Hyal2 -: less active, but more versatile?

被引:133
作者
Lepperdinger, G [1 ]
Müllegger, J [1 ]
Kreil, G [1 ]
机构
[1] Austrian Acad Sci, Inst Mol Biol, A-5020 Salzburg, Austria
关键词
hyaluronidase; Hyal2; hyaluronan; Xenopus development;
D O I
10.1016/S0945-053X(01)00170-6
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
Hyal2 is one of several hyaluronidases present in vertebrates. The human gene encoding this enzyme is present on chromosome 3p.21.3, close to two additional hyaluronidase genes. cDNAs encoding Hyal2 homologues have been characterized from mouse and Xenopus laevis. These enzymes hydrolyze high molecular mass hyaluronan to intermediates of approximately 20 kDa, a finding which implies that structural domains of this size exist in this polysaccharide which was mostly thought to be a random coil. Hyal2 enzymes have an acidic pH-optimum with an activity that is considerably lower than observed for other types of hyaluronidases. Originally considered to be a typical lysosomal enzyme, more recent evidence has shown that Hya12 proteins can also be exposed on the cell surface bound to the plasma membrane via a GPI anchor. Hyal2 is present in many tissues, one exception being the adult brain. In this tissue, the gene is silenced after birth by methylation. Current evidence about the role of Hya12 in tumor growth, inflammation and frog embryogenesis is discussed. (C) 2001 Elsevier Science B.V./International Society of Matrix Biology. All rights reserved.
引用
收藏
页码:509 / 514
页数:6
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