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'''Hyaluronan synthase 2''' is an [[enzyme]] that in humans is encoded by the ''HAS2'' [[gene]].<ref name="pmid9169154">{{cite journal |vauthors=Spicer AP, Seldin MF, Olsen AS, Brown N, Wells DE, Doggett NA, Itano N, Kimata K, Inazawa J, McDonald JA | title = Chromosomal localization of the human and mouse hyaluronan synthase genes | journal = Genomics | volume = 41 | issue = 3 | pages = 493–7 |date=Jul 1997 | pmid = 9169154 | pmc =  | doi = 10.1006/geno.1997.4696 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HAS2 hyaluronan synthase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3037| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Hyaluronan synthase 2
| HGNCid = 4819
| Symbol = HAS2
| AltSymbols =; MGC126241; MGC126242
| OMIM = 601636
| ECnumber = 
| Homologene = 3892
| MGIid = 107821
| GeneAtlas_image1 = PBB_GE_HAS2_206432_at_tn.png
| Function = {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}} {{GNF_GO|id=GO:0016758 |text = transferase activity, transferring hexosyl groups}} {{GNF_GO|id=GO:0050501 |text = hyaluronan synthase activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process =  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3037
    | Hs_Ensembl = ENSG00000170961
    | Hs_RefseqProtein = XP_001128807
    | Hs_RefseqmRNA = XM_001128807
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 8
    | Hs_GenLoc_start = 122694719
    | Hs_GenLoc_end = 122722811
    | Hs_Uniprot = Q92819
    | Mm_EntrezGene = 15117
    | Mm_Ensembl = ENSMUSG00000022367
    | Mm_RefseqmRNA = NM_008216
    | Mm_RefseqProtein = NP_032242
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 15
    | Mm_GenLoc_start = 56497742
    | Mm_GenLoc_end = 56512287
    | Mm_Uniprot = Q68EF7
  }}
}}
'''Hyaluronan synthase 2''', also known as '''HAS2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HAS2 hyaluronan synthase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3037| accessdate = }}</ref>


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{{PBB_Summary
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| section_title =  
| section_title =  
| summary_text = 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 through pore-like structures into the extracellular space.  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.  HAS2 is a member of the newly identified vertebrate gene family encoding putative hyaluronan synthases, and its amino acid sequence shows significant homology to glycosaminoglycan synthetase (DG42) from Xenopus laevis, and human and murine hyaluronan synthase 1.<ref name="entrez">{{cite web | title = Entrez Gene: HAS2 hyaluronan synthase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3037| accessdate = }}</ref>
| summary_text = Hyaluronan or hyaluronic acid 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.  Hyaluronic acid is synthesized by membrane-bound synthase at the inner surface of the plasma membrane, and the chains are extruded via ABC-Transporter<ref>Schulz,T.; Schumacher,U.; Prehm,P. Hyaluronan export by the ABC transporter MRP5 and its modulation by intracellular cGMP. J.Biol.Chem.282,20999-21004
</ref> into the extracellular space.  It serves a variety of functions, including space filling, lubrication of joints, and provision of a matrix through which cells can migrate.  Hyaluronic acid is produced during wound healing and tissue repair to provide a framework for ingrowth of blood vessels and fibroblasts.  Changes in the serum concentration of hyaluronic acid are associated with inflammatory and degenerative arthropathies such as rheumatoid arthritis.  In addition, the interaction of hyaluronic acid with the leukocyte receptor CD44 is important in tissue-specific homing by leukocytes, and overexpression of hyaluronic acid receptors has been correlated with tumor metastasis.  HAS2 is a member of the vertebrate gene family encoding putative hyaluronan synthases, and its amino acid sequence shows significant homology to glycosaminoglycan synthetase (DG42) from Xenopus laevis, and human and murine hyaluronan synthase 1.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Spicer AP, Nguyen TK |title=Mammalian hyaluronan synthases: investigation of functional relationships in vivo. |journal=Biochem. Soc. Trans. |volume=27 |issue= 2 |pages= 109-15 |year= 1999 |pmid= 10093717 |doi=  }}
*{{cite journal  |vauthors=Spicer AP, Nguyen TK |title=Mammalian hyaluronan synthases: investigation of functional relationships in vivo |journal=Biochem. Soc. Trans. |volume=27 |issue= 2 |pages= 109–15 |year= 1999 |pmid= 10093717 |doi=  }}
*{{cite journal  | author=Watanabe K, Yamaguchi Y |title=Molecular identification of a putative human hyaluronan synthase. |journal=J. Biol. Chem. |volume=271 |issue= 38 |pages= 22945-8 |year= 1996 |pmid= 8798477 |doi=  }}
*{{cite journal  |vauthors=Watanabe K, Yamaguchi Y |title=Molecular identification of a putative human hyaluronan synthase |journal=J. Biol. Chem. |volume=271 |issue= 38 |pages= 22945–8 |year= 1996 |pmid= 8798477 |doi=10.1074/jbc.271.38.22945 }}
*{{cite journal | author=Spicer AP, Seldin MF, Olsen AS, ''et al.'' |title=Chromosomal localization of the human and mouse hyaluronan synthase genes. |journal=Genomics |volume=41 |issue= 3 |pages= 493-7 |year= 1997 |pmid= 9169154 |doi= 10.1006/geno.1997.4696 }}
*{{cite journal   |vauthors=Simpson MA, Wilson CM, Furcht LT, etal |title=Manipulation of hyaluronan synthase expression in prostate adenocarcinoma cells alters pericellular matrix retention and adhesion to bone marrow endothelial cells |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10050–7 |year= 2002 |pmid= 11790779 |doi= 10.1074/jbc.M110069200 }}
*{{cite journal | author=Simpson MA, Wilson CM, Furcht LT, ''et al.'' |title=Manipulation of hyaluronan synthase expression in prostate adenocarcinoma cells alters pericellular matrix retention and adhesion to bone marrow endothelial cells. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10050-7 |year= 2002 |pmid= 11790779 |doi= 10.1074/jbc.M110069200 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Suzuki K, Yamamoto T, Usui T, etal |title=Expression of hyaluronan synthase in intraocular proliferative diseases: regulation of expression in human vascular endothelial cells by transforming growth factor-beta |journal=Jpn. J. Ophthalmol. |volume=47 |issue= 6 |pages= 557–64 |year= 2004 |pmid= 14636845 |doi=10.1016/j.jjo.2003.09.001  }}
*{{cite journal | author=Suzuki K, Yamamoto T, Usui T, ''et al.'' |title=Expression of hyaluronan synthase in intraocular proliferative diseases: regulation of expression in human vascular endothelial cells by transforming growth factor-beta. |journal=Jpn. J. Ophthalmol. |volume=47 |issue= 6 |pages= 557-64 |year= 2004 |pmid= 14636845 |doi= }}
*{{cite journal   |vauthors=Sussmann M, Sarbia M, Meyer-Kirchrath J, etal |title=Induction of hyaluronic acid synthase 2 (HAS2) in human vascular smooth muscle cells by vasodilatory prostaglandins |journal=Circ. Res. |volume=94 |issue= 5 |pages= 592–600 |year= 2004 |pmid= 14752026 |doi= 10.1161/01.RES.0000119169.87429.A0 }}
*{{cite journal | author=Sussmann M, Sarbia M, Meyer-Kirchrath J, ''et al.'' |title=Induction of hyaluronic acid synthase 2 (HAS2) in human vascular smooth muscle cells by vasodilatory prostaglandins. |journal=Circ. Res. |volume=94 |issue= 5 |pages= 592-600 |year= 2004 |pmid= 14752026 |doi= 10.1161/01.RES.0000119169.87429.A0 }}
*{{cite journal   |vauthors=Monslow J, Williams JD, Guy CA, etal |title=Identification and analysis of the promoter region of the human hyaluronan synthase 2 gene |journal=J. Biol. Chem. |volume=279 |issue= 20 |pages= 20576–81 |year= 2004 |pmid= 14988410 |doi= 10.1074/jbc.M312666200 }}
*{{cite journal | author=Monslow J, Williams JD, Guy CA, ''et al.'' |title=Identification and analysis of the promoter region of the human hyaluronan synthase 2 gene. |journal=J. Biol. Chem. |volume=279 |issue= 20 |pages= 20576-81 |year= 2004 |pmid= 14988410 |doi= 10.1074/jbc.M312666200 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Morerio C, Rapella A, Rosanda C, etal |title=PLAG1-HAS2 fusion in lipoblastoma with masked 8q intrachromosomal rearrangement |journal=Cancer Genet. Cytogenet. |volume=156 |issue= 2 |pages= 183–4 |year= 2005 |pmid= 15642402 |doi= 10.1016/j.cancergencyto.2004.04.017 }}
*{{cite journal  | author=Morerio C, Rapella A, Rosanda C, ''et al.'' |title=PLAG1-HAS2 fusion in lipoblastoma with masked 8q intrachromosomal rearrangement. |journal=Cancer Genet. Cytogenet. |volume=156 |issue= 2 |pages= 183-4 |year= 2005 |pmid= 15642402 |doi= 10.1016/j.cancergencyto.2004.04.017 }}
*{{cite journal  |vauthors=Ducale AE, Ward SI, Dechert T, Yager DR |title=Regulation of hyaluronan synthase-2 expression in human intestinal mesenchymal cells: mechanisms of interleukin-1beta-mediated induction |journal=Am. J. Physiol. Gastrointest. Liver Physiol. |volume=289 |issue= 3 |pages= G462–70 |year= 2005 |pmid= 15677552 |doi= 10.1152/ajpgi.00494.2004 }}
*{{cite journal | author=Ducale AE, Ward SI, Dechert T, Yager DR |title=Regulation of hyaluronan synthase-2 expression in human intestinal mesenchymal cells: mechanisms of interleukin-1beta-mediated induction. |journal=Am. J. Physiol. Gastrointest. Liver Physiol. |volume=289 |issue= 3 |pages= G462-70 |year= 2005 |pmid= 15677552 |doi= 10.1152/ajpgi.00494.2004 }}
*{{cite journal   |vauthors=Saavalainen K, Pasonen-Seppänen S, Dunlop TW, etal |title=The human hyaluronan synthase 2 gene is a primary retinoic acid and epidermal growth factor responding gene |journal=J. Biol. Chem. |volume=280 |issue= 15 |pages= 14636–44 |year= 2005 |pmid= 15722343 |doi= 10.1074/jbc.M500206200 }}
*{{cite journal  | author=Saavalainen K, Pasonen-Seppänen S, Dunlop TW, ''et al.'' |title=The human hyaluronan synthase 2 gene is a primary retinoic acid and epidermal growth factor responding gene. |journal=J. Biol. Chem. |volume=280 |issue= 15 |pages= 14636-44 |year= 2005 |pmid= 15722343 |doi= 10.1074/jbc.M500206200 }}
*{{cite journal  |vauthors=Chao H, Spicer AP |title=Natural antisense mRNAs to hyaluronan synthase 2 inhibit hyaluronan biosynthesis and cell proliferation |journal=J. Biol. Chem. |volume=280 |issue= 30 |pages= 27513–22 |year= 2005 |pmid= 15843373 |doi= 10.1074/jbc.M411544200 }}
*{{cite journal  | author=Chao H, Spicer AP |title=Natural antisense mRNAs to hyaluronan synthase 2 inhibit hyaluronan biosynthesis and cell proliferation. |journal=J. Biol. Chem. |volume=280 |issue= 30 |pages= 27513-22 |year= 2005 |pmid= 15843373 |doi= 10.1074/jbc.M411544200 }}
*{{cite journal  |vauthors=Nishida Y, Knudson W, Knudson CB, Ishiguro N |title=Antisense inhibition of hyaluronan synthase-2 in human osteosarcoma cells inhibits hyaluronan retention and tumorigenicity |journal=Exp. Cell Res. |volume=307 |issue= 1 |pages= 194–203 |year= 2005 |pmid= 15922739 |doi= 10.1016/j.yexcr.2005.03.026  | pmc=3182490 }}
*{{cite journal  | author=Nishida Y, Knudson W, Knudson CB, Ishiguro N |title=Antisense inhibition of hyaluronan synthase-2 in human osteosarcoma cells inhibits hyaluronan retention and tumorigenicity. |journal=Exp. Cell Res. |volume=307 |issue= 1 |pages= 194-203 |year= 2005 |pmid= 15922739 |doi= 10.1016/j.yexcr.2005.03.026 }}
*{{cite journal  |vauthors=Grskovic B, Pollaschek C, Mueller MM, Stuhlmeier KM |title=Expression of hyaluronan synthase genes in umbilical cord blood stem/progenitor cells |journal=Biochim. Biophys. Acta |volume=1760 |issue= 6 |pages= 890–5 |year= 2006 |pmid= 16564133 |doi= 10.1016/j.bbagen.2006.02.002 }}
*{{cite journal | author=Grskovic B, Pollaschek C, Mueller MM, Stuhlmeier KM |title=Expression of hyaluronan synthase genes in umbilical cord blood stem/progenitor cells. |journal=Biochim. Biophys. Acta |volume=1760 |issue= 6 |pages= 890-5 |year= 2006 |pmid= 16564133 |doi= 10.1016/j.bbagen.2006.02.002 }}
*{{cite journal   |vauthors=Monslow J, Williams JD, Fraser DJ, etal |title=Sp1 and Sp3 mediate constitutive transcription of the human hyaluronan synthase 2 gene |journal=J. Biol. Chem. |volume=281 |issue= 26 |pages= 18043–50 |year= 2006 |pmid= 16603733 |doi= 10.1074/jbc.M510467200 }}
*{{cite journal | author=Monslow J, Williams JD, Fraser DJ, ''et al.'' |title=Sp1 and Sp3 mediate constitutive transcription of the human hyaluronan synthase 2 gene. |journal=J. Biol. Chem. |volume=281 |issue= 26 |pages= 18043-50 |year= 2006 |pmid= 16603733 |doi= 10.1074/jbc.M510467200 }}
*{{cite journal   |vauthors=Selbi W, Day AJ, Rugg MS, etal |title=Overexpression of hyaluronan synthase 2 alters hyaluronan distribution and function in proximal tubular epithelial cells |journal=J. Am. Soc. Nephrol. |volume=17 |issue= 6 |pages= 1553–67 |year= 2007 |pmid= 16687630 |doi= 10.1681/ASN.2005080879 }}
*{{cite journal | author=Selbi W, Day AJ, Rugg MS, ''et al.'' |title=Overexpression of hyaluronan synthase 2 alters hyaluronan distribution and function in proximal tubular epithelial cells. |journal=J. Am. Soc. Nephrol. |volume=17 |issue= 6 |pages= 1553-67 |year= 2007 |pmid= 16687630 |doi= 10.1681/ASN.2005080879 }}
*{{cite journal   |vauthors=Campo GM, Avenoso A, Campo S, etal |title=TNF-alpha, IFN-gamma, and IL-1beta modulate hyaluronan synthase expression in human skin fibroblasts: synergistic effect by concomital treatment with FeSO4 plus ascorbate |journal=Mol. Cell. Biochem. |volume=292 |issue= 1–2 |pages= 169–78 |year= 2007 |pmid= 16786194 |doi= 10.1007/s11010-006-9230-7 }}
*{{cite journal  | author=Campo GM, Avenoso A, Campo S, ''et al.'' |title=TNF-alpha, IFN-gamma, and IL-1beta modulate hyaluronan synthase expression in human skin fibroblasts: synergistic effect by concomital treatment with FeSO4 plus ascorbate. |journal=Mol. Cell. Biochem. |volume=292 |issue= 1-2 |pages= 169-78 |year= 2007 |pmid= 16786194 |doi= 10.1007/s11010-006-9230-7 }}
*{{cite journal  |vauthors=Cook AC, Chambers AF, Turley EA, Tuck AB |title=Osteopontin induction of hyaluronan synthase 2 expression promotes breast cancer malignancy |journal=J. Biol. Chem. |volume=281 |issue= 34 |pages= 24381–9 |year= 2006 |pmid= 16807238 |doi= 10.1074/jbc.M602694200 }}
*{{cite journal  | author=Cook AC, Chambers AF, Turley EA, Tuck AB |title=Osteopontin induction of hyaluronan synthase 2 expression promotes breast cancer malignancy. |journal=J. Biol. Chem. |volume=281 |issue= 34 |pages= 24381-9 |year= 2006 |pmid= 16807238 |doi= 10.1074/jbc.M602694200 }}
*{{cite journal  |vauthors=Klewer SE, Yatskievych T, Pogreba K, Stevens MV, Antin PB, Camenisch TD |title=Has2 expression in heart forming regions is independent of BMP signaling |journal=Gene Expr Patterns |volume=6 |issue= 5 |pages= 462–70 |year= 2006 |pmid= 16458617 |doi= 10.1016/j.modgep.2005.11.005}}
*{{cite journal  |vauthors=Camenisch TD, Schroeder JA, Bradley J, Klewer SE, McDonald JA |title=Heart-valve mesenchyme formation is dependent on hyaluronan-augmented activation of ErbB2-ErbB3 receptors |journal=Nat Med. |volume=8 |issue= 8 |pages= 850–5 |year= 2002 |pmid= 12134143 |doi= 10.1038/nm742}}
*{{cite journal  |vauthors=Camenisch TD, Spicer AP, Brehm-Gibson T, Biesterfeldt J, Augustine ML, ((Calabro A Jr)), Kubalak S, Klewer SE, McDonald JA |title=Disruption of hyaluronan synthase-2 abrogates normal cardiac morphogenesis and hyaluronan-mediated transformation of epithelium to mesenchyme |journal=J Clin Invest |volume=106 |issue= 3 |pages= 349–60 |year= 2000 |pmid= 10930438 |doi= 10.1172/JCI10272  | pmc=314332}}
}}
}}
{{refend}}
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{{protein-stub}}
{{Glycosyltransferases}}
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Revision as of 04:25, 11 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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Wikidata
View/Edit Human

Hyaluronan synthase 2 is an enzyme that in humans is encoded by the HAS2 gene.[1][2]

Hyaluronan or hyaluronic acid 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. Hyaluronic acid is synthesized by membrane-bound synthase at the inner surface of the plasma membrane, and the chains are extruded via ABC-Transporter[3] into the extracellular space. It serves a variety of functions, including space filling, lubrication of joints, and provision of a matrix through which cells can migrate. Hyaluronic acid is produced during wound healing and tissue repair to provide a framework for ingrowth of blood vessels and fibroblasts. Changes in the serum concentration of hyaluronic acid are associated with inflammatory and degenerative arthropathies such as rheumatoid arthritis. In addition, the interaction of hyaluronic acid with the leukocyte receptor CD44 is important in tissue-specific homing by leukocytes, and overexpression of hyaluronic acid receptors has been correlated with tumor metastasis. HAS2 is a member of the vertebrate gene family encoding putative hyaluronan synthases, and its amino acid sequence shows significant homology to glycosaminoglycan synthetase (DG42) from Xenopus laevis, and human and murine hyaluronan synthase 1.[2]

References

  1. ↑ Spicer AP, Seldin MF, Olsen AS, Brown N, Wells DE, Doggett NA, Itano N, Kimata K, Inazawa J, McDonald JA (Jul 1997). "Chromosomal localization of the human and mouse hyaluronan synthase genes". Genomics. 41 (3): 493–7. doi:10.1006/geno.1997.4696. PMID 9169154.
  2. ↑ 2.0 2.1 "Entrez Gene: HAS2 hyaluronan synthase 2".
  3. ↑ Schulz,T.; Schumacher,U.; Prehm,P. Hyaluronan export by the ABC transporter MRP5 and its modulation by intracellular cGMP. J.Biol.Chem.282,20999-21004

Further reading



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