Glycobiology, Vol 9, 887-895, Copyright © 1999 by Oxford University Press
A Seko, K Kitajima, T Iwamatsu, Y Inoue and S Inoue
Two different types of peptide:N-glycanase (PNGase) were identified in
developing embryos of medaka fish ( Oryzias latipes ). Because the optimum
pH values for their activities were acidic and neutral, they were
designated as acid PNGase M and neutral PNGase M, respectively. The acid
PNGase M corresponded to the enzyme that had been partially purified from
medaka embryos (Seko,A., Kitajima,K., Inoue,Y. and Inoue,S. (1991) J. Biol.
Chem., 266, 22110-22114). The apparent molecular weight of this enzyme was
150 K, and the optimal pH was 3.5- 4.0, and the K m for L-hyosophorin was
44 &mgr;M. L-Hyosophorin is a cortical alveolus-derived
glycononapeptide with a large N-linked glycan chain present in the
perivitelline space of the developing embryo. Acid PNGase M was
competitively inhibited by a free de-N-glycosylated nonapeptide derived
from L-hyosophorin. This enzyme was expressed in ovaries and embryos at all
developmental stages after gastrulation, but activity was not detected in
embryos at developmental stages between fertilization and gastrula. Several
independent lines of evidence suggested that acid PNGase M may be
responsible for the unusual accumulation of free N-glycans derived from
yolk glycoproteins (Iwasaki,M., Seko,A., Kitajima,K., Inoue,Y. and Inoue,S.
(1992) J. Biol. Chem., 267, 24287-24296). In contrast, the neutral PNGase M
was expressed in blastoderms from the 4-8 cell stage and in cells up to
early gastrula. The general significance of these findings is that they
show a developmental stage-dependent expression of the two PNGase
activities, and that expression of the neutral PNGase M activity occurs
concomitantly with the de-N-glycosylation of L-hyosophorin. These data thus
support our conclusion that the neutral PNGase M is responsible for the
developmental-stage-related de-N-glycosylation of theL- hyosophorin.
ORIGINAL ARTICLES
Identification of two discrete peptide: N-glycanases in oryzias latipes during embryogenesis
Department of Biochemistry, Sasaki Institute, Kanda-Surugadai, Chiyoda- ku, Tokyo 101-0062, Japan, Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan, D.
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