HAS2

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

Protein-coding gene in the species Homo sapiens

HAS2
Identifiers
Aliases	HAS2, hyaluronan synthase 2
External IDs	OMIM: 601636; MGI: 107821; HomoloGene: 3892; GeneCards: HAS2; OMA:HAS2 - orthologs
Gene location (Human) Chr. Chromosome 8 (human)[1] Band 8q24.13 Start 121,612,116 bp[1] End 121,641,440 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15 D1|15 23.31 cM Start 56,529,023 bp[2] End 56,557,935 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in cartilage tissue stromal cell of endometrium tibia synovial joint sperm Achilles tendon gallbladder rectum islet of Langerhans epithelium of colon Top expressed in vas deferens tail of embryo abdominal wall maxillary prominence hand efferent ductule conjunctival fornix atrioventricular canal epiblast primitive streak More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity glycosyltransferase activity hyaluronan synthase activity protein binding identical protein binding Cellular component cytoplasm integral component of membrane membrane integral component of plasma membrane plasma membrane raft Biological process atrioventricular canal development positive regulation of keratinocyte proliferation hyaluronan biosynthetic process positive regulation of urine volume kidney development estrous cycle positive regulation of cell migration cellular response to tumor necrosis factor bone morphogenesis cellular response to platelet-derived growth factor stimulus cellular response to fluid shear stress vasculogenesis positive regulation of smooth muscle cell migration positive regulation of keratinocyte migration positive regulation of substrate adhesion-dependent cell spreading positive regulation of hyaluronan biosynthetic process extracellular matrix assembly cellular response to interleukin-1 positive regulation of cell population proliferation extracellular polysaccharide biosynthetic process hyaluronan metabolic process endocardial cushion to mesenchymal transition renal water absorption positive regulation of monocyte aggregation regulation of extracellular matrix assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3037 15117 Ensembl ENSG00000170961 ENSMUSG00000022367 UniProt Q92819 P70312 RefSeq (mRNA) NM_005328 NM_008216 RefSeq (protein) NP_005319 NP_032242 Location (UCSC) Chr 8: 121.61 – 121.64 Mb Chr 15: 56.53 – 56.56 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Hyaluronan synthase 2 is an enzyme that in humans is encoded by the HAS2 gene.^[5][6]

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.^[7] 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^[8] 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 the 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.^[6]

References

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1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000170961 – Ensembl, May 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000022367 – Ensembl, May 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ Spicer AP, Seldin MF, Olsen AS, Brown N, Wells DE, Doggett NA, et al. (May 1997). "Chromosomal localization of the human and mouse hyaluronan synthase genes". Genomics. 41 (3): 493–497. doi:10.1006/geno.1997.4696. PMID 9169154.
6. ^ ^{a b} "Entrez Gene: HAS2 hyaluronan synthase 2".
7. ^ Harth M, Furlan F (2024). "Microbial hyaluronic acid production in the 21 century: a roadmap toward high production, tailored molecular weight". Arquivos. 22 (3): e3913. doi:10.55905/oelv22n3-185.
8. ^ Schulz T, Schumacher U, Prehm P (July 2007). "Hyaluronan export by the ABC transporter MRP5 and its modulation by intracellular cGMP". The Journal of Biological Chemistry. 282 (29): 20999–1004. doi:10.1074/jbc.M700915200. PMID 17540771.

Further reading

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• Spicer AP, Nguyen TK (February 1999). "Mammalian hyaluronan synthases: investigation of functional relationships in vivo". Biochemical Society Transactions. 27 (2): 109–115. doi:10.1042/bst0270109. PMID 10093717.
• Watanabe K, Yamaguchi Y (September 1996). "Molecular identification of a putative human hyaluronan synthase". The Journal of Biological Chemistry. 271 (38): 22945–22948. doi:10.1074/jbc.271.38.22945. PMID 8798477.
• Simpson MA, Wilson CM, Furcht LT, Spicer AP, Oegema TR, McCarthy JB (March 2002). "Manipulation of hyaluronan synthase expression in prostate adenocarcinoma cells alters pericellular matrix retention and adhesion to bone marrow endothelial cells". The Journal of Biological Chemistry. 277 (12): 10050–10057. doi:10.1074/jbc.M110069200. PMID 11790779.
• Suzuki K, Yamamoto T, Usui T, Suzuki K, Heldin P, Yamashita H (2004). "Expression of hyaluronan synthase in intraocular proliferative diseases: regulation of expression in human vascular endothelial cells by transforming growth factor-beta". Japanese Journal of Ophthalmology. 47 (6): 557–564. doi:10.1016/j.jjo.2003.09.001. PMID 14636845.
• Sussmann M, Sarbia M, Meyer-Kirchrath J, Nüsing RM, Schrör K, Fischer JW (March 2004). "Induction of hyaluronic acid synthase 2 (HAS2) in human vascular smooth muscle cells by vasodilatory prostaglandins". Circulation Research. 94 (5): 592–600. doi:10.1161/01.RES.0000119169.87429.A0. PMID 14752026.
• Monslow J, Williams JD, Guy CA, Price IK, Craig KJ, Williams HJ, et al. (May 2004). "Identification and analysis of the promoter region of the human hyaluronan synthase 2 gene". The Journal of Biological Chemistry. 279 (20): 20576–20581. doi:10.1074/jbc.M312666200. PMID 14988410.
• Morerio C, Rapella A, Rosanda C, Tassano E, Gambini C, Romagnoli G, et al. (January 2005). "PLAG1-HAS2 fusion in lipoblastoma with masked 8q intrachromosomal rearrangement". Cancer Genetics and Cytogenetics. 156 (2): 183–184. doi:10.1016/j.cancergencyto.2004.04.017. PMID 15642402.
• Ducale AE, Ward SI, Dechert T, Yager DR (September 2005). "Regulation of hyaluronan synthase-2 expression in human intestinal mesenchymal cells: mechanisms of interleukin-1beta-mediated induction". American Journal of Physiology. Gastrointestinal and Liver Physiology. 289 (3): G462–G470. doi:10.1152/ajpgi.00494.2004. PMID 15677552.
• Saavalainen K, Pasonen-Seppänen S, Dunlop TW, Tammi R, Tammi MI, Carlberg C (April 2005). "The human hyaluronan synthase 2 gene is a primary retinoic acid and epidermal growth factor responding gene". The Journal of Biological Chemistry. 280 (15): 14636–14644. doi:10.1074/jbc.M500206200. PMID 15722343.
• Chao H, Spicer AP (July 2005). "Natural antisense mRNAs to hyaluronan synthase 2 inhibit hyaluronan biosynthesis and cell proliferation". The Journal of Biological Chemistry. 280 (30): 27513–27522. doi:10.1074/jbc.M411544200. PMID 15843373.
• Nishida Y, Knudson W, Knudson CB, Ishiguro N (July 2005). "Antisense inhibition of hyaluronan synthase-2 in human osteosarcoma cells inhibits hyaluronan retention and tumorigenicity". Experimental Cell Research. 307 (1): 194–203. doi:10.1016/j.yexcr.2005.03.026. PMC 3182490. PMID 15922739.
• Grskovic B, Pollaschek C, Mueller MM, Stuhlmeier KM (June 2006). "Expression of hyaluronan synthase genes in umbilical cord blood stem/progenitor cells". Biochimica et Biophysica Acta (BBA) - General Subjects. 1760 (6): 890–895. doi:10.1016/j.bbagen.2006.02.002. PMID 16564133.
• Monslow J, Williams JD, Fraser DJ, Michael DR, Foka P, Kift-Morgan AP, et al. (June 2006). "Sp1 and Sp3 mediate constitutive transcription of the human hyaluronan synthase 2 gene". The Journal of Biological Chemistry. 281 (26): 18043–18050. doi:10.1074/jbc.M510467200. PMID 16603733.
• Selbi W, Day AJ, Rugg MS, Fülöp C, de la Motte CA, Bowen T, et al. (June 2006). "Overexpression of hyaluronan synthase 2 alters hyaluronan distribution and function in proximal tubular epithelial cells". Journal of the American Society of Nephrology. 17 (6): 1553–1567. doi:10.1681/ASN.2005080879. PMID 16687630.
• Campo GM, Avenoso A, Campo S, Angela D, Ferlazzo AM, Calatroni A (November 2006). "TNF-alpha, IFN-gamma, and IL-1beta modulate hyaluronan synthase expression in human skin fibroblasts: synergistic effect by concomital treatment with FeSO4 plus ascorbate". Molecular and Cellular Biochemistry. 292 (1–2): 169–178. doi:10.1007/s11010-006-9230-7. PMID 16786194. S2CID 37598580.
• Cook AC, Chambers AF, Turley EA, Tuck AB (August 2006). "Osteopontin induction of hyaluronan synthase 2 expression promotes breast cancer malignancy". The Journal of Biological Chemistry. 281 (34): 24381–24389. doi:10.1074/jbc.M602694200. PMID 16807238.
• Klewer SE, Yatskievych T, Pogreba K, Stevens MV, Antin PB, Camenisch TD (June 2006). "Has2 expression in heart forming regions is independent of BMP signaling". Gene Expression Patterns. 6 (5): 462–470. doi:10.1016/j.modgep.2005.11.005. PMID 16458617.
• Camenisch TD, Schroeder JA, Bradley J, Klewer SE, McDonald JA (August 2002). "Heart-valve mesenchyme formation is dependent on hyaluronan-augmented activation of ErbB2-ErbB3 receptors". Nature Medicine. 8 (8): 850–855. doi:10.1038/nm742. PMID 12134143. S2CID 6092884.
• Camenisch TD, Spicer AP, Brehm-Gibson T, Biesterfeldt J, Augustine ML, Calabro A, et al. (August 2000). "Disruption of hyaluronan synthase-2 abrogates normal cardiac morphogenesis and hyaluronan-mediated transformation of epithelium to mesenchyme". The Journal of Clinical Investigation. 106 (3): 349–360. doi:10.1172/JCI10272. PMC 314332. PMID 10930438.

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