The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The pro domain of pre-pro-transforming growth factor .beta.1 when independently expressed is a functional binding protein for the mature growth factor
Abstract
Transforming growth factor beta 1 (TGF-beta 1) is proteolytically derived from the carboxyl terminus of a 390 amino acid precursor molecule termed pre-pro-TGF-beta 1. Previous studies have suggested that the pro piece of pre-pro-TGF-beta 1 may play an important role in the formation of an inactive, latent complex. These latent forms are thought to be important in the regulation of TGF-beta 1 activity. To understand this latent complex in more detail, we have expressed the pro domain of pre-pro-TGF-beta 1 in tissue culture cells independent of the mature growth factor. A stop codon was genetically engineered into the cDNA of pre-pro-TGF-beta 1 by changing the Arg-278 codon from CGA to the STOP codon TGA. The resulting protein is truncated just prior to the amino-terminal Ala residue of the mature growth factor. Transient expression studies and immunoblotting indicate that this pro piece is readily made and secreted by the COS-1 cells; the major form of the expressed pro piece, when analyzed by SDS-polyacrylamide gel electrophoresis, behaves as a disulfide-linked dimer (Mr 80,000). Bioassays, using mink lung indicator cells, reveal that the pro domain forms an inactive complex with exogenously added mature TGF-beta 1. Treatment of this complex with heat or acid results in the release of active TGF-beta 1, indicating an in vitro structure similar to natural, latent TGF-beta 1 complexes. The pro piece from TGF-beta 1 was also found to form latent structures with two closely related family members, TGF-beta 1.2 and TGF-beta 2.(ABSTRACT TRUNCATED AT 250 WORDS)
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Cites
A rapid method for determining sequences in DNA by primed synthesis with DNA polymerase
Sanger, F., & Coulson, A. R. (1975) · Journal of Molecular Biology · doi:10.1016/0022-2836(75)90213-2 · Cited by 2,709
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Annes, J. P., Munger, J. S., & Rifkin, D. B. (2003) · Journal of Cell Science · doi:10.1242/jcs.00229 · Cited by 1,628
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Lee, S.-J., & McPherron, A. C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151270098 · Cited by 1,616
Latent TGF-β structure and activation
Shi, M., Zhu, J., Wang, R., Chen, X., Mi, L., Walz, T., & Springer, T. A. (2011) · Nature · doi:10.1038/nature10152 · Cited by 1,013
Induction of Cachexia in Mice by Systemically Administered Myostatin
Zimmers, T. A., Davies, M. V., Koniaris, L. G., Haynes, P., Esquela, A. F., Tomkinson, K. N., McPherron, A. C., Wolfman, N. M., & Lee, S.-J. (2002) · Science · doi:10.1126/science.1069525 · Cited by 907
Activation of latent TGF-β by thrombospondin-1: mechanisms and physiology
Murphy-Ullrich, J. E., & Poczatek, M. (2000) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(99)00029-5 · Cited by 586
Metadata
- Authors
- Gentry, L. E., & Nash, B. W.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1990-07-24
- Volume
- 29
- Issue
- 29
- Pages
- 6851-6857
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2020568173
- Cited by
- 184
- References
- 1
- FWCI
- 3.92
- Type
- journal article
- Language
- en
- Open access
- closed
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