S. Reitinger et al., Xenopus kidney hyaluronidase-1 (XKH1), a novel type of membrane-bound hyaluronidase solely degrades hyaluronan at neutral pH, FEBS LETTER, 505(2), 2001, pp. 213-216
In search for Xenopus laevis hyaluronidase genes, a cDNA encoding a putativ
e PH-20-like enzyme was isolated. In the adult frog, this mRNA was only fou
nd to be expressed in the kidney and therefore named XKH1. When expressed b
y means of cRNA injection into frog oocytes, XKH1 solely exhibited at physi
ologic ionic strength hyaluronidase activity at neutral pH and in weakly ac
idic solutions. The enzyme was inactive below pH 5.4. In addition to hyalur
onic acid hydrolysis, chondroitin sulfate also was degraded at low yield as
assessed by fluorophore-assisted carbohydrate electrophoresis analysis of
the degradation products. The enzyme is sorted to the outer surface of the
cell membrane of XKH1 expressing oocytes. From there, it could not be remov
ed by phospholipase C nor was secreted hyaluronidase activity detectable. W
e conclude that XKH1 represents a membrane-bound hyaluronan-degrading enzym
e exclusively expressed in cells of the adult frog kidney where it either m
ay be involved in the reorganization of the extracellular architecture or i
n supporting physiological demands for proper renal functions. (C) 2001 Fed
eration of European Biochemical Societies. Published by Elsevier Science B.
V. All rights reserved.