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Gene Review

FBLN2  -  fibulin 2

Homo sapiens

Synonyms: FIBL-2, Fibulin-2
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Disease relevance of FBLN2


High impact information on FBLN2

  • The phenotype of these male cells was examined by immunohistochemistry using a panel of antibodies against alpha-smooth muscle actin (alpha SMA), vimentin, fibulin-2, and leukocyte common antigen (CD45) [3].
  • The same epitopes also participate in endostatin binding to heparan sulfate and sulfatides but not in its binding to the extracellular protein ligands fibulin-1 and fibulin-2 [4].
  • The presence of an EGF motif enhanced the affinity of interaction, and in particular the splice variant containing both EGF motifs had significantly higher affinity for ligands, such as tenascin-R and fibulin-2 [5].
  • Together these results suggest that fibulin-2 functions to bridge laminin-1 and laminin-5 with other extracellular matrix proteins, providing a linkage between the cell surface and the basement membrane [6].
  • Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences [6].

Biological context of FBLN2


Anatomical context of FBLN2


Associations of FBLN2 with chemical compounds


Co-localisations of FBLN2


Other interactions of FBLN2

  • Fibulin-1 and fibulin-2, two recently identified extracellular matrix proteins with a homologous domain structure, are known to bind various extracellular ligands and calcium [14].
  • We propose that, in regenerating skin, fibulin-2 is a late component of the cutaneous microfibrillar apparatus with an earlier existence in a fibrillar matrix mediated by fibronectin [11].
  • Fibulin-2 has also been found to adhere to cells via beta3 integrins [9].
  • UVB irradiation reduced fibulin-5, fibulin-2 and elastin markedly, moderately and weakly, respectively, compared with levels in control nontreated skin [15].
  • CONCLUSIONS: This study shows that deposition of fibulin-2 and elastin is highly co-ordinated, indicating that this protein plays an important role in elastic fibre and microfibril formation in normal and actinically damaged skin [13].

Analytical, diagnostic and therapeutic context of FBLN2

  • Recombinant mouse and human fibulin-2 were obtained as disulfide-bonded trimers from transfected kidney cell clones and used in solid phase, biosensor and radioligand binding assays [10].
  • Surface plasmon resonance assays demonstrated for fibulin-2 binding to nidogen and fibronectin high equilibrium dissociation constants (0.5 to 1 microM) due to a rapid initial dissociation of the complexes [10].
  • We report the temporo-spatial expression of fibulin-2 in skin regenerating from keratinocyte autografts [11].
  • By confocal microscopy, fibulin-1 and fibulin-2 immunostainings were co-localized with fibronectin in the adherent layer of long-term BM cultures [9].
  • This molecule was identified by Western blotting as fibulin-2, a recently identified extracellular matrix protein [6].


  1. Fibulin-2 exhibits high degree of variability, but no structural changes concordant with abdominal aortic aneurysms. Kuivaniemi, H., Marshall, A., Ganguly, A., Chu, M.L., Abbott, W.M., Tromp, G. Eur. J. Hum. Genet. (1998) [Pubmed]
  2. Fibulin-2: genetic mapping and exclusion as a candidate gene in Marfan syndrome type 2. Collod, G., Chu, M.L., Sasaki, T., Coulon, M., Timpl, R., Renkart, L., Weissenbach, J., Jondeau, G., Bourdarias, J.P., Junien, C., Boileau, C. Eur. J. Hum. Genet. (1996) [Pubmed]
  3. A significant proportion of myofibroblasts are of bone marrow origin in human liver fibrosis. Forbes, S.J., Russo, F.P., Rey, V., Burra, P., Rugge, M., Wright, N.A., Alison, M.R. Gastroenterology (2004) [Pubmed]
  4. Structural basis and potential role of heparin/heparan sulfate binding to the angiogenesis inhibitor endostatin. Sasaki, T., Larsson, H., Kreuger, J., Salmivirta, M., Claesson-Welsh, L., Lindahl, U., Hohenester, E., Timpl, R. EMBO J. (1999) [Pubmed]
  5. Alternative splicing in the aggrecan G3 domain influences binding interactions with tenascin-C and other extracellular matrix proteins. Day, J.M., Olin, A.I., Murdoch, A.D., Canfield, A., Sasaki, T., Timpl, R., Hardingham, T.E., Aspberg, A. J. Biol. Chem. (2004) [Pubmed]
  6. Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences. Utani, A., Nomizu, M., Yamada, Y. J. Biol. Chem. (1997) [Pubmed]
  7. Fibulin-2 (FBLN2): human cDNA sequence, mRNA expression, and mapping of the gene on human and mouse chromosomes. Zhang, R.Z., Pan, T.C., Zhang, Z.Y., Mattei, M.G., Timpl, R., Chu, M.L. Genomics (1994) [Pubmed]
  8. Fibrillin-1 and fibulin-2 interact and are colocalized in some tissues. Reinhardt, D.P., Sasaki, T., Dzamba, B.J., Keene, D.R., Chu, M.L., Göhring, W., Timpl, R., Sakai, L.Y. J. Biol. Chem. (1996) [Pubmed]
  9. Association of extracellular matrix proteins fibulin-1 and fibulin-2 with fibronectin in bone marrow stroma. Gu, Y.C., Nilsson, K., Eng, H., Ekblom, M. Br. J. Haematol. (2000) [Pubmed]
  10. Binding of mouse and human fibulin-2 to extracellular matrix ligands. Sasaki, T., Göhring, W., Pan, T.C., Chu, M.L., Timpl, R. J. Mol. Biol. (1995) [Pubmed]
  11. Confocal laser scanning analysis of the association of fibulin-2 with fibrillin-1 and fibronectin define different stages of skin regeneration. Raghunath, M., Tschödrich-Rotter, M., Sasaki, T., Meuli, M., Chu, M.L., Timpl, R. J. Invest. Dermatol. (1999) [Pubmed]
  12. Structural and functional analysis of the recombinant G domain of the laminin alpha4 chain and its proteolytic processing in tissues. Talts, J.F., Sasaki, T., Miosge, N., Göhring, W., Mann, K., Mayne, R., Timpl, R. J. Biol. Chem. (2000) [Pubmed]
  13. Increased deposition of fibulin-2 in solar elastosis and its colocalization with elastic fibres. Hunzelmann, N., Nischt, R., Brenneisen, P., Eickert, A., Krieg, T. Br. J. Dermatol. (2001) [Pubmed]
  14. The extracellular matrix proteins fibulin-1 and fibulin-2 in the early human embryo. Miosge, N., Götz, W., Sasaki, T., Chu, M.L., Timpl, R., Herken, R. Histochem. J. (1996) [Pubmed]
  15. Fibulin-5 deposition in human skin: decrease with ageing and ultraviolet B exposure and increase in solar elastosis. Kadoya, K., Sasaki, T., Kostka, G., Timpl, R., Matsuzaki, K., Kumagai, N., Sakai, L.Y., Nishiyama, T., Amano, S. Br. J. Dermatol. (2005) [Pubmed]
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