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Gene Review

CHSY1  -  chondroitin sulfate synthase 1

Homo sapiens

Synonyms: CHSY, CSS1, ChSy-1, Chondroitin glucuronyltransferase 1, Chondroitin sulfate synthase 1, ...
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Disease relevance of CHSY1

  • The interaction between SStp, the transit peptide of the precursor protein to the small subunit of Rubisco (prSSU) and two Hsp70 molecular chaperones, Escherichia coli DnaK and pea (Pisum sativum) CSS1, was investigated in detail [1].

High impact information on CHSY1

  • Activation of Notch2 was down-regulated by CHSY1 siRNA treatment [2].
  • Modulating Notch signaling by CHSY1 via its DDD motif provides new insight into mechanisms of the interactions between myeloma cells and their bone marrow microenvironment [2].
  • And interestingly, Fringe domain in CHSY1 has this DDD motif [2].
  • RNA interference experiments with CHSY1 small interfering RNA (siRNA) reduced the amount of CHSY1 in the co-culture conditioned medium, and this was associated with a 6.25-fold increase in apoptotic myeloma cells over control co-cultures [2].
  • Here, we show that when myeloma plasma cells are co-cultured with osteoclasts, chondroitin synthase 1 (CHSY1) is the most significantly altered soluble, secreted protein present in the conditioned medium [2].

Biological context of CHSY1


Associations of CHSY1 with chemical compounds


Other interactions of CHSY1

  • However, the specific activity of CSS3 was much lower than that of CSS1 [3].
  • Both glucuronyltransferase and N-acetylgalactosaminyltransferase activities were observed when chondroitin, CS polymer, and their corresponding oligosaccharides were used as the acceptor substrates, but no polymerization reaction was observed as in the case of CSS1 [3].

Analytical, diagnostic and therapeutic context of CHSY1

  • Quantitative real time PCR analysis revealed that the transcript level of CSS3 was much lower than that of CSS1, although it was ubiquitously expressed in various human tissues [3].


  1. Identification of a Hsp70 recognition domain within the rubisco small subunit transit peptide. Ivey, R.A., Subramanian, C., Bruce, B.D. Plant Physiol. (2000) [Pubmed]
  2. Chondroitin synthase 1 is a key molecule in myeloma cell-osteoclast interactions. Yin, L. J. Biol. Chem. (2005) [Pubmed]
  3. Chondroitin sulfate synthase-3. Molecular cloning and characterization. Yada, T., Sato, T., Kaseyama, H., Gotoh, M., Iwasaki, H., Kikuchi, N., Kwon, Y.D., Togayachi, A., Kudo, T., Watanabe, H., Narimatsu, H., Kimata, K. J. Biol. Chem. (2003) [Pubmed]
  4. Molecular cloning of a chondroitin polymerizing factor that cooperates with chondroitin synthase for chondroitin polymerization. Kitagawa, H., Izumikawa, T., Uyama, T., Sugahara, K. J. Biol. Chem. (2003) [Pubmed]
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