HYAL2: Difference between revisions

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Latest revision as of 14:13, 4 November 2018

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

↑ 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.
↑ 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.
↑ ^3.0 ^3.1 "Entrez Gene: HYAL2 hyaluronoglucosaminidase 2".
↑ Sandoiu, Ana (2017-01-17). "Scientists find genetic mutation that causes cleft lip and palate, heart defects". Medical News Today. Retrieved 2017-01-31.
↑ 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.

Lepperdinger G, Müllegger J, Kreil G (2002). "Hyal2--less active, but more versatile?". Matrix Biol. 20 (8): 509–14. doi:10.1016/S0945-053X(01)00170-6. PMID 11731268.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Wei MH, Latif F, Bader S, et al. (1996). "Construction of a 600-kilobase cosmid clone contig and generation of a transcriptional map surrounding the lung cancer tumor suppressor gene (TSG) locus on human chromosome 3p21.3: progress toward the isolation of a lung cancer TSG". Cancer Res. 56 (7): 1487–92. PMID 8603390.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Sun L, Feusi E, Sibalic A, et al. (1999). "Expression profile of hyaluronidase mRNA transcripts in the kidney and in renal cells". Kidney Blood Press. Res. 21 (6): 413–8. doi:10.1159/000025893. PMID 9933825.
Fiszer-Szafarz B, Litynska A, Zou L (2000). "Human hyaluronidases: electrophoretic multiple forms in somatic tissues and body fluids. Evidence for conserved hyaluronidase potential N-glycosylation sites in different mammalian species". J. Biochem. Biophys. Methods. 45 (2): 103–16. doi:10.1016/S0165-022X(00)00067-1. PMID 10989127.
Lerman MI, Minna JD (2000). "The 630-kb lung cancer homozygous deletion region on human chromosome 3p21.3: identification and evaluation of the resident candidate tumor suppressor genes. The International Lung Cancer Chromosome 3p21.3 Tumor Suppressor Gene Consortium". Cancer Res. 60 (21): 6116–33. PMID 11085536.
Rai SK, Duh FM, Vigdorovich V, et al. (2001). "Candidate tumor suppressor HYAL2 is a glycosylphosphatidylinositol (GPI)-anchored cell-surface receptor for jaagsiekte sheep retrovirus, the envelope protein of which mediates oncogenic transformation". Proc. Natl. Acad. Sci. U.S.A. 98 (8): 4443–8. doi:10.1073/pnas.071572898. PMC 31854. PMID 11296287.
Delpech B, Laquerriere A, Maingonnat C, et al. (2002). "Hyaluronidase is more elevated in human brain metastases than in primary brain tumours". Anticancer Res. 22 (4): 2423–7. PMID 12174938.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Liu SL, Duh FM, Lerman MI, Miller AD (2003). "Role of virus receptor Hyal2 in oncogenic transformation of rodent fibroblasts by sheep betaretrovirus env proteins". J. Virol. 77 (5): 2850–8. doi:10.1128/JVI.77.5.2850-2858.2003. PMC 149765. PMID 12584308.
Danilkovitch-Miagkova A, Duh FM, Kuzmin I, et al. (2003). "Hyaluronidase 2 negatively regulates RON receptor tyrosine kinase and mediates transformation of epithelial cells by jaagsiekte sheep retrovirus". Proc. Natl. Acad. Sci. U.S.A. 100 (8): 4580–5. doi:10.1073/pnas.0837136100. hdl:11382/303276. PMC 153598. PMID 12676986.
Junker N, Latini S, Petersen LN, Kristjansen PE (2003). "Expression and regulation patterns of hyaluronidases in small cell lung cancer and glioma lines". Oncol. Rep. 10 (3): 609–16. doi:10.3892/or.10.3.609. PMID 12684632.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.

This article on a gene on human chromosome 3 is a stub. You can help Wikipedia by expanding it.

[pmid9712871-1] 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.

[pmid9790770-2] 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.

[entrez-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.

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@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Underlinked|date=May 2014}}
-{{PBB_Controls
+{{Infobox_gene}}
-| update_page = yes
+'''Hyaluronidase-2''' is an [[enzyme]] that in humans is encoded by the ''HYAL2'' [[gene]].<ref name="pmid9712871">{{cite journal |vauthors=Lepperdinger G, Strobl B, Kreil G | title = HYAL2, a human gene expressed in many cells, encodes a lysosomal hyaluronidase with a novel type of specificity | journal = J Biol Chem | volume = 273 | issue = 35 | pages = 22466–70 |date=Sep 1998 | pmid = 9712871 | pmc =  | doi =10.1074/jbc.273.35.22466  }}</ref><ref name="pmid9790770">{{cite journal |vauthors=Strobl B, Wechselberger C, Beier DR, Lepperdinger G | title = Structural organization and chromosomal localization of Hyal2, a gene encoding a lysosomal hyaluronidase | journal = Genomics | volume = 53 | issue = 2 | pages = 214–9 |date=Dec 1998 | pmid = 9790770 | pmc =  | doi = 10.1006/geno.1998.5472 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HYAL2 hyaluronoglucosaminidase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8692| accessdate = }}</ref>
-| require_manual_inspection = no
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-}}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{GNF_Protein_box
- | image =
- | image_source =
- | PDB =
- | Name = Hyaluronoglucosaminidase 2
- | HGNCid = 5321
- | Symbol = HYAL2
- | AltSymbols =; LUCA2; LuCa-2
- | OMIM = 603551
- | ECnumber =
- | Homologene = 7776
-  | MGIid = 1196334
- | GeneAtlas_image1 = PBB_GE_HYAL2_206855_s_at_tn.png
-  | Function = {{GNF_GO|id=GO:0004415 |text = hyalurononglucosaminidase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
- | Component = {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
-  | Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006027 |text = glycosaminoglycan catabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 8692
-    | Hs_Ensembl = ENSG00000068001
-    | Hs_RefseqProtein = NP_003764
-    | Hs_RefseqmRNA = NM_003773
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 3
-    | Hs_GenLoc_start = 50330225
-    | Hs_GenLoc_end = 50335217
-    | Hs_Uniprot = Q12891
-    | Mm_EntrezGene = 15587
-    | Mm_Ensembl = ENSMUSG00000010047
-    | Mm_RefseqmRNA = NM_010489
-    | Mm_RefseqProtein = NP_034619
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 9
-    | Mm_GenLoc_start = 107427227
-    | Mm_GenLoc_end = 107430872
-    | Mm_Uniprot = Q3UZE4
-  }}
-}}
-'''Hyaluronoglucosaminidase 2''', also known as '''HYAL2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HYAL2 hyaluronoglucosaminidase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8692| accessdate = }}</ref>
 <!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
 {{PBB_Summary
 | section_title =
-| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: HYAL2 hyaluronoglucosaminidase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8692| accessdate = }}</ref>
+| summary_text = 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.<ref name="entrez" />
 }}
+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==
-{{reflist|2}}
+{{reflist}}
 ==Further reading==
 {{refbegin | 2}}
 {{PBB_Further_reading
 | citations =
-*{{cite journal  | author=Lepperdinger G, Müllegger J, Kreil G |title=Hyal2--less active, but more versatile? |journal=Matrix Biol. |volume=20 |issue= 8 |pages= 509-14 |year= 2002 |pmid= 11731268 |doi=  }}
+* {{cite journal  |vauthors=Lepperdinger G, Müllegger J, Kreil G |title=Hyal2--less active, but more versatile? |journal=Matrix Biol. |volume=20 |issue= 8 |pages= 509–14 |year= 2002 |pmid= 11731268 |doi=10.1016/S0945-053X(01)00170-6  }}
-*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
+* {{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
-*{{cite journal  | author=Wei MH, Latif F, Bader S, ''et al.'' |title=Construction of a 600-kilobase cosmid clone contig and generation of a transcriptional map surrounding the lung cancer tumor suppressor gene (TSG) locus on human chromosome 3p21.3: progress toward the isolation of a lung cancer TSG. |journal=Cancer Res. |volume=56 |issue= 7 |pages= 1487-92 |year= 1996 |pmid= 8603390 |doi=  }}
+* {{cite journal  | author=Wei MH |title=Construction of a 600-kilobase cosmid clone contig and generation of a transcriptional map surrounding the lung cancer tumor suppressor gene (TSG) locus on human chromosome 3p21.3: progress toward the isolation of a lung cancer TSG |journal=Cancer Res. |volume=56 |issue= 7 |pages= 1487–92 |year= 1996 |pmid= 8603390 |doi=  |name-list-format=vanc| author2=Latif F  | author3=Bader S  | display-authors=3  | last4=Kashuba  | first4=V  | last5=Chen  | first5=JY  | last6=Duh  | first6=FM  | last7=Sekido  | first7=Y  | last8=Lee  | first8=CC  | last9=Geil  | first9=L  }}
-*{{cite journal  | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
+* {{cite journal  | author=Andersson B |title=A "double adaptor" method for improved shotgun library construction |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138  |name-list-format=vanc| author2=Wentland MA  | author3=Ricafrente JY  | display-authors=3  | last4=Liu  | first4=W  | last5=Gibbs  | first5=RA }}
-*{{cite journal  | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi=  }}
+* {{cite journal  | author=Yu W |title=Large-scale concatenation cDNA sequencing |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi=  10.1101/gr.7.4.353| pmc=139146  |name-list-format=vanc| author2=Andersson B  | author3=Worley KC  | display-authors=3  | last4=Muzny  | first4=DM  | last5=Ding  | first5=Y  | last6=Liu  | first6=W  | last7=Ricafrente  | first7=JY  | last8=Wentland  | first8=MA  | last9=Lennon  | first9=G  }}
-*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
+* {{cite journal  | author=Suzuki Y |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |name-list-format=vanc| author2=Yoshitomo-Nakagawa K  | author3=Maruyama K  | display-authors=3  | last4=Suyama  | first4=A  | last5=Sugano  | first5=S  }}
-*{{cite journal  | author=Lepperdinger G, Strobl B, Kreil G |title=HYAL2, a human gene expressed in many cells, encodes a lysosomal hyaluronidase with a novel type of specificity. |journal=J. Biol. Chem. |volume=273 |issue= 35 |pages= 22466-70 |year= 1998 |pmid= 9712871 |doi=  }}
+* {{cite journal  | author=Sun L |title=Expression profile of hyaluronidase mRNA transcripts in the kidney and in renal cells |journal=Kidney Blood Press. Res. |volume=21 |issue= 6 |pages= 413–8 |year= 1999 |pmid= 9933825 |doi=10.1159/000025893  |name-list-format=vanc| author2=Feusi E  | author3=Sibalic A  | display-authors=3  | last4=Beck-Schimmer  | first4=Beatrice  | last5=wÜThrich  | first5=Rudolf P.  }}
-*{{cite journal  | author=Strobl B, Wechselberger C, Beier DR, Lepperdinger G |title=Structural organization and chromosomal localization of Hyal2, a gene encoding a lysosomal hyaluronidase. |journal=Genomics |volume=53 |issue= 2 |pages= 214-9 |year= 1998 |pmid= 9790770 |doi= 10.1006/geno.1998.5472 }}
+* {{cite journal  |vauthors=Fiszer-Szafarz B, Litynska A, Zou L |title=Human hyaluronidases: electrophoretic multiple forms in somatic tissues and body fluids. Evidence for conserved hyaluronidase potential N-glycosylation sites in different mammalian species |journal=J. Biochem. Biophys. Methods |volume=45 |issue= 2 |pages= 103–16 |year= 2000 |pmid= 10989127 |doi=10.1016/S0165-022X(00)00067-1  }}
-*{{cite journal  | author=Sun L, Feusi E, Sibalic A, ''et al.'' |title=Expression profile of hyaluronidase mRNA transcripts in the kidney and in renal cells. |journal=Kidney Blood Press. Res. |volume=21 |issue= 6 |pages= 413-8 |year= 1999 |pmid= 9933825 |doi=  }}
+* {{cite journal  |vauthors=Lerman MI, Minna JD |title=The 630-kb lung cancer homozygous deletion region on human chromosome 3p21.3: identification and evaluation of the resident candidate tumor suppressor genes. The International Lung Cancer Chromosome 3p21.3 Tumor Suppressor Gene Consortium |journal=Cancer Res. |volume=60 |issue= 21 |pages= 6116–33 |year= 2000 |pmid= 11085536 |doi=  }}
-*{{cite journal  | author=Fiszer-Szafarz B, Litynska A, Zou L |title=Human hyaluronidases: electrophoretic multiple forms in somatic tissues and body fluids. Evidence for conserved hyaluronidase potential N-glycosylation sites in different mammalian species. |journal=J. Biochem. Biophys. Methods |volume=45 |issue= 2 |pages= 103-16 |year= 2000 |pmid= 10989127 |doi=  }}
+* {{cite journal  | author=Rai SK |title=Candidate tumor suppressor HYAL2 is a glycosylphosphatidylinositol (GPI)-anchored cell-surface receptor for jaagsiekte sheep retrovirus, the envelope protein of which mediates oncogenic transformation |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 8 |pages= 4443–8 |year= 2001 |pmid= 11296287 |doi= 10.1073/pnas.071572898  | pmc=31854  |name-list-format=vanc| author2=Duh FM  | author3=Vigdorovich V  | display-authors=3  | last4=Danilkovitch-Miagkova  | first4=A  | last5=Lerman  | first5=MI  | last6=Miller  | first6=AD }}
-*{{cite journal  | author=Lerman MI, Minna JD |title=The 630-kb lung cancer homozygous deletion region on human chromosome 3p21.3: identification and evaluation of the resident candidate tumor suppressor genes. The International Lung Cancer Chromosome 3p21.3 Tumor Suppressor Gene Consortium. |journal=Cancer Res. |volume=60 |issue= 21 |pages= 6116-33 |year= 2000 |pmid= 11085536 |doi=  }}
+* {{cite journal  | author=Delpech B |title=Hyaluronidase is more elevated in human brain metastases than in primary brain tumours |journal=Anticancer Res. |volume=22 |issue= 4 |pages= 2423–7 |year= 2002 |pmid= 12174938 |doi=  |name-list-format=vanc| author2=Laquerriere A  | author3=Maingonnat C  | display-authors=3  | last4=Bertrand  | first4=P  | last5=Freger  | first5=P  }}
-*{{cite journal  | author=Rai SK, Duh FM, Vigdorovich V, ''et al.'' |title=Candidate tumor suppressor HYAL2 is a glycosylphosphatidylinositol (GPI)-anchored cell-surface receptor for jaagsiekte sheep retrovirus, the envelope protein of which mediates oncogenic transformation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 8 |pages= 4443-8 |year= 2001 |pmid= 11296287 |doi= 10.1073/pnas.071572898 }}
+* {{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=Delpech B, Laquerriere A, Maingonnat C, ''et al.'' |title=Hyaluronidase is more elevated in human brain metastases than in primary brain tumours. |journal=Anticancer Res. |volume=22 |issue= 4 |pages= 2423-7 |year= 2002 |pmid= 12174938 |doi=  }}
+* {{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=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  | 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  | author=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=  }}
+* {{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=Danilkovitch-Miagkova A, Duh FM, Kuzmin I, ''et al.'' |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 }}
+* {{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=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=  }}
+* {{cite journal  | author=Gerhard DS |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  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
-*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |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 }}
-*{{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 }}
 }}
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HYAL2: Difference between revisions

Latest revision as of 14:13, 4 November 2018

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