Glypican 2: Difference between revisions

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{{Infobox_gene}}
{{Infobox_gene}}
'''Glypican 2''' ('''GPC2'''), also known '''cerebroglycan''', is a [[protein]] which in humans is encoded by the ''GPC2'' [[gene]].<ref name="pmid8294498">{{cite journal |vauthors=Stipp CS, Litwack ED, Lander AD | title = Cerebroglycan: an integral membrane heparan sulfate proteoglycan that is unique to the developing nervous system and expressed specifically during neuronal differentiation | journal = J. Cell Biol. | volume = 124 | issue = 1–2 | pages = 149–160 |date=January 1994 | pmid = 8294498 | pmc = 2119891 | doi = 10.1083/jcb.124.1.149 | url =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: GPC2 glypican 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=221914| accessdate = }}</ref>
'''Glypican 2''' ('''GPC2'''), also known '''cerebroglycan''', is a [[protein]] which in humans is encoded by the ''GPC2'' [[gene]].<ref name="pmid8294498">{{cite journal | vauthors = Stipp CS, Litwack ED, Lander AD | title = Cerebroglycan: an integral membrane heparan sulfate proteoglycan that is unique to the developing nervous system and expressed specifically during neuronal differentiation | journal = The Journal of Cell Biology | volume = 124 | issue = 1-2 | pages = 149–60 | date = January 1994 | pmid = 8294498 | pmc = 2119891 | doi = 10.1083/jcb.124.1.149 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: GPC2 glypican 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=221914| access-date = }}</ref>


==Function==
== Function ==


Cerebroglycan is a [[glycophosphatidylinositol]]-linked integral membrane [[heparan sulfate]] [[proteoglycan]] found in the  
Cerebroglycan is a [[glycophosphatidylinositol]]-linked integral membrane [[heparan sulfate]] [[proteoglycan]] found in the  
[[developmental biology|developing]] nervous system.  Cerebroglycan participates in [[cell adhesion]] and is thought to regulate the growth and [[axon guidance|guidance]] of [[axon]]s.<ref name="pmid9133438">{{cite journal |vauthors=Ivins JK, Litwack ED, Kumbasar A, Stipp CS, Lander AD | title = Cerebroglycan, a developmentally regulated cell-surface heparan sulfate proteoglycan, is expressed on developing axons and growth cones | journal = Dev. Biol. | volume = 184 | issue = 2 | pages = 320–332 |date=April 1997 | pmid = 9133438 | doi = 10.1006/dbio.1997.8532 | url =  }}</ref> Cerebroglycan has especially high affinity for [[laminin, alpha 1|laminin-1]].<ref name="pmid9949192">{{cite journal |vauthors=Herndon ME, Stipp CS, Lander AD | title = Interactions of neural glycosaminoglycans and proteoglycans with protein ligands: assessment of selectivity, heterogeneity and the participation of core proteins in binding | journal = Glycobiology | volume = 9 | issue = 2 | pages = 143–155 |date=February 1999 | pmid = 9949192 | doi = 10.1093/glycob/9.2.143 | url =  }}</ref>
[[developmental biology|developing]] nervous system.  Cerebroglycan participates in [[cell adhesion]] and is thought to regulate the growth and [[axon guidance|guidance]] of [[axon]]s.<ref name="pmid9133438">{{cite journal | vauthors = Ivins JK, Litwack ED, Kumbasar A, Stipp CS, Lander AD | title = Cerebroglycan, a developmentally regulated cell-surface heparan sulfate proteoglycan, is expressed on developing axons and growth cones | journal = Developmental Biology | volume = 184 | issue = 2 | pages = 320–32 | date = April 1997 | pmid = 9133438 | doi = 10.1006/dbio.1997.8532 }}</ref> Cerebroglycan has especially high affinity for [[laminin, alpha 1|laminin-1]].<ref name="pmid9949192">{{cite journal | vauthors = Herndon ME, Stipp CS, Lander AD | title = Interactions of neural glycosaminoglycans and proteoglycans with protein ligands: assessment of selectivity, heterogeneity and the participation of core proteins in binding | journal = Glycobiology | volume = 9 | issue = 2 | pages = 143–55 | date = February 1999 | pmid = 9949192 | doi = 10.1093/glycob/9.2.143 }}</ref>


==See also==
== Implications in cancer ==
GPC2 is highly expressed in about half of neuroblastoma cases and that high GPC2 expression correlates with poor overall survival, suggesting GPC2 as a therapeutic target in neuroblastoma.<ref name = "Li_2017">{{cite journal | vauthors = Li N, Fu H, Hewitt SM, Dimitrov DS, Ho M | title = Therapeutically targeting glypican-2 via single-domain antibody-based chimeric antigen receptors and immunotoxins in neuroblastoma | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 114 | issue = 32 | pages = E6623–E6631 | date = August 2017 | pmid = 28739923 | pmc = 5559039 | doi = 10.1073/pnas.1706055114 }}</ref><ref name="Bosse_2017">{{cite journal | vauthors = Bosse KR, Raman P, Zhu Z, Lane M, Martinez D, Heitzeneder S, Rathi KS, Kendsersky NM, Randall M, Donovan L, Morrissy S, Sussman RT, Zhelev DV, Feng Y, Wang Y, Hwang J, Lopez G, Harenza JL, Wei JS, Pawel B, Bhatti T, Santi M, Ganguly A, Khan J, Marra MA, Taylor MD, Dimitrov DS, Mackall CL, Maris JM | display-authors = 6 | title = Identification of GPC2 as an Oncoprotein and Candidate Immunotherapeutic Target in High-Risk Neuroblastoma | journal = Cancer Cell | volume = 32 | issue = 3 | pages = 295–309.e12 | date = September 2017 | pmid = 28898695 | doi = 10.1016/j.ccell.2017.08.003 }}</ref> GPC2 silencing inactivates Wnt/β-catenin signaling and reduces the expression of N-Myc, an oncogenic driver of neuroblastoma tumorigenesis. Immunotoxins and chimeric antigen receptor (CAR) T cells targeting GPC2 inhibit neuroblastoma growth in mouse models.<ref name = "Li_2017" />
 
== See also ==
* [[Glypican]]
* [[Glypican]]


==References==
== References ==
{{reflist}}
{{reflist}}


==External links==
== External links ==
* {{MeshName|GPC2+protein,+human}}
* {{MeshName|GPC2+protein,+human}}


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{{protein-stub}}

Latest revision as of 05:03, 2 June 2018

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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

Glypican 2 (GPC2), also known cerebroglycan, is a protein which in humans is encoded by the GPC2 gene.[1][2]

Function

Cerebroglycan is a glycophosphatidylinositol-linked integral membrane heparan sulfate proteoglycan found in the developing nervous system. Cerebroglycan participates in cell adhesion and is thought to regulate the growth and guidance of axons.[3] Cerebroglycan has especially high affinity for laminin-1.[4]

Implications in cancer

GPC2 is highly expressed in about half of neuroblastoma cases and that high GPC2 expression correlates with poor overall survival, suggesting GPC2 as a therapeutic target in neuroblastoma.[5][6] GPC2 silencing inactivates Wnt/β-catenin signaling and reduces the expression of N-Myc, an oncogenic driver of neuroblastoma tumorigenesis. Immunotoxins and chimeric antigen receptor (CAR) T cells targeting GPC2 inhibit neuroblastoma growth in mouse models.[5]

See also

References

  1. Stipp CS, Litwack ED, Lander AD (January 1994). "Cerebroglycan: an integral membrane heparan sulfate proteoglycan that is unique to the developing nervous system and expressed specifically during neuronal differentiation". The Journal of Cell Biology. 124 (1–2): 149–60. doi:10.1083/jcb.124.1.149. PMC 2119891. PMID 8294498.
  2. "Entrez Gene: GPC2 glypican 2".
  3. Ivins JK, Litwack ED, Kumbasar A, Stipp CS, Lander AD (April 1997). "Cerebroglycan, a developmentally regulated cell-surface heparan sulfate proteoglycan, is expressed on developing axons and growth cones". Developmental Biology. 184 (2): 320–32. doi:10.1006/dbio.1997.8532. PMID 9133438.
  4. Herndon ME, Stipp CS, Lander AD (February 1999). "Interactions of neural glycosaminoglycans and proteoglycans with protein ligands: assessment of selectivity, heterogeneity and the participation of core proteins in binding". Glycobiology. 9 (2): 143–55. doi:10.1093/glycob/9.2.143. PMID 9949192.
  5. 5.0 5.1 Li N, Fu H, Hewitt SM, Dimitrov DS, Ho M (August 2017). "Therapeutically targeting glypican-2 via single-domain antibody-based chimeric antigen receptors and immunotoxins in neuroblastoma". Proceedings of the National Academy of Sciences of the United States of America. 114 (32): E6623–E6631. doi:10.1073/pnas.1706055114. PMC 5559039. PMID 28739923.
  6. Bosse KR, Raman P, Zhu Z, Lane M, Martinez D, Heitzeneder S, et al. (September 2017). "Identification of GPC2 as an Oncoprotein and Candidate Immunotherapeutic Target in High-Risk Neuroblastoma". Cancer Cell. 32 (3): 295–309.e12. doi:10.1016/j.ccell.2017.08.003. PMID 28898695.

External links