spacer gif spacer gif spacer gif spacer gif Propose a workshop for 2011 spacer gif
 QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    


This Article
Right arrow Full Text (PDF)
Right arrow References
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Unsold, C.
Right arrow Articles by Keski-Oja, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Unsold, C.
Right arrow Articles by Keski-Oja, J.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Journal of Cell Science, Vol 114, Issue 1 187-197, Copyright © 2001 by Company of Biologists


JOURNAL ARTICLES

Latent TGF-beta binding protein LTBP-1 contains three potential extracellular matrix interacting domains

C Unsold, M Hyytiainen, L Bruckner-Tuderman and J Keski-Oja
Departments of Pathology and Virology, The Haartman Institute and Helsinki University Hospital, University of Helsinki, FIN-00014 Helsinki, Finland.

Latent TGF-beta binding proteins (LTBPs) are components of the extracellular matrix (ECM). They belong to the fibrillin/LTBP-superfamily, and are high molecular weight glycoproteins characterized by EGF-like repeats and 8-Cys repeats. Most LTBPs associate with the small latent forms of TGF-beta. Their roles include to facilitate the secretion of latent TGF-beta and to target it to the ECM. In order to identify new matrix-binding domains of LTBP-1 and to characterize their association with the extracellular matrix, we have produced (in a mammalian expression system) partly overlapping recombinant fragments of its shorter form, LTBP-1S, and analyzed the binding of the purified fusion proteins to extracellular matrices of cultured human dermal and lung fibroblasts. Recombinant fragments from three different regions of the N- and C-termini showed affinity to the matrix. These interacting regions contain either the first (hybrid), second or fourth 8-Cys domains of the LTBP-1S molecule. They bound independently to the matrix. Each of them had an ability to inhibit the association of native exogenous LTBP-1 with fibroblast extracellular matrix. The interactions of the LTBP-1 fragments with the extracellular matrix resisted treatment with sodium deoxycholate, suggesting strong, possibly covalent binding. The binding occurred in a time- and dose-dependent fashion. The N-terminal fragments bound more readily to the matrices. With all fragments the binding took place both with intact fibroblast matrices and with matrices isolated by sodium deoxycholate. When using CHO cell layers, which form sparse matrices, only the N-terminal fragment of LTBP-1 was efficiently incorporated. The association of the binding fragments with isolated matrices was enhanced by soluble, cell-derived factors. The current data suggest that LTBP-1 contains three different domains with an ability to associate with the extracellular matrix.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
R. N. Ono, G. Sengle, N. L. Charbonneau, V. Carlberg, H. P. Bachinger, T. Sasaki, S. Lee-Arteaga, L. Zilberberg, D. B. Rifkin, F. Ramirez, et al.
Latent Transforming Growth Factor {beta}-binding Proteins and Fibulins Compete for Fibrillin-1 and Exhibit Exquisite Specificities in Binding Sites
J. Biol. Chem., June 19, 2009; 284(25): 16872 - 16881.
[Abstract] [Full Text] [PDF]


Home page
JCBHome page
P.-J. Wipff, D. B. Rifkin, J.-J. Meister, and B. Hinz
Myofibroblast contraction activates latent TGF- 1 from the extracellular matrix
J. Cell Biol., December 17, 2007; 179(6): 1311 - 1323.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Q. Chen, P. Sivakumar, C. Barley, D. M. Peters, R. R. Gomes, M. C. Farach-Carson, and S. L. Dallas
Potential Role for Heparan Sulfate Proteoglycans in Regulation of Transforming Growth Factor-beta (TGF-beta) by Modulating Assembly of Latent TGF-beta-binding Protein-1
J. Biol. Chem., September 7, 2007; 282(36): 26418 - 26430.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Respir. Cell Mol. Bio.Home page
M. M. Choe, P. H. S. Sporn, and M. A. Swartz
Extracellular Matrix Remodeling by Dynamic Strain in a Three-Dimensional Tissue-Engineered Human Airway Wall Model
Am. J. Respir. Cell Mol. Biol., September 1, 2006; 35(3): 306 - 313.
[Abstract] [Full Text] [PDF]


Home page
FASEB J.Home page
L. Fontana, Y. Chen, P. Prijatelj, T. Sakai, R. Fassler, L. Y. Sakai, and D. B. Rifkin
Fibronectin is required for integrin {alpha}v{beta}6-mediated activation of latent TGF-{beta} complexes containing LTBP-1
FASEB J, November 1, 2005; 19(13): 1798 - 1808.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
R. Mazzieri, V. Jurukovski, H. Obata, J. Sung, A. Platt, E. Annes, N. Karaman-Jurukovska, P.-E. Gleizes, and D. B. Rifkin
Expression of truncated latent TGF-{beta}-binding protein modulates TGF-{beta} signaling
J. Cell Sci., May 15, 2005; 118(10): 2177 - 2187.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. L. Dallas, P. Sivakumar, C. J. P. Jones, Q. Chen, D. M. Peters, D. F. Mosher, M. J. Humphries, and C. M. Kielty
Fibronectin Regulates Latent Transforming Growth Factor-{beta} (TGF{beta}) by Controlling Matrix Assembly of Latent TGF{beta}-binding Protein-1
J. Biol. Chem., May 13, 2005; 280(19): 18871 - 18880.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. B. Rifkin
Latent Transforming Growth Factor-{beta} (TGF-{beta}) Binding Proteins: Orchestrators of TGF-{beta} Availability
J. Biol. Chem., March 4, 2005; 280(9): 7409 - 7412.
[Full Text] [PDF]


Home page
JCBHome page
J. P. Annes, Y. Chen, J. S. Munger, and D. B. Rifkin
Integrin {alpha}V{beta}6-mediated activation of latent TGF-{beta} requires the latent TGF-{beta} binding protein-1
J. Cell Biol., June 7, 2004; 165(5): 723 - 734.
[Abstract] [Full Text] [PDF]


Home page
JCBHome page
M. Hyytiainen and J. Keski-Oja
Latent TGF-{beta} binding protein LTBP-2 decreases fibroblast adhesion to fibronectin
J. Cell Biol., December 22, 2003; 163(6): 1363 - 1374.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. Vehvilainen, M. Hyytiainen, and J. Keski-Oja
Latent Transforming Growth Factor-{beta}-binding Protein 2 Is an Adhesion Protein for Melanoma Cells
J. Biol. Chem., June 27, 2003; 278(27): 24705 - 24713.
[Abstract] [Full Text] [PDF]


Home page
DiabetesHome page
T. Kanzaki and M. Otabe
Latent Transforming Growth Factor-{beta} Binding Protein-1, a Component of Latent Transforming Growth Factor-{beta} Complex, Accelerates the Migration of Aortic Smooth Muscle Cells in Diabetic Rats Through Integrin-{beta}3
Diabetes, March 1, 2003; 52(3): 824 - 828.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Z. Isogai, R. N. Ono, S. Ushiro, D. R. Keene, Y. Chen, R. Mazzieri, N. L. Charbonneau, D. P. Reinhardt, D. B. Rifkin, and L. Y. Sakai
Latent Transforming Growth Factor beta -binding Protein 1 Interacts with Fibrillin and Is a Microfibril-associated Protein
J. Biol. Chem., January 17, 2003; 278(4): 2750 - 2757.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
J. P. Annes, J. S. Munger, and D. B Rifkin
Making sense of latent TGF{beta} activation
J. Cell Sci., January 15, 2003; 116(2): 217 - 224.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
C. Penttinen, J. Saharinen, K. Weikkolainen, M. Hyytiainen, and J. Keski-Oja
Secretion of human latent TGF-{beta}-binding protein-3 (LTBP-3) is dependent on co-expression of TGF-{beta}
J. Cell Sci., January 9, 2002; 115(17): 3457 - 3468.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
K. Koli, J. Saharinen, M. Karkkainen, and J. Keski-Oja
Novel non-TGF-{beta}-binding splice variant of LTBP-4 in human cells and tissues provides means to decrease TGF-{beta} deposition
J. Cell Sci., January 8, 2001; 114(15): 2869 - 2878.
[Abstract] [Full Text] [PDF]




© The Company of Biologists Ltd 2001