HYAL2: Difference between revisions

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One study found associations between [[Cleft lip and cleft palate|cleft lip and palate]] and mutations in the ''HYAL2'' gene.<ref>{{Cite news|url=http://www.medicalnewstoday.com/articles/315211.php|title=Scientists find genetic mutation that causes cleft lip and palate, heart defects|last=Sandoiu|first=Ana|date=2017-01-17|work=|newspaper=Medical News Today|language=en|access-date=2017-01-31|via=}}</ref>
One study found associations between [[Cleft lip and cleft palate|cleft lip and palate]] and mutations in the ''HYAL2'' gene.<ref>{{Cite news|url=http://www.medicalnewstoday.com/articles/315211.php|title=Scientists find genetic mutation that causes cleft lip and palate, heart defects|last=Sandoiu|first=Ana|date=2017-01-17|work=|newspaper=Medical News Today|language=en|access-date=2017-01-31|via=}}</ref>
An investigation published in 2017, attributed an additional function to the Hyaluronidase 2 (HYAL2) protein. The study found interactions between HYAL2 and proteins involved in the [[alternative splicing]] of ''[[CD44]]'' [[Precursor mRNA|pre-mRNA]],<ref>{{Cite journal|last=Midgley|first=Adam C.|last2=Oltean|first2=Sebastian|last3=Hascall|first3=Vincent|last4=Woods|first4=Emma L.|last5=Steadman|first5=Robert|last6=Phillips|first6=Aled O.|last7=Meran|first7=Soma|date=2017-11-21|title=Nuclear hyaluronidase 2 drives alternative splicing of CD44 pre-mRNA to determine profibrotic or antifibrotic cell phenotype|journal=Science Signaling|volume=10|issue=506|doi=10.1126/scisignal.aao1822|issn=1937-9145|pmid=29162741}}</ref> suggesting a broader regulatory role for the HYAL2 protein in cell biology.


==References==
==References==
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* {{cite journal  | author=Strausberg RL |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  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
* {{cite journal  | author=Strausberg RL |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  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
* {{cite journal  |vauthors=Liu SL, Duh FM, Lerman MI, Miller AD |title=Role of virus receptor Hyal2 in oncogenic transformation of rodent fibroblasts by sheep betaretrovirus env proteins |journal=J. Virol. |volume=77 |issue= 5 |pages= 2850–8 |year= 2003 |pmid= 12584308 |doi=10.1128/JVI.77.5.2850-2858.2003  | pmc=149765  }}
* {{cite journal  |vauthors=Liu SL, Duh FM, Lerman MI, Miller AD |title=Role of virus receptor Hyal2 in oncogenic transformation of rodent fibroblasts by sheep betaretrovirus env proteins |journal=J. Virol. |volume=77 |issue= 5 |pages= 2850–8 |year= 2003 |pmid= 12584308 |doi=10.1128/JVI.77.5.2850-2858.2003  | pmc=149765  }}
* {{cite journal  | author=Danilkovitch-Miagkova A |title=Hyaluronidase 2 negatively regulates RON receptor tyrosine kinase and mediates transformation of epithelial cells by jaagsiekte sheep retrovirus |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 8 |pages= 4580–5 |year= 2003 |pmid= 12676986 |doi= 10.1073/pnas.0837136100  | pmc=153598  |name-list-format=vanc| author2=Duh FM  | author3=Kuzmin I  | display-authors=3  | last4=Angeloni  | first4=D  | last5=Liu  | first5=SL  | last6=Miller  | first6=AD  | last7=Lerman  | first7=MI }}
* {{cite journal  | author=Danilkovitch-Miagkova A |title=Hyaluronidase 2 negatively regulates RON receptor tyrosine kinase and mediates transformation of epithelial cells by jaagsiekte sheep retrovirus |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 8 |pages= 4580–5 |year= 2003 |pmid= 12676986 |doi= 10.1073/pnas.0837136100  | pmc=153598  |name-list-format=vanc| author2=Duh FM  | author3=Kuzmin I  | display-authors=3  | last4=Angeloni  | first4=D  | last5=Liu  | first5=SL  | last6=Miller  | first6=AD  | last7=Lerman  | first7=MI |hdl=11382/303276}}
* {{cite journal  |vauthors=Junker N, Latini S, Petersen LN, Kristjansen PE |title=Expression and regulation patterns of hyaluronidases in small cell lung cancer and glioma lines |journal=Oncol. Rep. |volume=10 |issue= 3 |pages= 609–16 |year= 2003 |pmid= 12684632 |doi= 10.3892/or.10.3.609 }}
* {{cite journal  |vauthors=Junker N, Latini S, Petersen LN, Kristjansen PE |title=Expression and regulation patterns of hyaluronidases in small cell lung cancer and glioma lines |journal=Oncol. Rep. |volume=10 |issue= 3 |pages= 609–16 |year= 2003 |pmid= 12684632 |doi= 10.3892/or.10.3.609 }}
* {{cite journal  | author=Ota T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285  |name-list-format=vanc| author2=Suzuki Y  | author3=Nishikawa T  | display-authors=3  | last4=Otsuki  | first4=Tetsuji  | last5=Sugiyama  | first5=Tomoyasu  | last6=Irie  | first6=Ryotaro  | last7=Wakamatsu  | first7=Ai  | last8=Hayashi  | first8=Koji  | last9=Sato  | first9=Hiroyuki }}
* {{cite journal  | author=Ota T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285  |name-list-format=vanc| author2=Suzuki Y  | author3=Nishikawa T  | display-authors=3  | last4=Otsuki  | first4=Tetsuji  | last5=Sugiyama  | first5=Tomoyasu  | last6=Irie  | first6=Ryotaro  | last7=Wakamatsu  | first7=Ai  | last8=Hayashi  | first8=Koji  | last9=Sato  | first9=Hiroyuki }}

Latest revision as of 14:13, 4 November 2018

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

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RefSeq (protein)

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

Hyaluronidase-2 is an enzyme that in humans is encoded by the HYAL2 gene.[1][2][3]

This gene encodes a protein which is similar in structure to hyaluronidases. Hyaluronidases intracellularly degrade hyaluronan, one of the major glycosaminoglycans of the extracellular matrix. Hyaluronan is thought to be involved in cell proliferation, migration and differentiation. Varying functions have been described for this protein. It has been described as a lysosomal hyaluronidase which is active at a pH below 4 and specifically hydrolyzes high molecular weight hyaluronan. It has also been described as a GPI-anchored cell surface protein which does not display hyaluronidase activity but does serve as a receptor for the oncogenic virus Jaagsiekte sheep retrovirus. The gene is one of several related genes in a region of chromosome 3p21.3 associated with tumor suppression. This gene encodes two alternatively spliced transcript variants which differ only in the 5' UTR.[3]

One study found associations between cleft lip and palate and mutations in the HYAL2 gene.[4]

An investigation published in 2017, attributed an additional function to the Hyaluronidase 2 (HYAL2) protein. The study found interactions between HYAL2 and proteins involved in the alternative splicing of CD44 pre-mRNA,[5] suggesting a broader regulatory role for the HYAL2 protein in cell biology.

References

  1. Lepperdinger G, Strobl B, Kreil G (Sep 1998). "HYAL2, a human gene expressed in many cells, encodes a lysosomal hyaluronidase with a novel type of specificity". J Biol Chem. 273 (35): 22466–70. doi:10.1074/jbc.273.35.22466. PMID 9712871.
  2. Strobl B, Wechselberger C, Beier DR, Lepperdinger G (Dec 1998). "Structural organization and chromosomal localization of Hyal2, a gene encoding a lysosomal hyaluronidase". Genomics. 53 (2): 214–9. doi:10.1006/geno.1998.5472. PMID 9790770.
  3. 3.0 3.1 "Entrez Gene: HYAL2 hyaluronoglucosaminidase 2".
  4. Sandoiu, Ana (2017-01-17). "Scientists find genetic mutation that causes cleft lip and palate, heart defects". Medical News Today. Retrieved 2017-01-31.
  5. Midgley, Adam C.; Oltean, Sebastian; Hascall, Vincent; Woods, Emma L.; Steadman, Robert; Phillips, Aled O.; Meran, Soma (2017-11-21). "Nuclear hyaluronidase 2 drives alternative splicing of CD44 pre-mRNA to determine profibrotic or antifibrotic cell phenotype". Science Signaling. 10 (506). doi:10.1126/scisignal.aao1822. ISSN 1937-9145. PMID 29162741.

Further reading