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Articular Cartilage Development
Published in Kyriacos A. Athanasiou, Eric M. Darling, Grayson D. DuRaine, Jerry C. Hu, A. Hari Reddi, Articular Cartilage, 2017
Kyriacos A. Athanasiou, Eric M. Darling, Grayson D. DuRaine, Jerry C. Hu, A. Hari Reddi
TGF-β and BMP signaling is based on the interactions of four different kinds of molecules. Signaling pathways in the TGF-β superfamily are composed of different, albeit similar, components for both the BMP and TGF-β ligand groups (Table 2.4), such as cell surface receptors (and secondary binding receptors such as decorin) and internal signaling molecules called Smad, which were originally identified as homologs of Mad in Drosophila and Sma in Caenorhabditis elegans (Sekelsky et al. 1995; Savage et al. 1996). Once activated, these ligands bind to type II transmembrane receptors, which then recruit and phosphorylate type I receptors, both of which exist as homodimers. The serine/threonine kinase activity of the type I receptor is then able to phosphorylate the carboxy-terminus of the receptor-activated Smads (R-Smad). For BMPs and GDFs, two type I receptors (BMPRIA and BMPRIB), which exist as heterodimers, complex with the type II receptor (BMPRII), which exists as a homodimer. These recruit and phosphorylate Smad1, 5, and 8, which interact with the common Smad (Smad4) with both TGF-β and BMP pathways (Figure 2.18). For TGF-β, the key players are the TGFRI and TGFRII receptors, which interact with Smad2 or 3 and then Smad4 (Derynck and Zhang 2003; Shi and Massague 2003; Miyazono et al. 2005). Recent evidence also indicates that cartilage oligomeric matrix protein (COMP) plays a role in binding to and presenting TGF-β to these receptors, resulting in enhanced signaling (Haudenschild et al. 2011).
Core genes in lung adenocarcinoma identified by integrated bioinformatic analysis
Published in International Journal of Environmental Health Research, 2023
Liu Yang, Qi Yu, Yonghang Zhu, Manthar Ali Mallah, Wei Wang, Feifei Feng, Qiao Zhang
The PI3K-AKT pathway is one of the key signaling pathways involved in proliferation, migration and invasion of lung cancer cells (Jiang et al. 2020). It has been noted that aberrant activation of PI3K-AKT pathway is related to cancer tumorigenesis and progression (Mayer and Arteaga 2016). We found that six genes (ANGPT1, TEK, COL1A1, SPP1, THBS2 and VWF) involved in PI3K-AKT pathway (Figure 8). COL1A1, SPP1, THBS2 and VWF in extracellular matrix (ECM) activate focal adhesion kinase (FAK) by binding to integrin (ITGA and ITGB), which activates the PI3K/AKT signaling in turn. As a growth factor, ANGPT1 activates the PI3K/AKT and MEK/ERK signaling pathways by combining with TEK receptor tyrosine kinase. Club cell secretory protein (CC16) is encoded by the SCGB1A1 gene (Almuntashiri et al. 2020). Studies have showed that SPARCL1 (Ma et al. 2018) and CC16 (Zhou et al. 2019) can inhibit the transduction of mitogen‑activated protein kinase kinase (MEK)/extracellular signal‑related kinase (ERK) signaling. Previous studies demonstrated that hepatic stellate cells (HSCs)-derived cartilage oligomeric matrix protein (COMP) collaborated with CD36 and subsequently activate MEK/ERK and PI3K/AKT signaling pathways (Li et al. 2018). Stromal cell-derived factor 1 (SDF-1) could induce PECAM-1 through Src family tyrosine kinases to enhance the chemotactic signaling pathway involving PI3K/AKT/mTORC1 (Umezawa et al. 2017). Core genes could affect cell survival, migration, proliferation and metabolism by activating or inhibiting the PI3K-AKT signaling pathway. Taken together, we speculated that core genes may modulate LUAD through PI3K-AKT pathway.