Chondroitin sulfate synthase-2 is necessary for chain extension of chondroitin sulfate but not critical for skeletal development.

Chondroitin sulfate (CS) is a linear polysaccharide consisting of repeating disaccharide units of N-acetyl-D-galactosamine and D-glucuronic acid residues, modified with sulfated residues at various positions. Based on its structural diversity in chain length and sulfation patterns, CS provides speci...

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Autores principales: Hiroyasu Ogawa, Sonoko Hatano, Nobuo Sugiura, Naoko Nagai, Takashi Sato, Katsuji Shimizu, Koji Kimata, Hisashi Narimatsu, Hideto Watanabe
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Publicado: Public Library of Science (PLoS) 2012
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spelling oai:doaj.org-article:e931deb526c34021a508c3c9a0dcd4992021-11-18T07:07:19ZChondroitin sulfate synthase-2 is necessary for chain extension of chondroitin sulfate but not critical for skeletal development.1932-620310.1371/journal.pone.0043806https://doaj.org/article/e931deb526c34021a508c3c9a0dcd4992012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22952769/?tool=EBIhttps://doaj.org/toc/1932-6203Chondroitin sulfate (CS) is a linear polysaccharide consisting of repeating disaccharide units of N-acetyl-D-galactosamine and D-glucuronic acid residues, modified with sulfated residues at various positions. Based on its structural diversity in chain length and sulfation patterns, CS provides specific biological functions in cell adhesion, morphogenesis, neural network formation, and cell division. To date, six glycosyltransferases are known to be involved in the biosynthesis of chondroitin saccharide chains, and a hetero-oligomer complex of chondroitin sulfate synthase-1 (CSS1)/chondroitin synthase-1 and chondroitin sulfate synthase-2 (CSS2)/chondroitin polymerizing factor is known to have the strongest polymerizing activity. Here, we generated and analyzed CSS2(-/-) mice. Although they were viable and fertile, exhibiting no overt morphological abnormalities or osteoarthritis, their cartilage contained CS chains with a shorter length and at a similar number to wild type. Further analysis using CSS2(-/-) chondrocyte culture systems, together with siRNA of CSS1, revealed the presence of two CS chain species in length, suggesting two steps of CS chain polymerization; i.e., elongation from the linkage region up to Mr ∼10,000, and further extension. There, CSS2 mainly participated in the extension, whereas CSS1 participated in both the extension and the initiation. Our study demonstrates the distinct function of CSS1 and CSS2, providing a clue in the elucidation of the mechanism of CS biosynthesis.Hiroyasu OgawaSonoko HatanoNobuo SugiuraNaoko NagaiTakashi SatoKatsuji ShimizuKoji KimataHisashi NarimatsuHideto WatanabePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 8, p e43806 (2012)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Hiroyasu Ogawa
Sonoko Hatano
Nobuo Sugiura
Naoko Nagai
Takashi Sato
Katsuji Shimizu
Koji Kimata
Hisashi Narimatsu
Hideto Watanabe
Chondroitin sulfate synthase-2 is necessary for chain extension of chondroitin sulfate but not critical for skeletal development.
description Chondroitin sulfate (CS) is a linear polysaccharide consisting of repeating disaccharide units of N-acetyl-D-galactosamine and D-glucuronic acid residues, modified with sulfated residues at various positions. Based on its structural diversity in chain length and sulfation patterns, CS provides specific biological functions in cell adhesion, morphogenesis, neural network formation, and cell division. To date, six glycosyltransferases are known to be involved in the biosynthesis of chondroitin saccharide chains, and a hetero-oligomer complex of chondroitin sulfate synthase-1 (CSS1)/chondroitin synthase-1 and chondroitin sulfate synthase-2 (CSS2)/chondroitin polymerizing factor is known to have the strongest polymerizing activity. Here, we generated and analyzed CSS2(-/-) mice. Although they were viable and fertile, exhibiting no overt morphological abnormalities or osteoarthritis, their cartilage contained CS chains with a shorter length and at a similar number to wild type. Further analysis using CSS2(-/-) chondrocyte culture systems, together with siRNA of CSS1, revealed the presence of two CS chain species in length, suggesting two steps of CS chain polymerization; i.e., elongation from the linkage region up to Mr ∼10,000, and further extension. There, CSS2 mainly participated in the extension, whereas CSS1 participated in both the extension and the initiation. Our study demonstrates the distinct function of CSS1 and CSS2, providing a clue in the elucidation of the mechanism of CS biosynthesis.
format article
author Hiroyasu Ogawa
Sonoko Hatano
Nobuo Sugiura
Naoko Nagai
Takashi Sato
Katsuji Shimizu
Koji Kimata
Hisashi Narimatsu
Hideto Watanabe
author_facet Hiroyasu Ogawa
Sonoko Hatano
Nobuo Sugiura
Naoko Nagai
Takashi Sato
Katsuji Shimizu
Koji Kimata
Hisashi Narimatsu
Hideto Watanabe
author_sort Hiroyasu Ogawa
title Chondroitin sulfate synthase-2 is necessary for chain extension of chondroitin sulfate but not critical for skeletal development.
title_short Chondroitin sulfate synthase-2 is necessary for chain extension of chondroitin sulfate but not critical for skeletal development.
title_full Chondroitin sulfate synthase-2 is necessary for chain extension of chondroitin sulfate but not critical for skeletal development.
title_fullStr Chondroitin sulfate synthase-2 is necessary for chain extension of chondroitin sulfate but not critical for skeletal development.
title_full_unstemmed Chondroitin sulfate synthase-2 is necessary for chain extension of chondroitin sulfate but not critical for skeletal development.
title_sort chondroitin sulfate synthase-2 is necessary for chain extension of chondroitin sulfate but not critical for skeletal development.
publisher Public Library of Science (PLoS)
publishDate 2012
url https://doaj.org/article/e931deb526c34021a508c3c9a0dcd499
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