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Interleukin-1
Published in Jason Kelley, Cytokines of the Lung, 2022
Timothy R. Aksamit, Gary W. Hunninghake
The majority of IL-1–binding sites on the surface of fibroblasts are localized to attachment sites to extracellular matrix. The functional significance of this finding is unclear; however, the observation suggests that there may be complex interactions between IL-1 and extracellular matrix on various functions of fibroblasts (Qwarnstrom et al., 1988, 1989; Dayer et al., 1986a,b). Additional studies have demonstrated that IL-1 induces phosphorylation of talin and possibly mediates other alterations in the cytoskeleton of cells (Qwarmstrom et al., 1991).
Mechanotransduction Mechanisms of Hypertrophy and Performance with Resistance Exercise
Published in Peter M. Tiidus, Rebecca E. K. MacPherson, Paul J. LeBlanc, Andrea R. Josse, The Routledge Handbook on Biochemistry of Exercise, 2020
Andrew C. Fry, Justin X. Nicoll, Luke A. Olsen
The family of integrin proteins, 24 in all, are heterodimeric consisting of 18 α and 8 β subunits (13). As transmembrane proteins, the integrin physically connects the extracellular matrix to the intracellular space. Within the cell, the integrin indirectly connects to the actin cytoskeleton through scaffolding proteins positioned at the integrin's cytoplasmic tail such as talin, kindlin, and paxillin. Thus, through its transmembrane nature, the integrin allows communication in a bidirectional manner—both in an inside-out and outside-in fashion (96). Interestingly, research has shed light upon the extended physical continuity from the cytoskeleton into the nucleus, made possible by the linker of the nucleoskeleton and cytoskeleton (LINC) complex (109). This continuous physical link from the extracellular space, through the integrin to the cytoskeleton, and into the nucleus via the LINC complex, directly influences gene expression in a matter of seconds upon mechanical activity, such as muscle tension produced with exercise.
Overview of Cell Adhesion Molecules and Their Antagonism
Published in Bruce S. Bochner, Adhesion Molecules in Allergic Disease, 2020
Although their intracytoplasmic segments are relatively short, integrins interact with extracellular cytoskeletal components, such as actin and talin. The name integrins derives from the concept that these molecules “integrate” information from the extracellular milieu to intracellular compartments. Recently, it has been established that integrins are capable of bidirectional signaling, as they also transduce signals “inside out” (15). Thus, many integrins constitutively have minimal ability to bind their ligands. Upon activation of the cell, integrins undergo conformational changes that permit binding of divalent cations by the α-subunit and markedly increase their avidity for ligand. The presence of conformationally dissimilar forms has been confirmed by the description of monoclonal antibodies (mAb) specific for individual integrins at distinct states of activation.
Suspended cell lines for inactivated virus vaccine production
Published in Expert Review of Vaccines, 2023
Jiayou Zhang, Zhenyu Qiu, Siya Wang, Zhenbin Liu, Ziling Qiao, Jiamin Wang, Kai Duan, Xuanxuan Nian, Zhongren Ma, Xiaoming Yang
Talin is the most characteristic binding protein linking integrins to actin and is a major component of focal adhesions (FAs). Talin has two subtypes, namely talin-1 and talin-2. Talin-1 gene knockout cell lines were established in fibroblasts, and it was found that they could not activate their integrins nor bind to the fibrin in ECM, thus leading to a significant decline in cell adhesion [96]. Other studies have confirmed the role of talin-1 in carcinogenesis and provided a new therapeutic target for the treatment of hepatocellular carcinoma (HCC). Furthermore, talin-1 may promote cell adhesion by regulating the epithelial-mesenchymal transition (EMT) process [97]. Studies have also shown that T cells and T cell exocrines lacking talin-2 show reduced binding with integrin ligands ICAM-1 and MAdCAM-1 [113], demonstrating that knockdown of the talin-2 gene can reduce cell adhesion. Kindlins, which contain three members (Kindlin-1, Kindlin-2, and Kindlin-3), are key cell-ECM adhesion proteins and key activators of integrins. Kindlin-2, also known as mig-2, can directly bind to the β1- and β3-integrin tail [98]. Studies have shown that knockdown of the Kindlin-2 gene can prevent the activation of integrins, thus significantly affecting the adhesion ability of cells [99]. Additionally, deficiencies in Kindlin-1 and Kindlin-3 can lead to diseases. For example, Kindlin-1 deficiency causes skin weakness and blistering (called Kindler syndrome), and Kindlin-3 deficiency causes hemorrhagic disease and immune deficiency.
Recent advances in molecular biomarkers for patients with hepatocellular carcinoma
Published in Expert Review of Molecular Diagnostics, 2019
Shinichi Umeda, Mitsuro Kanda, Yasuhiro Kodera
Talin 1 (TLN1) is an adaptor protein that conjugates integrins to the cytoskeleton and regulates integrin and focal adhesion signaling [58]. Chen et al. determined TLN1 levels in 200 HCC patients and downregulation of TLN1 were significantly correlated with younger age, larger tumor size, higher α-fetoprotein levels and poor prognosis [48]. They also found that TLN1 knockdown induced EMT by regulating E-cadherin, N-cadherin, vimentin, and β-catenin. Silencing TLN1 promoted the growth of lamellipodia and enhanced cell migration and invasion [48]. Western blot analysis of EMT-associated cancer pathway proteins revealed that phosphorylated ERK1/2 was significantly elevated in TLN1 knockdown cells [48]. They concluded that TLN1 acts as a tumor suppressor to inhibit EMT, migration, and invasion of HCC cells by decreasing activation of the ERK1/2 pathway and that TLN1 is a potential prognostic biomarker for HCC patients.
Extracellular Matrix Remodeling During Palate Development
Published in Organogenesis, 2020
Xia Wang, Chunman Li, Zeyao Zhu, Li Yuan, Wood Yee Chan, Ou Sha
Talin (Tln) is one of the important intracellular proteins which activates integrins by binding to its β subunit.93,94 Two Tln isoforms are present in most vertebrates95 and three in zebrafish.96 In zebrafish, tln1 is required for the cranial neural crest cell proliferation during palate morphogenesis.97 In mice, global loss of Tln1 leads to embryonic lethality during gastrulation98, while Tln2 null mice are viable and fertile.99 Conditional mouse models would provide more evidence on how Talin engages in Integrin signal transduction during palate development.