FBLN2

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Template:Short description An Error has occurred retrieving Wikidata item for infobox Fibulin-2 is a protein that in humans is encoded by the FBLN2 gene.[1][2]

This gene encodes an extracellular matrix protein, which belongs to the fibulin family. This protein binds various extracellular ligands and calcium. It may play a role during organ development, in particular, during the differentiation of heart, skeletal and neuronal structures. Alternatively spliced transcript variants encoding different isoforms have been identified.[2]

Its role as a biomarker for meningiomas (a common tumour affecting the central nervous system) was recently described where a blood test can predict whether patients have a grade II meningiomas (poor outcome) and not a grade I meningioma (better outcome), without the need for a surgical biopsy.[3]

Interactions

FBLN2 has been shown to interact with Laminin, alpha 1,[4][5] Laminin, alpha 5[4] and Perlecan.[6][7]

References

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  1. ^ Page Module:Citation/CS1/styles.css has no content.Zhang RZ, Pan TC, Zhang ZY, Mattei MG, Timpl R, Chu ML (January 1995). "Fibulin-2 (FBLN2): human cDNA sequence, mRNA expression, and mapping of the gene on human and mouse chromosomes". Genomics. 22 (2): 425–30. doi:10.1006/geno.1994.1404. PMID 7806230.
  2. ^ a b EntrezGene 2199 "FBLN2 fibulin 2 [ Homo sapiens (human) ]"
  3. ^ Page Module:Citation/CS1/styles.css has no content.Sofela, Agbolahan A.; Hilton, David A.; Ammoun, Sylwia; Baiz, Daniele; Adams, Claire L.; Ercolano, Emanuela; Jenkinson, Michael D.; Kurian, Kathreena M.; Teo, Mario; Whitfield, Peter C.; Sahm, Felix; Hanemann, C. Oliver (8 January 2021). "Fibulin-2: A Novel Biomarker for Differentiating Grade II from Grade I Meningiomas". International Journal of Molecular Sciences. 22 (2): 560. doi:10.3390/ijms22020560. PMC 7827565. PMID 33429944.
  4. ^ a b Page Module:Citation/CS1/styles.css has no content.Utani, A; Nomizu M; Yamada Y (January 1997). "Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences". J. Biol. Chem. 272 (5): 2814–20. doi:10.1074/jbc.272.5.2814. PMID 9006922.
  5. ^ Page Module:Citation/CS1/styles.css has no content.Talts, J F; Sasaki T; Miosge N; Göhring W; Mann K; Mayne R; Timpl R (November 2000). "Structural and functional analysis of the recombinant G domain of the laminin alpha4 chain and its proteolytic processing in tissues". J. Biol. Chem. 275 (45): 35192–9. doi:10.1074/jbc.M003261200. PMID 10934193.
  6. ^ Page Module:Citation/CS1/styles.css has no content.Hopf, M; Göhring W; Mann K; Timpl R (August 2001). "Mapping of binding sites for nidogens, fibulin-2, fibronectin and heparin to different IG modules of perlecan". J. Mol. Biol. 311 (3): 529–41. doi:10.1006/jmbi.2001.4878. PMID 11493006.
  7. ^ Page Module:Citation/CS1/styles.css has no content.Sasaki, T; Göhring W; Pan T C; Chu M L; Timpl R (December 1995). "Binding of mouse and human fibulin-2 to extracellular matrix ligands". J. Mol. Biol. 254 (5): 892–9. doi:10.1006/jmbi.1995.0664. PMID 7500359.

Further reading

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