Hyaluronan synthase 1 is an
enzyme that in humans is encoded by the HAS1gene.[5][6]
Structure
Hyaluronan or
hyaluronic acid (HA) is a high molecular weight unbranched
polysaccharide synthesized by a wide variety of organisms from bacteria to mammals, and is a constituent of the
extracellular matrix. It consists of alternating glucuronic acid and N-acetylglucosamine residues that are linked by beta-1-3 and beta-1-4 glycosidic bonds. HA is synthesized by membrane-bound
synthase at the inner surface of the plasma membrane, and the chains are extruded via ABC-transporter into the extracellular space.[7]
Function
It serves a variety of functions, including space filling, lubrication of
joints, and provision of a matrix through which cells can migrate. HA is actively produced during
wound healing and tissue repair to provide a framework for ingrowth of blood vessels and
fibroblasts. Changes in the serum concentration of HA are associated with inflammatory and degenerative
arthropathies such as
rheumatoid arthritis. In addition, the interaction of HA with the leukocyte receptor
CD44 is important in tissue-specific homing by
leukocytes, and overexpression of HA receptors has been correlated with tumor
metastasis. HAS1 is a member of the newly identified vertebrate gene family encoding putative hyaluronan synthases, and its amino acid sequence shows significant
homology to the hasA gene product of
Streptococcus pyogenes, a glycosaminoglycan synthetase (DG42) from Xenopus laevis, and a recently described murine hyaluronan synthase.[6]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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Adamia S, Crainie M, Kriangkum J, et al. (2003). "Abnormal expression of hyaluronan synthases in patients with Waldenstrom's macroglobulimenia". Semin. Oncol. 30 (2): 165–8.
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PMID12720129.
Suzuki K, Yamamoto T, Usui T, et al. (2004). "Expression of hyaluronan synthase in intraocular proliferative diseases: regulation of expression in human vascular endothelial cells by transforming growth factor-beta". Jpn. J. Ophthalmol. 47 (6): 557–64.
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10.1016/j.jjo.2003.09.001.
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Grskovic B, Pollaschek C, Mueller MM, Stuhlmeier KM (2006). "Expression of hyaluronan synthase genes in umbilical cord blood stem/progenitor cells". Biochim. Biophys. Acta. 1760 (6): 890–5.
doi:
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Kao JJ (2007). "The NF-kappaB inhibitor pyrrolidine dithiocarbamate blocks IL-1beta induced hyaluronan synthase 1 (HAS1) mRNA transcription, pointing at NF-kappaB dependence of the gene HAS1". Exp. Gerontol. 41 (6): 641–7.
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10.1016/j.exger.2006.04.003.
PMID16723203.
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Campo GM, Avenoso A, Campo S, et al. (2007). "TNF-alpha, IFN-gamma, and IL-1beta modulate hyaluronan synthase expression in human skin fibroblasts: synergistic effect by concomital treatment with FeSO4 plus ascorbate". Mol. Cell. Biochem. 292 (1–2): 169–78.
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