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Distinct transforming growth factor-beta (TGF-beta) receptor subsets as determinants of cellular responsiveness to three TGF-beta isoforms
Open accessAbstract
Characterization of the three mammalian transforming growth factor-beta (TGF-beta) isoforms, TGF-beta 1, -beta 2, and -beta 3, indicates that TGF-beta 3 is somewhat more potent (ED50 = 0.5 pM versus 2 pM) than TGF-beta 1 and TGF-beta 2 as a growth inhibitor of the Mv1Lu mink lung epithelial cell line. In the fetal bovine heart endothelial (FBHE) cell line, however, TGF-beta 1 and -beta 3 are at least 50-fold more potent than TGF-beta 2 which is a very weak growth inhibitor (ED50 greater than or equal to 0.5 nM). Thus, as growth inhibitors, TGF-beta 1 and -beta 3 resemble each other more than TGF-beta 2. The presence of serum alpha 2-macroglobulin in the FBHE cell assays decreases the biological potency of TGF-beta s, in particular TGF-beta 2. This effect of alpha 2-macroglobulin, however, is not sufficient to explain the low responsiveness of FBHE cells to TGF-beta 2. Evaluation of the role of TGF-beta receptors as determinants of cell-specific responsiveness to TGF-beta isoforms indicates that TGF-beta 1, -beta 2, and -beta 3 have similar affinity for the membrane proteoglycan, betaglycan. They differ, however, in their ability to bind to receptor types I and II which are implicated in TGF-beta signal transduction. TGF-beta 1 is similar, albeit not identical, to TGF-beta 3 and much more potent than TGF-beta 2 as a competitor for binding to the overall population of receptors I and II in all cell lines tested. A subset of receptors I and II has been identified in Mv1Lu cells which has high affinity for TGF-beta 2 (KD approximately 10 pM) and binds this factor at concentrations that are biologically active in Mv1Lu cells. This receptor subset could not be detected in FBHE cells, suggesting that cell-specific differences in the level of high affinity of TGF-beta 2 receptors may lead to cell-specific differences in responsiveness to this isoform. Thus, despite their structural and biological similarities, TGF-beta 1, -beta 2, and -beta 3 diverge in their ability to bind to receptors in a manner that correlates with their potency as growth inhibitors.
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Andres, J. L., Stanley, K., Cheifetz, S., & Massagué, J. (1989) · The Journal of cell biology · doi:10.1083/jcb.109.6.3137 · Cited by 354
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Cheifetz, S., Bellón, T., Calés, C., Vera, S., Bernabeu, C., Massagué, J., & Letarte, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41732-2 · Cited by 836
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Self-citationLiu, F., Ventura, F., Doody, J., & Massagué, J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3479 · Cited by 593
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Metadata
- Authors
- Cheifetz, S., Hernandez, H., Laiho, M., ten Dijke, P., Iwata, K. K., & Massagué, J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1990-11
- Volume
- 265
- Issue
- 33
- Pages
- 20533-20538
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2246378037
- Cited by
- 348
- References
- 1
- FWCI
- 6.75
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Cheifetz, S., Hernandez, H., Laiho, M., ten Dijke, P., Iwata, K. K., & Massagué, J. (1990). Distinct transforming growth factor-beta (TGF-beta) receptor subsets as determinants of cellular responsiveness to three TGF-beta isoforms. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)30535-5
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
