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{{Infobox_gene}}
{{PBB_Controls
'''Hyaluronan synthase 1''' is an [[enzyme]] that in humans is encoded by the ''HAS1'' [[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: HAS1 hyaluronan synthase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3036| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==Structure==
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Hyaluronan synthase 1
| HGNCid = 4818
| Symbol = HAS1
| AltSymbols =; HAS
| OMIM = 601463
| ECnumber = 
| Homologene = 1165
| MGIid = 106590
| GeneAtlas_image1 = PBB_GE_HAS1_207316_at_tn.png
| Function = {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}} {{GNF_GO|id=GO:0050501 |text = hyaluronan synthase activity}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006024 |text = glycosaminoglycan biosynthetic process}} {{GNF_GO|id=GO:0006929 |text = substrate-bound cell migration}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3036
    | Hs_Ensembl = ENSG00000105509
    | Hs_RefseqProtein = NP_001514
    | Hs_RefseqmRNA = NM_001523
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 56908177
    | Hs_GenLoc_end = 56919033
    | Hs_Uniprot = Q92839
    | Mm_EntrezGene = 15116
    | Mm_Ensembl = ENSMUSG00000003665
    | Mm_RefseqmRNA = NM_008215
    | Mm_RefseqProtein = NP_032241
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 17548242
    | Mm_GenLoc_end = 17555272
    | Mm_Uniprot = Q05A37
  }}
}}
'''Hyaluronan synthase 1''', also known as '''HAS1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HAS1 hyaluronan synthase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3036| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="pmid17540771">{{cite journal |vauthors=Schulz T, Schumacher U, Prehm P | title = Hyaluronan export by the ABC transporter MRP5 and its modulation by intracellular cGMP | journal = J. Biol. Chem. | volume = 282 | issue = 29 | pages = 20999–1004 |date=July 2007 | pmid = 17540771 | doi = 10.1074/jbc.M700915200 }}</ref>
{{PBB_Summary
 
| section_title =
==Function==
| 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.  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.<ref name="entrez">{{cite web | title = Entrez Gene: HAS1 hyaluronan synthase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3036| accessdate = }}</ref>
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 (biology)|homology]] to the hasA gene product of [[Streptococcus pyogenes]], a glycosaminoglycan synthetase (DG42) from ''[[Xenopus laevis]]'', and a recently described murine hyaluronan synthase.<ref name="entrez"/>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
{{Clear}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{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=  }}
| citations =
*{{cite journal  | author=Mian N |title=Analysis of cell-growth-phase-related variations in hyaluronate synthase activity of isolated plasma-membrane fractions of cultured human skin fibroblasts. |journal=Biochem. J. |volume=237 |issue= 2 |pages= 333–42 |year= 1987 |pmid= 3099751 |doi= | pmc=1146992 }}
*{{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=Itano N, Kimata K |title=Molecular cloning of human hyaluronan synthase. |journal=Biochem. Biophys. Res. Commun. |volume=222 |issue= 3 |pages= 816–20 |year= 1996 |pmid= 8651928 |doi= 10.1006/bbrc.1996.0827 }}
*{{cite journal  | author=Mian N |title=Analysis of cell-growth-phase-related variations in hyaluronate synthase activity of isolated plasma-membrane fractions of cultured human skin fibroblasts. |journal=Biochem. J. |volume=237 |issue= 2 |pages= 333-42 |year= 1987 |pmid= 3099751 |doi=  }}
*{{cite journal   |vauthors=Shyjan AM, Heldin P, Butcher EC, etal |title=Functional cloning of the cDNA for a human hyaluronan synthase. |journal=J. Biol. Chem. |volume=271 |issue= 38 |pages= 23395–9 |year= 1996 |pmid= 8798544 |doi=10.1074/jbc.271.38.23395  }}
*{{cite journal  | author=Itano N, Kimata K |title=Molecular cloning of human hyaluronan synthase. |journal=Biochem. Biophys. Res. Commun. |volume=222 |issue= 3 |pages= 816-20 |year= 1996 |pmid= 8651928 |doi= 10.1006/bbrc.1996.0827 }}
*{{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=Shyjan AM, Heldin P, Butcher EC, ''et al.'' |title=Functional cloning of the cDNA for a human hyaluronan synthase. |journal=J. Biol. Chem. |volume=271 |issue= 38 |pages= 23395-9 |year= 1996 |pmid= 8798544 |doi= }}
*{{cite journal  |vauthors=Calabro A, Oken MM, Hascall VC, Masellis AM |title=Characterization of hyaluronan synthase expression and hyaluronan synthesis in bone marrow mesenchymal progenitor cells: predominant expression of HAS1 mRNA and up-regulated hyaluronan synthesis in bone marrow cells derived from multiple myeloma patients. |journal=Blood |volume=100 |issue= 7 |pages= 2578–85 |year= 2002 |pmid= 12239172 |doi= 10.1182/blood-2002-01-0030 }}
*{{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=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=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=Adamia S, Crainie M, Kriangkum J, etal |title=Abnormal expression of hyaluronan synthases in patients with Waldenstrom's macroglobulimenia. |journal=Semin. Oncol. |volume=30 |issue= 2 |pages= 165–8 |year= 2003 |pmid= 12720129 |doi= 10.1053/sonc.2003.50042 }}
*{{cite journal | author=Calabro A, Oken MM, Hascall VC, Masellis AM |title=Characterization of hyaluronan synthase expression and hyaluronan synthesis in bone marrow mesenchymal progenitor cells: predominant expression of HAS1 mRNA and up-regulated hyaluronan synthesis in bone marrow cells derived from multiple myeloma patients. |journal=Blood |volume=100 |issue= 7 |pages= 2578-85 |year= 2002 |pmid= 12239172 |doi= 10.1182/blood-2002-01-0030 }}
*{{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=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=Adamia S, Reiman T, Crainie M, etal |title=Intronic splicing of hyaluronan synthase 1 (HAS1): a biologically relevant indicator of poor outcome in multiple myeloma. |journal=Blood |volume=105 |issue= 12 |pages= 4836–44 |year= 2005 |pmid= 15731173 |doi= 10.1182/blood-2004-10-3825  | pmc=1894997 }}
*{{cite journal | author=Adamia S, Crainie M, Kriangkum J, ''et al.'' |title=Abnormal expression of hyaluronan synthases in patients with Waldenstrom's macroglobulimenia. |journal=Semin. Oncol. |volume=30 |issue= 2 |pages= 165-8 |year= 2003 |pmid= 12720129 |doi= 10.1053/sonc.2003.50042 }}
*{{cite journal   |vauthors=Yabushita H, Kishida T, Fusano K, etal |title=Role of hyaluronan and hyaluronan synthase in endometrial cancer. |journal=Oncol. Rep. |volume=13 |issue= 6 |pages= 1101–5 |year= 2005 |pmid= 15870928 |doi= 10.3892/or.13.6.1101}}
*{{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=Stuhlmeier KM, Pollaschek C |title=Adenovirus-mediated gene transfer of mutated IkappaB kinase and IkappaBalpha reveal NF-kappaB-dependent as well as NF-kappaB-independent pathways of HAS1 activation. |journal=J. Biol. Chem. |volume=280 |issue= 52 |pages= 42766–73 |year= 2006 |pmid= 16258173 |doi= 10.1074/jbc.M503374200 }}
*{{cite journal | author=Adamia S, Reiman T, Crainie M, ''et al.'' |title=Intronic splicing of hyaluronan synthase 1 (HAS1): a biologically relevant indicator of poor outcome in multiple myeloma. |journal=Blood |volume=105 |issue= 12 |pages= 4836-44 |year= 2005 |pmid= 15731173 |doi= 10.1182/blood-2004-10-3825 }}
*{{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=Yabushita H, Kishida T, Fusano K, ''et al.'' |title=Role of hyaluronan and hyaluronan synthase in endometrial cancer. |journal=Oncol. Rep. |volume=13 |issue= 6 |pages= 1101-5 |year= 2005 |pmid= 15870928 |doi= }}
*{{cite journal  | author=Kao JJ |title=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. |journal=Exp. Gerontol. |volume=41 |issue= 6 |pages= 641–7 |year= 2007 |pmid= 16723203 |doi= 10.1016/j.exger.2006.04.003 }}
*{{cite journal  | author=Stuhlmeier KM, Pollaschek C |title=Adenovirus-mediated gene transfer of mutated IkappaB kinase and IkappaBalpha reveal NF-kappaB-dependent as well as NF-kappaB-independent pathways of HAS1 activation. |journal=J. Biol. Chem. |volume=280 |issue= 52 |pages= 42766-73 |year= 2006 |pmid= 16258173 |doi= 10.1074/jbc.M503374200 }}
*{{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=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=Ewing RM, Chu P, Elisma F, etal |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue= 1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 | pmc=1847948 }}
*{{cite journal | author=Kao JJ |title=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. |journal=Exp. Gerontol. |volume=41 |issue= 6 |pages= 641-7 |year= 2007 |pmid= 16723203 |doi= 10.1016/j.exger.2006.04.003 }}
*{{cite journal   |vauthors=Meran S, Thomas D, Stephens P, etal |title=Involvement of hyaluronan in regulation of fibroblast phenotype. |journal=J. Biol. Chem. |volume=282 |issue= 35 |pages= 25687–97 |year= 2007 |pmid= 17611197 |doi= 10.1074/jbc.M700773200 }}
*{{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=Kyossev Z, Weigel PH |title=An enzyme capture assay for analysis of active hyaluronan synthases. |journal=Anal. Biochem. |volume=371 |issue= 1 |pages= 62–70 |year= 2007 |pmid= 17904513 |doi= 10.1016/j.ab.2007.08.025 }}
*{{cite journal  | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue= |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
*{{cite journal | author=Meran S, Thomas D, Stephens P, ''et al.'' |title=Involvement of hyaluronan in regulation of fibroblast phenotype. |journal=J. Biol. Chem. |volume=282 |issue= 35 |pages= 25687-97 |year= 2007 |pmid= 17611197 |doi= 10.1074/jbc.M700773200 }}
*{{cite journal  | author=Kyossev Z, Weigel PH |title=An enzyme capture assay for analysis of active hyaluronan synthases. |journal=Anal. Biochem. |volume=371 |issue= 1 |pages= 62-70 |year= 2007 |pmid= 17904513 |doi= 10.1016/j.ab.2007.08.025 }}
}}
{{refend}}
{{refend}}
{{Glycosyltransferases}}
{{Enzymes}}
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Latest revision as of 13:27, 31 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Hyaluronan synthase 1 is an enzyme that in humans is encoded by the HAS1 gene.[1][2]

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.[3]

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.[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: HAS1 hyaluronan synthase 1".
  3. Schulz T, Schumacher U, Prehm P (July 2007). "Hyaluronan export by the ABC transporter MRP5 and its modulation by intracellular cGMP". J. Biol. Chem. 282 (29): 20999–1004. doi:10.1074/jbc.M700915200. PMID 17540771.

Further reading