Chondroitinase-mediated degradation of rare 3-O-sulfated glucuronic acid in functional oversulfated chondroitin sulfate K and E

Chondroitin sulfate K (CS-K) from king crab cartilage rich in rare 3-O-sulfated glucuronic acid (GlcUA(3S)) displayed neuritogenic activity and affinity toward various growth factors like CS-E from squid cartilage. CS-K-mediated neuritogenesis of mouse hippocampal neurons in culture was abolished by...

Full description

Saved in:
Bibliographic Details
Main Authors: Fongmoon D., Shetty A.K., Basappa, Yamada S., Sugiura M., Kongtawelert P., Sugahara K.
Format: Article
Language:English
Published: 2014
Online Access:http://www.scopus.com/inward/record.url?eid=2-s2.0-37549032527&partnerID=40&md5=63e679b96476858eecf57c2e0d5c73e4
http://cmuir.cmu.ac.th/handle/6653943832/2081
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: Chiang Mai University
Language: English
id th-cmuir.6653943832-2081
record_format dspace
spelling th-cmuir.6653943832-20812014-08-30T02:00:27Z Chondroitinase-mediated degradation of rare 3-O-sulfated glucuronic acid in functional oversulfated chondroitin sulfate K and E Fongmoon D. Shetty A.K. Basappa Yamada S. Sugiura M. Kongtawelert P. Sugahara K. Chondroitin sulfate K (CS-K) from king crab cartilage rich in rare 3-O-sulfated glucuronic acid (GlcUA(3S)) displayed neuritogenic activity and affinity toward various growth factors like CS-E from squid cartilage. CS-K-mediated neuritogenesis of mouse hippocampal neurons in culture was abolished by digestion with chondroitinase (CSase) ABC, indicating the possible involvement of GlcUA(3S). However, identification of GlcUA(3S) in CS chains by conventional high performance liquid chromatography has been hampered by its CSase ABC-mediated degradation. To investigate the degradation process, an authentic CS-E tetrasaccharide, Δ4,5HexUA-GalNAc(4S)-GlcUA(3S)- GalNAc(4S), was digested with CSase ABC, and the end product was identified as GalNAc(4S) by electrospray ionization mass spectrometry (ESI-MS). Putative GalNAc(6S) and GalNAc(4S,6S), derived presumably from GlcUA(3S)-GalNAc(6S) and GlcUA(3S)-GalNAc(4S,6S), respectively, were also detected by ESI-MS in the CSase ABC digest of a CS-E oligosaccharide fraction resistant to CSases AC-I and AC-II. Intermediates during the CSase ABC-mediated degradation of Δ4,5HexUA(3S)-GalNAc(4S) to GalNAc(4S) were identified through ESI-MS of a partial CSase ABC digest of a CS-K tetrasaccharide, GlcUA(3S)-GalNAc(4S)-GlcUA(3S)-GalNAc(4S), and the conceivable mechanism behind the degradation of the GlcUA(3S) moiety was elucidated. Although a fucose branch was also identified in CS-K, defucosylated CS-K exhibited greater neuritogenic activity than the native CS-K, excluding the possibility of the involvement of fucose in the activity. Rather, (3S)-containing disaccharides are likely involved. These findings will enable us to detect GlcUA(3S)-containing disaccharides in CS chains to better understand CS-mediated biological processes. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc. 2014-08-30T02:00:27Z 2014-08-30T02:00:27Z 2007 Article 00219258 10.1074/jbc.M707082200 17951579 JBCHA http://www.scopus.com/inward/record.url?eid=2-s2.0-37549032527&partnerID=40&md5=63e679b96476858eecf57c2e0d5c73e4 http://cmuir.cmu.ac.th/handle/6653943832/2081 English
institution Chiang Mai University
building Chiang Mai University Library
country Thailand
collection CMU Intellectual Repository
language English
description Chondroitin sulfate K (CS-K) from king crab cartilage rich in rare 3-O-sulfated glucuronic acid (GlcUA(3S)) displayed neuritogenic activity and affinity toward various growth factors like CS-E from squid cartilage. CS-K-mediated neuritogenesis of mouse hippocampal neurons in culture was abolished by digestion with chondroitinase (CSase) ABC, indicating the possible involvement of GlcUA(3S). However, identification of GlcUA(3S) in CS chains by conventional high performance liquid chromatography has been hampered by its CSase ABC-mediated degradation. To investigate the degradation process, an authentic CS-E tetrasaccharide, Δ4,5HexUA-GalNAc(4S)-GlcUA(3S)- GalNAc(4S), was digested with CSase ABC, and the end product was identified as GalNAc(4S) by electrospray ionization mass spectrometry (ESI-MS). Putative GalNAc(6S) and GalNAc(4S,6S), derived presumably from GlcUA(3S)-GalNAc(6S) and GlcUA(3S)-GalNAc(4S,6S), respectively, were also detected by ESI-MS in the CSase ABC digest of a CS-E oligosaccharide fraction resistant to CSases AC-I and AC-II. Intermediates during the CSase ABC-mediated degradation of Δ4,5HexUA(3S)-GalNAc(4S) to GalNAc(4S) were identified through ESI-MS of a partial CSase ABC digest of a CS-K tetrasaccharide, GlcUA(3S)-GalNAc(4S)-GlcUA(3S)-GalNAc(4S), and the conceivable mechanism behind the degradation of the GlcUA(3S) moiety was elucidated. Although a fucose branch was also identified in CS-K, defucosylated CS-K exhibited greater neuritogenic activity than the native CS-K, excluding the possibility of the involvement of fucose in the activity. Rather, (3S)-containing disaccharides are likely involved. These findings will enable us to detect GlcUA(3S)-containing disaccharides in CS chains to better understand CS-mediated biological processes. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.
format Article
author Fongmoon D.
Shetty A.K.
Basappa
Yamada S.
Sugiura M.
Kongtawelert P.
Sugahara K.
spellingShingle Fongmoon D.
Shetty A.K.
Basappa
Yamada S.
Sugiura M.
Kongtawelert P.
Sugahara K.
Chondroitinase-mediated degradation of rare 3-O-sulfated glucuronic acid in functional oversulfated chondroitin sulfate K and E
author_facet Fongmoon D.
Shetty A.K.
Basappa
Yamada S.
Sugiura M.
Kongtawelert P.
Sugahara K.
author_sort Fongmoon D.
title Chondroitinase-mediated degradation of rare 3-O-sulfated glucuronic acid in functional oversulfated chondroitin sulfate K and E
title_short Chondroitinase-mediated degradation of rare 3-O-sulfated glucuronic acid in functional oversulfated chondroitin sulfate K and E
title_full Chondroitinase-mediated degradation of rare 3-O-sulfated glucuronic acid in functional oversulfated chondroitin sulfate K and E
title_fullStr Chondroitinase-mediated degradation of rare 3-O-sulfated glucuronic acid in functional oversulfated chondroitin sulfate K and E
title_full_unstemmed Chondroitinase-mediated degradation of rare 3-O-sulfated glucuronic acid in functional oversulfated chondroitin sulfate K and E
title_sort chondroitinase-mediated degradation of rare 3-o-sulfated glucuronic acid in functional oversulfated chondroitin sulfate k and e
publishDate 2014
url http://www.scopus.com/inward/record.url?eid=2-s2.0-37549032527&partnerID=40&md5=63e679b96476858eecf57c2e0d5c73e4
http://cmuir.cmu.ac.th/handle/6653943832/2081
_version_ 1681419791164768256