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Mechanical Signaling in the Urinary Bladder
Published in Jiro Nagatomi, Eno Essien Ebong, Mechanobiology Handbook, 2018
Aruna Ramachandran, Ramaswamy Krishnan, Rosalyn M. Adam
Studies in our laboratory and others using primary BSMC subjected to mechanical stretch using the FlexCell system have revealed stretch-induced signaling via multiple parallel kinase cascades, activation of select genes [53,54], and induction of a hyperplastic and hypertrophic response [51,52,55–57]. In particular, cyclic stretch relaxation of BSMC has been shown to activate the receptor tyrosine kinases (RTKs) epidermal growth factor receptor (EGFR)/ErbB1 [58] and ErbB2 [52], the mitogen-activated protein kinase Erk [59,60], the stress-activated kinases JNK/SAPK [52,61] and p38SAPK2 [52] and the phosphoinositide-3-kinase (PI3K)/Akt survival pathway [56]. In spite of the activation of several discrete signaling pathways following mechanical stimulation, the transcriptional response of stretched SMC has been shown to be highly selective. In a recent study from our laboratory, genome-scale analysis of gene expression in primary human BSMC exposed to cyclic stretch relaxation in vitro revealed less than 0.2% of the expressed genome in these cells to be mechanically responsive [53]. The gene found to be upregulated to the greatest extent in this study was that encoding heparin-binding EGF-like growth factor (HB-EGF), a member of the EGF-like growth factor family and activating ligand for the EGFR/ErbB1 and the related receptor ErbB4 [62,63]. Interestingly, a previous study from our program had provided the first demonstration that HB-EGF, a known SMC mitogen [62], was a stretch-sensitive gene in BSMC [51].
Terpenoids: The Biological Key Molecules
Published in Dijendra Nath Roy, Terpenoids Against Human Diseases, 2019
Moumita Majumdar, Dijendra Nath Roy
The ErbB, or HER, pathway is regulated by terpenoids in an interactive manner. ErbB proteins are, in nature, tyrosine kinases comprising four receptors structurally analogous to epidermal growth factor receptor (EGFR). In the human body, these include Her1 (EGFR, ErbB1), Her2 (Neu, ErbB2), Her3 (ErbB3) and Her4 (ErbB4). With the overexpression of genes, this pathway causes uncontrolled cell proliferation, leading to cancer development (Cho and Leahy 2002). After conformational changes, phosphorylated tyrosine residues of the receptor proteins act as binding sites for the RAS-rapidly accelerated fibrosarcoma-MAPK (RAS-Raf-MAPK) pathway, which inhibits apoptosis (Herbst 2004).
Small-Molecule Inhibitors Targeting Receptor Tyrosine Kinases in Cancer
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2020
Mohammad Hojjat-Farsangi, Gholamreza Khamisipour
EGFR or ErbB family have four members with similar structure, including EGFR (ErbB1), HER2/neu (ErbB2), HER3 (ErbB3), and HER4 (ErbB4). Members of this family are important for the regulation of normal cell proliferation, differentiation, and survival. In normal situations, EGFR ligand (EGF) binds to the extracellular part of EGFR and induce EGFR homo/heterodimerization with other members of this family and leads to phosphorylation at specific tyrosine amino acids within the kinase domain (Ono and Kuwano, 2006).
A new Ho(III) dinuclear complex: treatment activity and cure values on mania by reducing the expression of the ErbB4 on the noradrenergic neurons
Published in Inorganic and Nano-Metal Chemistry, 2021
Yong-Hua Chen, Yan Xu, Hao Wu, Xiao-Yi Li, Ming-Jun Zhang
ErbB4 is a ubiquitously expressed member of the ErbB family of receptor tyrosine kinases that is essential for normal development of the mammary gland, nervous system, and heart. To explain the experimental results that the Ho metal complex may exhibit activities to the ErbB4 kinase, the molecular docking has been performed for the Ho metal complex in contacting with 3BCE receptor.