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Gene Review

Fbln1  -  fibulin 1

Mus musculus

Synonyms: BM-90, Basement-membrane protein 90, FIBL-1, Fibulin-1
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Disease relevance of Fbln1

  • Attempts to rescue the placental phenotypes of a congenic model of interspecies hybrid placental dysplasia (IHPD) by normalizing expression of Fbln1 proved that Fbln1 alone is not the key cause of phenotypes in these models of placental hyperplasia [1].
  • MEM-2 represents a useful new tool for the study of Fbln-1 in breast cancer [2].

High impact information on Fbln1


Biological context of Fbln1

  • Fibulin-1 is particularly well expressed in the endocardial cushion tissue (ECT) during embryogenesis and we therefore compared the expression patterns of fibulin-1 and -2 in the developing mouse heart [7].
  • By searching the database we identified most of the exons encoding the human fibulin-1 gene and showed that its exon-intron organization is similar to that of the mouse gene [8].
  • Fibulin-1 and fibulin-2 expression during organogenesis in the developing mouse embryo [9].
  • Here, we show that a murine placental overgrowth phenotype is associated with elevated Fbln1 transcript levels, suggesting that the gene and its product have a functional role in placentation [1].
  • Absence of fibulin-1 caused considerable blood loss but did not compromise blood clotting [6].

Anatomical context of Fbln1


Associations of Fbln1 with chemical compounds

  • Self aggregation into nest-like oligomers was observed at high concentrations of fibulin-1 which was not sensitive to EDTA [11].
  • Evidence that fibulin family members contribute to the steroid-dependent extravascular sequestration of sex hormone-binding globulin [12].
  • Fibulin-1 is a calcium-binding glycoprotein present in the extracellular matrix and in the serum [13].
  • Cultured human endometrial stromal cells treated with progesterone responded with a dramatic increase of fibulin-1 protein expression [14].
  • Altogether the results show a cycle-dependent regulation of endometrial fibulin-1 expression controlled by both progesterone and estrogen [14].
  • We found that the recombinant TM14 protein was glycosylated with N-linked oligosaccharides and interacted with heparin, fibronectin, fibulin-1, and dentin sialophosphoprotein [15].

Regulatory relationships of Fbln1

  • Our studies show that fibulin-1 is expressed surrounding the primordial VSMCs of the vessel wall before elastin precursors are present and suggest that differential expression of the JB3 antigen (Wunsch et al., 1994) may be indicative of early diversity among embryonic VSMCs [16].

Other interactions of Fbln1

  • Different susceptibilities of fibulin-1 and fibulin-2 to cleavage by matrix metalloproteinases and other tissue proteases [17].
  • Fibulin-1 (95 kDa) was readily cleaved by leucocyte elastase, weakly by matrilysin and not by the other proteases [17].
  • The laminin connector molecule, nidogen-1, had a distribution similar to that of laminin beta(1) and gamma(1), whereas fibulin-1 and -2, which compete with nidogen-1, were mostly confined to blood vessels [18].
  • The extracellular matrix protein fibulin-1 (FBLN1) is an important component of blood vessel walls, as shown by the lethality of mice with homozygous targeted deletion of the Fbln1 gene [1].
  • The protein BM-90 was solubilized from the mouse Engelbreth-Holm-Swarm tumor with neutral buffers in molar yields lower (15-30%) than found for other basement membrane proteins (e.g. laminin, BM-40) [19].

Analytical, diagnostic and therapeutic context of Fbln1


  1. Expression and functional analysis of fibulin-1 (Fbln1) during normal and abnormal placental development of the mouse. Singh, U., Sun, T., Larsson, T., Elliott, R.W., Kostka, G., Fundele, R.H. Placenta (2006) [Pubmed]
  2. Monoclonal antibody to fibulin-1 generated by genetic immunization. Pupa, S.M., Forti, S., Invernizzi, A.M., Giovanazzi, R., Twal, W.O., Argraves, W.S., Ménard, S. J. Cell. Biochem. (2003) [Pubmed]
  3. Structure, function and tissue forms of the C-terminal globular domain of collagen XVIII containing the angiogenesis inhibitor endostatin. Sasaki, T., Fukai, N., Mann, K., Göhring, W., Olsen, B.R., Timpl, R. EMBO J. (1998) [Pubmed]
  4. Structure and expression of fibulin-2, a novel extracellular matrix protein with multiple EGF-like repeats and consensus motifs for calcium binding. Pan, T.C., Sasaki, T., Zhang, R.Z., Fässler, R., Timpl, R., Chu, M.L. J. Cell Biol. (1993) [Pubmed]
  5. Altered vascular remodeling in fibulin-5-deficient mice reveals a role of fibulin-5 in smooth muscle cell proliferation and migration. Spencer, J.A., Hacker, S.L., Davis, E.C., Mecham, R.P., Knutsen, R.H., Li, D.Y., Gerard, R.D., Richardson, J.A., Olson, E.N., Yanagisawa, H. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  6. Perinatal lethality and endothelial cell abnormalities in several vessel compartments of fibulin-1-deficient mice. Kostka, G., Giltay, R., Bloch, W., Addicks, K., Timpl, R., Fässler, R., Chu, M.L. Mol. Cell. Biol. (2001) [Pubmed]
  7. Extracellular matrix protein fibulin-2 is expressed in the embryonic endocardial cushion tissue and is a prominent component of valves in adult heart. Zhang, H.Y., Chu, M.L., Pan, T.C., Sasaki, T., Timpl, R., Ekblom, P. Dev. Biol. (1995) [Pubmed]
  8. Complete exon-intron organization of the mouse fibulin-1 gene and its comparison with the human fibulin-1 gene. Pan, T.C., Kostka, G., Zhang, R.Z., Timpl, R., Chu, M.L. FEBS Lett. (1999) [Pubmed]
  9. Fibulin-1 and fibulin-2 expression during organogenesis in the developing mouse embryo. Zhang, H.Y., Timpl, R., Sasaki, T., Chu, M.L., Ekblom, P. Dev. Dyn. (1996) [Pubmed]
  10. Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement-membrane ligands. Pan, T.C., Kluge, M., Zhang, R.Z., Mayer, U., Timpl, R., Chu, M.L. Eur. J. Biochem. (1993) [Pubmed]
  11. Structural characterization of two variants of fibulin-1 that differ in nidogen affinity. Sasaki, T., Kostka, G., Göhring, W., Wiedemann, H., Mann, K., Chu, M.L., Timpl, R. J. Mol. Biol. (1995) [Pubmed]
  12. Evidence that fibulin family members contribute to the steroid-dependent extravascular sequestration of sex hormone-binding globulin. Ng, K.M., Catalano, M.G., Pinós, T., Selva, D.M., Avvakumov, G.V., Munell, F., Hammond, G.L. J. Biol. Chem. (2006) [Pubmed]
  13. The fibulin-1 gene (FBLN1) is located on human chromosome 22 and on mouse chromosome 15. Mattei, M.G., Pan, T.C., Zhang, R.Z., Timpl, R., Chu, M.L. Genomics (1994) [Pubmed]
  14. Cycle-dependent endometrial expression and hormonal regulation of the fibulin-1 gene. Haendler, B., Yamanouchi, H., Lessey, B.A., Chwalisz, K., Hess-Stumpp, H. Mol. Reprod. Dev. (2004) [Pubmed]
  15. TM14 is a new member of the fibulin family (fibulin-7) that interacts with extracellular matrix molecules and is active for cell binding. de Vega, S., Iwamoto, T., Nakamura, T., Hozumi, K., McKnight, D.A., Fisher, L.W., Fukumoto, S., Yamada, Y. J. Biol. Chem. (2007) [Pubmed]
  16. Development of the aortic vessel wall as defined by vascular smooth muscle and extracellular matrix markers. Hungerford, J.E., Owens, G.K., Argraves, W.S., Little, C.D. Dev. Biol. (1996) [Pubmed]
  17. Different susceptibilities of fibulin-1 and fibulin-2 to cleavage by matrix metalloproteinases and other tissue proteases. Sasaki, T., Mann, K., Murphy, G., Chu, M.L., Timpl, R. Eur. J. Biochem. (1996) [Pubmed]
  18. Distinct distribution of laminin and its integrin receptors in the pancreas. Jiang, F.X., Naselli, G., Harrison, L.C. J. Histochem. Cytochem. (2002) [Pubmed]
  19. Characterization of a novel calcium-binding 90-kDa glycoprotein (BM-90) shared by basement membranes and serum. Kluge, M., Mann, K., Dziadek, M., Timpl, R. Eur. J. Biochem. (1990) [Pubmed]
  20. Fibulins: physiological and disease perspectives. Argraves, W.S., Greene, L.M., Cooley, M.A., Gallagher, W.M. EMBO Rep. (2003) [Pubmed]
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