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Fibulin-2 is a protein that in humans is encoded by the FBLN2 gene.[5][6]

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.[6]

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.[7]

Interactions

FBLN2 has been shown to interact with Laminin, alpha 1,[8][9] Laminin, alpha 5[8] and Perlecan.[10][11]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000163520Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000064080Ensembl, May 2017
  3. ^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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): 425–430. doi:10.1006/geno.1994.1404. PMID 7806230.
  6. ^ a b EntrezGene 2199 “FBLN2 fibulin 2 [ Homo sapiens (human) ]”
  7. ^ Sofela AA, Hilton DA, Ammoun S, Baiz D, Adams CL, Ercolano E, et al. (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.
  8. ^ a b 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”. The Journal of Biological Chemistry. 272 (5): 2814–2820. doi:10.1074/jbc.272.5.2814. PMID 9006922.
  9. ^ Talts JF, Sasaki T, Miosge N, Göhring W, Mann K, Mayne R, et al. (November 2000). “Structural and functional analysis of the recombinant G domain of the laminin alpha4 chain and its proteolytic processing in tissues”. The Journal of Biological Chemistry. 275 (45): 35192–35199. doi:10.1074/jbc.M003261200. PMID 10934193.
  10. ^ 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”. Journal of Molecular Biology. 311 (3): 529–541. doi:10.1006/jmbi.2001.4878. PMID 11493006.
  11. ^ Sasaki T, Göhring W, Pan TC, Chu ML, Timpl R (December 1995). “Binding of mouse and human fibulin-2 to extracellular matrix ligands”. Journal of Molecular Biology. 254 (5): 892–899. doi:10.1006/jmbi.1995.0664. PMID 7500359.

Further reading