binding lectin consisting of subunits of 35 kDa (P35) with a collagen-like sequence, When P35 is isolated from human serum, it forms a homopolymer by means of intermolecular disulfide bonding, as is the case with collectins, P35 cDNA was cloned from a human liver cDNA library, and the deduced amino acid sequence of 313 residues revealed that the mature form of P35 consists mainly of collagen- and fibrinogen-like domains, The latter contained two potential Ca2+-binding sites that may be involved in carbohydrate binding, The overall sequence of P35 was highly homologous to porcine ficolins alpha and beta. Northern blots of various human tissues showed that the major product of the 1.3-kilobase-long P35 transcript is expressed in liver, P35 enhanced phagocytosis of Salmonella typhimurium by neutrophils, suggesting an opsonic effect via the collagen region, P35 was found to bind to GlcNAc-conjugated bovine serum albumin, a neoglycoprotein, as web as to neoglycolipids containing complex-type oligosaccharides derived from glycoproteins, suggesting that P35 recognizes GlcNAc residues such as those found in microbial glycoconjugates and complex-type oligosaccharides. Therefore, P35 represents a new type of GlcNAc-binding lectin with structural and functional similarities to collectins involved in innate immunity.
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页码:2448 / 2454
页数:7
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