Latent transforming growth factor β-binding protein 1 interacts with fibrillin and is a microfibril-associated protein

Isogai, Zenzo, Ono, Robert N., Ushiro, Shin, Keene, Douglas R., Chen, Yan, Mazzieri, Roberta, Charbonneau, Noe L., Reinhardt, Dieter P., Rifkin, Daniel B. and Sakai, Lynn Y. (2003) Latent transforming growth factor β-binding protein 1 interacts with fibrillin and is a microfibril-associated protein. Journal of Biological Chemistry, 278 4: 2750-2757. doi:10.1074/jbc.M209256200

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Author Isogai, Zenzo
Ono, Robert N.
Ushiro, Shin
Keene, Douglas R.
Chen, Yan
Mazzieri, Roberta
Charbonneau, Noe L.
Reinhardt, Dieter P.
Rifkin, Daniel B.
Sakai, Lynn Y.
Title Latent transforming growth factor β-binding protein 1 interacts with fibrillin and is a microfibril-associated protein
Formatted title
Latent transforming growth factor β-binding protein 1 interacts with fibrillin and is a microfibril-associated protein
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 2003-01-24
Year available 2002
Sub-type Article (original research)
DOI 10.1074/jbc.M209256200
Open Access Status File (Publisher version)
Volume 278
Issue 4
Start page 2750
End page 2757
Total pages 8
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Formatted abstract
Latent transforming growth factor β-binding protein I (LTBP-1) targets latent complexes of transforming growth factor β to the extracellular matrix, where the latent cytokine is subsequently activated by several dif-ferent mechanisms. Fibrillins are extracellular matrix macromolecules whose primary function is architectur-al: fibrillins assemble into ultrastructurally distinct mi-crofibrils that are ubiquitous in the connective tissue space. LTBPs and fibrillins are highly homologous mol-ecules, and colocalization in the matrix of cultured cells has been reported. To address whether LTBP-1 func-tions architecturally like fibrillins, microfibrils were ex-tracted from tissues and analyzed immunochemically. In addition, binding studies were conducted to deter-mine whether LTBP-1 interacts with fibrillins. LTBP-1 was not detected in extracted beaded-string microfi-brils, suggesting that LTBP-1 is not an integral struc-tural component of microfibrils. However, binding studies demonstrated interactions between LTBP-1 and fibrillins. The binding site was within three domains of the LTBP-1 C terminus, and in fibrillin-1 the site was defined within four domains near the N terminus. Immunolocalization data were consistent with the hypothesis that LTBP-1 is a fibrillin-associated protein present in certain tissues but not in others. In tissues where LTBP-1 is not expressed, LTBP-4 may substitute for LTBP-1, because the C-terminal end of LTBP-4 binds equally well to fibrillin. A model depicting the relationship between LTBP-1 and fibrillin microfibrils is proposed.
Keyword Biochemistry & Molecular Biology
Biochemistry & Molecular Biology
BIOCHEMISTRY & MOLECULAR BIOLOGY
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID CA 23753
DE13742
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: UQ Diamantina Institute Publications
 
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