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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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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
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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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- CoChat. (2026). Citation check: The pro domain of pre-pro-transforming growth factor .beta.1 when independently expressed is a functional binding protein for the mature growth factor. https://app.cochat.ai/papers/10.1021/bi00481a014
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- Gentry, L. E., & Nash, B. W. (1990). The pro domain of pre-pro-transforming growth factor .beta.1 when independently expressed is a functional binding protein for the mature growth factor. Biochemistry. https://doi.org/10.1021/bi00481a014
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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