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Hyal2——活性较低,但功能更具多样性?

Hyal2--less active, but more versatile?

作者信息

Lepperdinger G, Müllegger J, Kreil G

机构信息

Institute of Molecular Biology, Austrian Academy of Sciences, Billrothstrasse 11, A-5020 Salzburg, Austria.

出版信息

Matrix Biol. 2001 Dec;20(8):509-14. doi: 10.1016/s0945-053x(01)00170-6.

Abstract

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 Hyal2 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 Hyal2 in tumor growth, inflammation and frog embryogenesis is discussed.

摘要

Hyal2是脊椎动物体内存在的几种透明质酸酶之一。编码这种酶的人类基因位于3号染色体p.21.3上,靠近另外两个透明质酸酶基因。已经从小鼠和非洲爪蟾中鉴定出编码Hyal2同源物的cDNA。这些酶将高分子量的透明质酸水解为大约20 kDa的中间体,这一发现表明这种多糖中存在这种大小的结构域,而这种多糖大多被认为是无规卷曲。Hyal2酶的最适pH为酸性,其活性明显低于其他类型的透明质酸酶。最初被认为是一种典型的溶酶体酶,最近的证据表明,Hyal2蛋白也可以通过糖基磷脂酰肌醇(GPI)锚定暴露在与质膜结合的细胞表面。Hyal2存在于许多组织中,成年大脑是一个例外。在这个组织中,该基因在出生后通过甲基化而沉默。本文讨论了目前关于Hyal2在肿瘤生长、炎症和青蛙胚胎发育中作用的证据。

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