Identification and characterization of an eight-cysteine repeat of the latent transforming growth factor-β binding protein-1 that mediates bonding to the latent transforming growth factor-β1

Gleizes, Pierre-Emmanuel, Beavis, Ronald C., Mazzieri, Roberta, Shen, Bin and Rifkin, Daniel B. (1996) Identification and characterization of an eight-cysteine repeat of the latent transforming growth factor-β binding protein-1 that mediates bonding to the latent transforming growth factor-β1. Journal of Biological Chemistry, 271 47: 29891-29896. doi:10.1074/jbc.271.47.29891

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Author Gleizes, Pierre-Emmanuel
Beavis, Ronald C.
Mazzieri, Roberta
Shen, Bin
Rifkin, Daniel B.
Title Identification and characterization of an eight-cysteine repeat of the latent transforming growth factor-β binding protein-1 that mediates bonding to the latent transforming growth factor-β1
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 1996-11-01
Year available 1996
Sub-type Article (original research)
DOI 10.1074/jbc.271.47.29891
Open Access Status File (Publisher version)
Volume 271
Issue 47
Start page 29891
End page 29896
Total pages 6
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Formatted abstract
Most cultured cell types secrete small latent transforming growth factor-β (TGF-β) as a disulfide-bonded complex with a member of the latent TGF-β binding protein (LTBP) family. Using the baculovirus expression system, we have mapped the domain of LTBP-1 mediating covalent association with small latent TGF-β1. Coexpression in Sf9 cells of small latent TGF-β1 with deletion mutants of LTBP-1 showed that the third eight-cysteine repeat of LTBP-1 is necessary and sufficient for covalent interaction with small latent TGF-β1. Analysis by mass spectrometry of this eight-cysteine repeat, produced as a recombinant peptide in Sf9 cells, confirmed that it was N-glycosylated, as expected from the primary sequence. No other post-translational modifications of this domain were detected. Alkylation of the recombinant peptide with vinyl pyridine failed to reveal any free cysteines, indicating that, in the absence of small latent TGF-β, the eight cysteines of this domain are engaged in intramolecular bonds. These data demonstrate that the third LTBP-1 eight-cysteine repeat recognizes and associates covalently with small latent TGF-β1 through a mechanism that does not require any specific post-translational modification of this domain. They also suggest that this domain adopts different conformations depending on whether it is free or bound to small latent TGF-β.
Keyword Biochemistry & Molecular Biology
Biochemistry & Molecular Biology
BIOCHEMISTRY & MOLECULAR BIOLOGY
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID CA 23753
Institutional Status Non-UQ

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