Lafyatis, R. Transforming growth factor β–at the centre of systemic sclerosis. Nat. Rev. Rheumatol. 10, 706–719 (2014).
Pickup, M., Novitskiy, S. & Moses, H. L. The roles of TGFβ in the tumour microenvironment. Nat. Rev. Cancer 13, 788–799 (2013).
Occleston, N. L., Laverty, H. G., O’Kane, S. & Ferguson, M. W. J. Prevention and reduction of scarring in the skin by Transforming Growth Factor beta 3 (TGF beta 3): from laboratory discovery to clinical pharmaceutical. J. Biomater. Sci. Polym. Ed. 19, 1047–1063 (2008).
Moses, H. L., Roberts, A. B. & Derynck, R. The discovery and early days of TGF-beta: a historical perspective. Cold Spring Harb. Perspect. Biol. 8, a021865 (2016).
Grimaud, E., Heymann, D. & Redini, F. Recent advances in TGF-beta effects on chondrocyte metabolism. Potential therapeutic roles of TGF-beta in cartilage disorders. Cytokine Growth Factor Rev. 13, 241–257 (2002).
Moutos, F. T., Freed, L. E. & Guilak, F. A biomimetic three-dimensional woven composite scaffold for functional tissue engineering of cartilage. Nat. Mater. 6, 162–167 (2007).
Shoulders, M. D. & Raines, R. T. Collagen structure and stability. Annu. Rev. Biochem. 78, 929–958 (2009).
Kiani, C., Chen, L., Wu, Y. J., Yee, A. J. & Yang, B. B. Structure and function of aggrecan. Cell Res. 12, 19–32 (2002).
Cai, L. et al. Biomaterial stiffness guides cross-talk between chondrocytes: implications for a novel cellular response in cartilage tissue engineering. ACS Biomater. Sci. Eng. 6, 4476–4489 (2020).
Wei, J. et al. Osteoblasts induce glucose-derived ATP perturbations in chondrocytes through noncontact communication. Acta Biochim. Biophys. Sin. (Shanghai). 54, 625–636 (2022).
Hootman, J. M. & Helmick, C. G. Projections of US prevalence of arthritis and associated activity limitations. Arthritis Rheum. 54, 226–229 (2006).
Xie, J., Zhang, D., Lin, Y., Yuan, Q. & Zhou, X. Anterior cruciate ligament transection-induced cellular and extracellular events in menisci: implications for osteoarthritis. Am. J. Sports Med. 46, 1185–1198 (2018).
Yoo, K. H. et al. Transforming growth factor-beta family and stem cell-derived exosome therapeutic treatment in osteoarthritis (Review). Int. J. Mol. Med. 49, 62 (2022).
Wang, M. K. et al. Different roles of TGF-beta in the multi-lineage differentiation of stem cells. World J. Stem Cells 4, 28–34 (2012).
Wrana, J. L. & Attisano, L. The Smad pathway. Cytokine Growth Factor Rev. 11, 5–13 (2000).
Thielen, N. G. M., van der Kraan, P. M. & van Caam, A. P. M. TGFbeta/BMP signaling pathway in cartilage homeostasis. Cells 8, 969 (2019).
Jin, K. et al. TGF-β1-induced RAP2 regulates invasion in pancreatic cancer. Acta Biochim. Biophys. Sin. (Shanghai). 54, 361–369 (2022).
de Larco, J. E. & Todaro, G. J. Growth factors from murine sarcoma virus-transformed cells. Proc. Natl Acad. Sci. USA 75, 4001–4005 (1978).
Roberts, A. B., Anzano, M. A., Lamb, L. C., Smith, J. M. & Sporn, M. B. New class of transforming growth factors potentiated by epidermal growth factor: isolation from non-neoplastic tissues. Proc. Natl Acad. Sci. USA 78, 5339–5343 (1981).
Anzano, M. A. et al. Synergistic interaction of two classes of transforming growth factors from murine sarcoma cells. Cancer Res. 42, 4776–4778 (1982).
Herpin, A., Lelong, C. & Favrel, P. Transforming growth factor-beta-related proteins: an ancestral and widespread superfamily of cytokines in metazoans. Dev. Comp. Immunol. 28, 461–485 (2004).
Okamura, T., Yamamoto, K. & Fujio, K. Early growth response gene 2-expressing CD4(+)LAG3(+) regulatory T cells: the therapeutic potential for treating autoimmune diseases. Front. Immunol. 9, 340 (2018).
Annes, J. P., Munger, J. S. & Rifkin, D. B. Making sense of latent TGFbeta activation. J. Cell Sci. 116, 217–224 (2003).
Okamura, T. et al. Role of TGF-beta3 in the regulation of immune responses. Clin. Exp. Rheumatol. 33, S63–S69 (2015).
Chaudhry, S. S. et al. Fibrillin-1 regulates the bioavailability of TGFbeta1. J. Cell Biol. 176, 355–367 (2007).
Ge, G. & Greenspan, D. S. BMP1 controls TGFbeta1 activation via cleavage of latent TGFbeta-binding protein. J. Cell Biol. 175, 111–120 (2006).
Sengle, G., Ono, R. N., Sasaki, T. & Sakai, L. Y. Prodomains of transforming growth factor beta (TGFbeta) superfamily members specify different functions: extracellular matrix interactions and growth factor bioavailability. J. Biol. Chem. 286, 5087–5099 (2011).
Koli, K., Myllarniemi, M., Keski-Oja, J. & Kinnula, V. L. Transforming growth factor-beta activation in the lung: focus on fibrosis and reactive oxygen species. Antioxid. Redox Signal. 10, 333–342 (2008).
Shi, M. et al. Latent TGF-beta structure and activation. Nature 474, 343–349 (2011).
Annes, J. P., Chen, Y., Munger, J. S. & Rifkin, D. B. Integrin alphaVbeta6-mediated activation of latent TGF-beta requires the latent TGF-beta binding protein-1. J. Cell Biol. 165, 723–734 (2004).
Wipff, P. J. & Hinz, B. Integrins and the activation of latent transforming growth factor beta1 - an intimate relationship. Eur. J. Cell Biol. 87, 601–615 (2008).
Wang, J. et al. Atypical interactions of integrin alphaVbeta8 with pro-TGF-beta1. Proc. Natl. Acad. Sci. USA 114, E4168–E4174 (2017).
Annes, J. P., Rifkin, D. B. & Munger, J. S. The integrin alphaVbeta6 binds and activates latent TGFbeta3. FEBS Lett. 511, 65–68 (2002).
Cordeiro, M. F. Beyond Mitomycin: TGF-beta and wound healing. Prog. Retin. Eye Res. 21, 75–89 (2002).
Yoshinaga, K. et al. Perturbation of transforming growth factor (TGF)-beta1 association with latent TGF-beta binding protein yields inflammation and tumors. Proc. Natl. Acad. Sci. USA 105, 18758–18763 (2008).
Robertson, I. B. et al. Latent TGF-beta-binding proteins. Matrix Biol. 47, 44–53 (2015).
Saharinen, J. & Keski-Oja, J. Specific sequence motif of 8-Cys repeats of TGF-beta binding proteins, LTBPs, creates a hydrophobic interaction surface for binding of small latent TGF-beta. Mol. Biol. Cell 11, 2691–2704 (2000).
Rifkin, D. B., Rifkin, W. J. & Zilberberg, L. LTBPs in biology and medicine: LTBP diseases. Matrix Biol. 71-72, 90–99 (2018).
Zuo, W. et al. c-Cbl-mediated neddylation antagonizes ubiquitination and degradation of the TGF-beta type II receptor. Mol. Cell 49, 499–510 (2013).
Atfi, A. et al. The disintegrin and metalloproteinase ADAM12 contributes to TGF-beta signaling through interaction with the type II receptor. J. Cell Biol. 178, 201–208 (2007).
Kang, J. S., Liu, C. & Derynck, R. New regulatory mechanisms of TGF-beta receptor function. Trends Cell Biol. 19, 385–394 (2009).
Imamura, T., Oshima, Y. & Hikita, A. Regulation of TGF-beta family signalling by ubiquitination and deubiquitination. J. Biochem. 154, 481–489 (2013).
Hinck, A. P. Structural studies of the TGF-betas and their receptors - insights into evolution of the TGF-beta superfamily. FEBS Lett. 586, 1860–1870 (2012).
Goumans, M. J., Liu, Z. & ten Dijke, P. TGF-beta signaling in vascular biology and dysfunction. Cell Res. 19, 116–127 (2009).
Mitchell, E. J., Fitz-Gibbon, L. & O’Connor-McCourt, M. D. Subtypes of betaglycan and of type I and type II transforming growth factor-beta (TGF-beta) receptors with different affinities for TGF-beta 1 and TGF-beta 2 are exhibited by human placental trophoblast cells. J. Cell. Physiol. 150, 334–343 (1992).
Huang, T. et al. TGF-beta signalling is mediated by two autonomously functioning TbetaRI:TbetaRII pairs. EMBO J. 30, 1263–1276 (2011).
Tzavlaki, K. & Moustakas, A. TGF-beta signaling. Biomolecules 10, 487 (2020).
Derynck, R. & Zhang, Y. E. Smad-dependent and Smad-independent pathways in TGF-beta family signalling. Nature 425, 577–584 (2003).
Feng, X. H. & Derynck, R. Specificity and versatility in tgf-beta signaling through Smads. Annu. Rev. Cell Dev. Biol. 21, 659–693 (2005).
Gaarenstroom, T. & Hill, C. S. TGF-beta signaling to chromatin: how Smads regulate transcription during self-renewal and differentiation. Semin. Cell Dev. Biol. 32, 107–118 (2014).
Makkar, P., Metpally, R. P., Sangadala, S. & Reddy, B. V. Modeling and analysis of MH1 domain of Smads and their interaction with promoter DNA sequence motif. J. Mol. Graph. Model. 27, 803–812 (2009).
MacFarlane, E. G., Haupt, J., Dietz, H. C. & Shore, E. M. TGF-beta family signaling in connective tissue and skeletal diseases. Cold Spring Harb. Perspect. Biol. 9, a022269 (2017).
Derynck, R. & Budi, E. H. Specificity, versatility, and control of TGF-beta family signaling. Sci. Signal. 12, eaav5183 (2019).
Yano, M. et al. Smad7 inhibits differentiation and mineralization of mouse osteoblastic cells. Endocr. J. 59, 653–662 (2012).
留言 (0)