Glycobiology Advance Access published online on May 19, 2007
Glycobiology, doi:10.1093/glycob/cwm051
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Glycosaminoglycans in Hydra magnipapillata (Hydrozoa, Cnidaria): demonstration of chondroitin in the developing nematocyst, sting organelle, and structural characterization of glycosaminoglycans
2 Department of Biochemistry, Kobe Pharmaceutical University, Higashinada-ku, Kobe 658-8558
3 Laboratory of Proteoglycan Signaling and Therapeutics, Hokkaido University Graduate School of Life Science, Sapporo 001-0021
4 Department of Developmental Genetics, National Institute of Genetics, Mishima 411-0801, Japan
1 To whom corresponding should be addressed: Laboratory of Proteoglycan Signaling and Therapeutics, Graduate School of Life Science, Hokkaido University, Frontier Research Center for Post-Genomic Science and Technology, Nishi 11-choume, Kita 21-jo, Kita-ku, Sapporo, Hokkaido 001-0021, Japan. Tel.: 81-(11)-706-9054; Fax: 81-(11)-706-9056; E-mail: k-sugar{at}sci.hokudai.ac.jp
Received on April 12, 2007; revised on May 1, 2007; accepted on May 5, 2007
The hydrazoan is the simplest organism whose movements are governed by the neuromuscular system, and its de novo morphogenesis can be easily induced by removing body parts. These features make the hydrazoan an excellent model for studying the regeneration of tissues in vivo, especially in the nervous system. Although glycosaminoglycans (GAGs) and proteoglycans have been implicated in the signaling functions of various growth factors and play critical roles in the development of the central nervous system, the isolation and characterization of GAGs from hydrazoans has never been reported. Here we characterized GAGs of Hydra. Immunostaining using anti-GAG antibodies showed chondroitin in the developing nematocyst, which is a sting organelle specific to cnidarians. The chondroitin or chondroitin sulfate (CS) proteoglycans might furnish an environment for assembling nematocyst components, and might themselves be components of nematocysts. Therefore, GAGs were isolated from Hydra and their structural features were examined. A considerable amount of CS, three orders of magnitude less heparan sulfate (HS), but no hyaluronan were found as in Caenorhabditis elegans. Analysis of the disaccharide composition of HS revealed glucosamine 2-N-sulfation, glucosamine 6-O-sulfation, and uronate 2-O-sulfation. CS contains not only nonsulfated and 4-O-sulfated GalNAc but also 6-O-sulfated GalNAc. The average molecular size of CS and HS was 110 and 10 kDa, respectively. It has also been established here that CS chains are synthesized on the core protein through the ubiquitous linkage region tetrasaccharide, suggesting that indispensable functions of the linkage region in the synthesis of GAGs have been conserved during evolution.
5 These authors contributed equally to this work.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  R. Lawrence, S. K. Olson, R. E. Steele, L. Wang, R. Warrior, R. D. Cummings, and J. D. Esko Evolutionary Differences in Glycosaminoglycan Fine Structure Detected by Quantitative Glycan Reductive Isotope Labeling J. Biol. Chem., November 28, 2008; 283(48): 33674 - 33684. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. A Deakin and M. Lyon A simplified and sensitive fluorescent method for disaccharide analysis of both heparan sulfate and chondroitin/dermatan sulfates from biological samples Glycobiology, June 1, 2008; 18(6): 483 - 491. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Kaneiwa, S. Yamada, S. Mizumoto, A. M. Montano, S. Mitani, and K. Sugahara Identification of a Novel Chondroitin Hydrolase in Caenorhabditis elegans J. Biol. Chem., May 30, 2008; 283(22): 14971 - 14979. [Abstract] [Full Text] [PDF]
|
|