China
Africa
Explore chapters and articles related to this topic
Interleukin-1
Published in Jason Kelley, Cytokines of the Lung, 2022
Timothy R. Aksamit, Gary W. Hunninghake
The human IL-1 receptor that is expressed on T cells and fibroblasts has also been cloned, and it has a striking structural similarity to the murine receptor (Sims et al., 1989). Both the murine and human proteins have a cytoplasmic domain, a transmembrane region, and an extracellular domain. The extracellular domain of this human T-cell type receptor consists of 319 amino acids, with five potential N-glycosylation sites and three immunoglobulinlike domains that are stabilized by three interchain disulfide bonds. These findings suggest that this portion of the molecule is a member of the immunoglobulin superfamily (Williams, 1987). The extracellular domain is responsible for binding IL-1, and it retains its ability to bind IL-1 after the transmembrane region and cytoplasmic domain have been removed (Dower et al., 1989). The transmembrane portion of the protein is, as expected, hydrophobic and consists of a 20-amino acid sequence. The cytoplasmic domain comprises 213 amino acids and exhibits no significant similarity to any other receptor kinases. Specifically, it has no similarity to the tyrosine kinase structure present in the platelet-derived growth factor (PDGF) and epidermal growth factor (EGF) receptors (Sims et al., 1988; Hunter, 1987). Signal transduction following IL-1 binding to the receptor requires the presence of the cytoplasmic domain; truncated portions of the IL-1 receptor without the cytoplasmic domain bind IL-1 normally, but do not mediate functional responses to IL-1 (Curtis et al., 1989).
Interleukin-6 Receptor
Published in Andrzej Mackiewicz, Irving Kushner, Heinz Baumann, Acute Phase Proteins, 2020
Stefan Rose-John, Peter C. Heinrich
IL-6 confers its signal to target cells by binding to IL-6-specific cell-surface receptors. A cDNA coding for an IL-6 receptor molecule has been cloned from the human natural killer-like cell line YT.15 The IL-6 receptor cDNA encodes a protein consisting of 468 amino acids, including a signal peptide of 19 amino acids. The 90-amino acid-long N-terminal part of the extracellular domain shows homology to the immunoglobulin superfamily. The cytoplasmic part of 82 amino acids lacks a tyrosine kinase domain, unlike other growth factor receptors. The deletion of the cytoplasmic and transmembrane domains of the 80-kDa subunit of the IL-6 receptor showed that neither was required for IL-6 signaling.16 This finding led to the discovery of the second subunit needed for the signal transduction of IL-6, a protein of a molecular weight of 130 kDa (gp130).16
Host Defense I: Non-specific Immunity
Published in Constantin A. Bona, Francisco A. Bonilla, Textbook of Immunology, 2019
Constantin A. Bona, Francisco A. Bonilla
Several adhesion molecules are members of the immunoglobulin superfamily (see Chapter 8). These include ICAM-1 (CD54), and ICAM-2 (CD102), the ligands of LFA-1 (CD11a/CD18), and LFA-2 (CD2) and LFA-3 (CD58). The expression of ICAM-1 on vascular endothelial cells is greatly increased by IL-1 or TNF. ICAM-1 is also the cellular receptor for rhinoviruses, the predominant cause of the common cold. CD2 and CD58 are mutual receptors/ligands and have important roles in T lymphocyte interactions (see Chapter 6). VCAM-1, the ligand for VLA-4 is also a member of the Ig superfamily. VCAM-1 is expressed by endothelial cells in germinal centers in response to IL-1 and TNF, and is important in lymphocyte homing. CD56 is its own ligand (it is homophilic). This molecule is expressed by NK cells and some T cells and may be important in NK cell cytotoxicity for CD56+ cells such as glioblastomas. CD31 is a homophilic adhesion molecule expressed on endothelial cells, platelets and a T cell subset.
Angelica sinensis polysaccharides alleviate the oxidative burden on hematopoietic cells by restoring 5-fluorouracil-induced oxidative damage in perivascular mesenchymal progenitor cells
Published in Pharmaceutical Biology, 2023
Yilin Niu, Hanxianzhi Xiao, Biyao Wang, Ziling Wang, Kunhang Du, Yaping Wang, Lu Wang
Cell-cell interactions between stromal cells and HSCs and cell-matrix interactions in the bone marrow are additional important factors in HSC maintenance. Integrins and selectins are essential mediators (Pillozzi and Becchetti 2012; Ding and Morrison 2013). Membrane-bound receptors of the immunoglobulin superfamily, including intercellular adhesion molecule-1 (ICAM-1; CD54), vascular cell adhesion molecule-1 (VCAM-1; CD105), and CD166, also constitute the bone marrow niche. ICAM-1/LFA-1 and VCAM-1/VLA-4 adhesion pairs are important for hematopoietic stem cell proliferation in mice (Chen et al. 2011). Overexpression or downregulation of these adhesion molecules affects HSC function. In the current study, we analyzed stromal and hematopoietic cell adhesion molecules. It was further demonstrated that 5-FU toxicity dramatically impaired adhesion between perivascular mesenchymal progenitors and hematopoietic cells. In summary, 5-FU caused oxidative damage to perivascular mesenchymal progenitors and destroyed diverse facets of perivascular hematopoietic niche function. We hypothesized that this might result in an ensuing stress response in the surrounding hematopoietic cells.
Fusobacterium nucleatum promotes colorectal cancer cells adhesion to endothelial cells and facilitates extravasation and metastasis by inducing ALPK1/NF-κB/ICAM1 axis
Published in Gut Microbes, 2022
Ying Zhang, Lu Zhang, Sheng Zheng, Mengjie Li, Chaochao Xu, Dingjiacheng Jia, Yadong Qi, Tongyao Hou, Lan Wang, Boya Wang, Aiqing Li, Shujie Chen, Jianmin Si, Wei Zhuo
During metastasis, cancer cells leave the original tumor organ and migrate to the target metastasis organs through a process that involves intravasation, adhesion and extravasation, among which the adhesion to endothelial cells and trans-endothelial invasion of tumor cells are key steps in the metastatic process.3,4 Indeed, changes in the expression or functions of cell adhesion molecules have been implicated in all steps of tumor progression. Cell adhesion molecules belonging to the immunoglobulin superfamily commonly play critical and necessary roles in metastasis,5–7 among which intercellular adhesion molecule 1 (ICAM1) is a well-known transmembrane glycoprotein involved in cell-cell direct interactions.7 The interaction between ICAM1 and its specific ligand could facilitate the adhesion of cancer cells to the vascular endothelium and subsequently in the promotion of metastasis. Importantly, the expression of ICAM1 was positively correlated with cancer progression and metastasis.8–10
Prognostic significance of CD56 expression in patients with multiple myeloma: a meta-analysis
Published in Hematology, 2022
Lijuan Zhang, Yun Huang, Yun Lin, Aili Zhang, Rong Zou, Huiying Xu, Sili Wang
CD56, a membrane glycoprotein belonging to the immunoglobulin superfamily, is also referred to as neural cell adhesion molecule (NCAM) [6,7]. It is first reported that the expression of CD56 was strongly positive in myeloma plasma cells in 1990 by Van Camp et al [8]. Subsequently, studies have reported that CD56 is expressed in 70–80% of MM patients [9]. It is widely accepted that CD56 is one of the important hallmarks of distinguishing benign and malignant diseases at present because it is hardly expressed on normal cells [10–12]. However, the expression of CD56 did not occur on all myeloma plasma cells, CD56 negative MM patients are also not uncommon. A large number of researches have focused on the clinical characteristics and prognostic factors of CD56 negative MM patients. Nevertheless, the results have not reached a consensus. In this study, a meta-analysis was performed for further comprehensive understanding of the prognostic significance of CD56 in MM.