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Gene Review

HYAL1  -  hyaluronoglucosaminidase 1

Homo sapiens

Synonyms: FUS2, HYAL-1, Hyal-1, Hyaluronidase-1, Hyaluronoglucosaminidase-1, ...
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Disease relevance of HYAL1


High impact information on HYAL1

  • The discovery of Ca(2+) transport by mitochondria is conventionally credited to De Luca and Engstrom, and Vasington and Murphy, who showed in 1961-1962 that Ca(2+) was taken up by isolated mitochondria using respiratory or ATP energy [5].
  • The evolution of the enzymatic systems for (i) DNA replication; and (ii) membrane and cell wall biosynthesis, enabled independent escape of the first archaebacterial and eubacterial cells from their hydrothermal hatchery, within which the LUCA itself remained confined [6].
  • Furthermore, we could not detect hyaluronidase activity associated with or secreted by cells expressing HYAL2, whereas we could easily detect such activity from cells expressing the related serum hyaluronidase HYAL1 [7].
  • These genes, HYAL1 and HYAL2, encode two distinct lysosomal hyaluronidases with different substrate specificities [1].
  • We identified two mutations in the HYAL1 alleles of the patient, a 1412G --> A mutation that introduces a nonconservative amino acid substitution (Glu268Lys) in a putative active site residue and a complex intragenic rearrangement, 1361del37ins14, that results in a premature termination codon [1].

Chemical compound and disease context of HYAL1


Biological context of HYAL1


Anatomical context of HYAL1


Associations of HYAL1 with chemical compounds

  • Expression of tumor markers hyaluronic acid and hyaluronidase (HYAL1) in head and neck tumors [15].
  • Since individuals react to different degrees to HMW, HYAL, and PHOS A, there does not appear to be a single principal allergen in honeybee venom [16].
  • We have previously shown that maximal Ret-P-Man synthesis occurs in vitro at 20-30 min, followed by a subsequent loss of mannose from Ret-P-Man, suggestive of an intermediary function of Ret-P-Man and/or Ret-P-Man breakdown [Shidoji, Silverman-Jones & De Luca (1982) Biochem. J [17].
  • The presence, but not the number, of sulfate groups on the sHA molecule determined its potency (e.g., IC50 for HYAL-1: sHA2.0, 0.019 microM; sHA2.75, 0.0083 microM) [18].
  • Histamine release in response to ACID P appears harder to block with hyperimmune beekeeper plasma than that provoked by PLA2 or HYAL (p less than 0.01) [19].

Regulatory relationships of HYAL1

  • The expression of HYAL1 mRNA was enhanced by about 3.5- and 3.7-fold at maximum after 1-hour stimulation with 1 ng/ml IL-1beta and after 3-hour stimulation with 10 ng/ml TNF-alpha, respectively [12].

Other interactions of HYAL1

  • Analogously to PH-20, the smaller isozyme of HYAL1 is likely to be a proteolytically processed product of the larger isozyme [20].
  • In contrast to BMP-7, IL-1beta did not influence Hyal expression [21].
  • Hyaluronan synthase (HAS) or hyaluronidase (HYAL) mRNA levels were assessed by reverse transcription-PCR [22].
  • Coexpression of Hyal1 with HAS2 diminished HA retention but restored growth kinetics, supporting a possible combined role for excess HA synthesis and processing in maximizing unrestricted growth of prostate cancer cells [23].

Analytical, diagnostic and therapeutic context of HYAL1


  1. Mutations in HYAL1, a member of a tandemly distributed multigene family encoding disparate hyaluronidase activities, cause a newly described lysosomal disorder, mucopolysaccharidosis IX. Triggs-Raine, B., Salo, T.J., Zhang, H., Wicklow, B.A., Natowicz, M.R. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  2. Regulation of hyaluronidase activity by alternative mRNA splicing. Lokeshwar, V.B., Schroeder, G.L., Carey, R.I., Soloway, M.S., Iida, N. J. Biol. Chem. (2002) [Pubmed]
  3. Expression patterns of hyaluronan, hyaluronan synthases and hyaluronidases indicate a role for hyaluronan in the progression of endometrial cancer. Paiva, P., Van Damme, M.P., Tellbach, M., Jones, R.L., Jobling, T., Salamonsen, L.A. Gynecol. Oncol. (2005) [Pubmed]
  4. The over-expression of HAS2, Hyal-2 and CD44 is implicated in the invasiveness of breast cancer. Udabage, L., Brownlee, G.R., Nilsson, S.K., Brown, T.J. Exp. Cell Res. (2005) [Pubmed]
  5. Historical review: mitochondria and calcium: ups and downs of an unusual relationship. Carafoli, E. Trends Biochem. Sci. (2003) [Pubmed]
  6. On the origin of genomes and cells within inorganic compartments. Koonin, E.V., Martin, W. Trends Genet. (2005) [Pubmed]
  7. Candidate tumor suppressor HYAL2 is a glycosylphosphatidylinositol (GPI)-anchored cell-surface receptor for jaagsiekte sheep retrovirus, the envelope protein of which mediates oncogenic transformation. Rai, S.K., Duh, F.M., Vigdorovich, V., Danilkovitch-Miagkova, A., Lerman, M.I., Miller, A.D. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  8. Evaluation of the prognostic potential of hyaluronic acid and hyaluronidase (HYAL1) for prostate cancer. Posey, J.T., Soloway, M.S., Ekici, S., Sofer, M., Civantos, F., Duncan, R.C., Lokeshwar, V.B. Cancer Res. (2003) [Pubmed]
  9. HYAL1LUCA-1, a candidate tumor suppressor gene on chromosome 3p21.3, is inactivated in head and neck squamous cell carcinomas by aberrant splicing of pre-mRNA. Frost, G.I., Mohapatra, G., Wong, T.M., Csóka, A.B., Gray, J.W., Stern, R. Oncogene (2000) [Pubmed]
  10. The hyaluronidase gene HYAL1 maps to chromosome 3p21.2-p21.3 in human and 9F1-F2 in mouse, a conserved candidate tumor suppressor locus. Csóka, A.B., Frost, G.I., Heng, H.H., Scherer, S.W., Mohapatra, G., Stern, R., Csóka, T.B. Genomics (1998) [Pubmed]
  11. Characterization of the murine hyaluronidase gene region reveals complex organization and cotranscription of Hyal1 with downstream genes, Fus2 and Hyal3. Shuttleworth, T.L., Wilson, M.D., Wicklow, B.A., Wilkins, J.A., Triggs-Raine, B.L. J. Biol. Chem. (2002) [Pubmed]
  12. Expression and activity of hyaluronidase in human periodontal ligament fibroblasts. Ohno, S., Ijuin, C., Doi, T., Yoneno, K., Tanne, K. J. Periodontol. (2002) [Pubmed]
  13. HYAL1 hyaluronidase in prostate cancer: a tumor promoter and suppressor. Lokeshwar, V.B., Cerwinka, W.H., Isoyama, T., Lokeshwar, B.L. Cancer Res. (2005) [Pubmed]
  14. Plasma hyaluronidase (Hyal-1) promotes tumor cell cycling. Lin, G., Stern, R. Cancer Lett. (2001) [Pubmed]
  15. Expression of tumor markers hyaluronic acid and hyaluronidase (HYAL1) in head and neck tumors. Franzmann, E.J., Schroeder, G.L., Goodwin, W.J., Weed, D.T., Fisher, P., Lokeshwar, V.B. Int. J. Cancer (2003) [Pubmed]
  16. A high molecular weight allergenic fraction of honeybee venom. Karpas, A.B., Baer, H., Hooton, M.L., Evans, R. J. Allergy Clin. Immunol. (1977) [Pubmed]
  17. Synthesis of retinyl phosphate mannose in vitro. Non-enzymic breakdown and reversibility. Creek, K.E., Rimoldi, D., Silverman-Jones, C.S., De Luca, L.M. Biochem. J. (1985) [Pubmed]
  18. Differential selectivity of hyaluronidase inhibitors toward acidic and basic hyaluronidases. Isoyama, T., Thwaites, D., Selzer, M.G., Carey, R.I., Barbucci, R., Lokeshwar, V.B. Glycobiology (2006) [Pubmed]
  19. Histamine release from peripheral blood leukocytes with purified bee venom allergens: effect of hyperimmune beekeeper plasma. Clinton, P.M., Kemeny, D.M., Youlten, L.J., Lessof, M.H. Int. Arch. Allergy Appl. Immunol. (1989) [Pubmed]
  20. Purification and microsequencing of hyaluronidase isozymes from human urine. Csóka, A.B., Frost, G.I., Wong, T., Stern, R., Csóka, T.B. FEBS Lett. (1997) [Pubmed]
  21. BMP-7 modulates hyaluronan-mediated proximal tubular cell-monocyte interaction. Selbi, W., de la Motte, C., Hascall, V., Phillips, A. J. Am. Soc. Nephrol. (2004) [Pubmed]
  22. Myofibroblastic differentiation leads to hyaluronan accumulation through reduced hyaluronan turnover. Jenkins, R.H., Thomas, G.J., Williams, J.D., Steadman, R. J. Biol. Chem. (2004) [Pubmed]
  23. Concurrent expression of hyaluronan biosynthetic and processing enzymes promotes growth and vascularization of prostate tumors in mice. Simpson, M.A. Am. J. Pathol. (2006) [Pubmed]
  24. Expression and regulation patterns of hyaluronidases in small cell lung cancer and glioma lines. Junker, N., Latini, S., Petersen, L.N., Kristjansen, P.E. Oncol. Rep. (2003) [Pubmed]
  25. Identification of bladder tumor-derived hyaluronidase: its similarity to HYAL1. Lokeshwar, V.B., Young, M.J., Goudarzi, G., Iida, N., Yudin, A.I., Cherr, G.N., Selzer, M.G. Cancer Res. (1999) [Pubmed]
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