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1

Beta 3-Integrin cytoplasmic binding proteins

100%
Zhao R., Pathak A. S., Stouffer G. A.
Archivum Immunologiae et Therapiae Experimentalis
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2004
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vol. 52
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issue 5
348-355
EN
Integrins are cell-surface adhesion receptors that play an important role in mediating numerous physiological processes, including inflammation, migration, adhesion, and proliferation. Integrin regulation by events within the cell has been termed 'inside-out' signaling; this is a capacity that is unique to integrin receptors. As is typical of other cell-surface receptors, integrins can also transduce signals from outside the cell into the cytoplasm on binding extracellular ligands ('outside-in signaling'). Integrins are composed of an alpha and a beta subunit, which form a heterodimer. The beta 3-integrin family consists of alphaIIbbeta3 found on platelets and megakaryocytes, and the more widely distributed alpha beta3. beta subunits consist of a large extracellular domain, a single transmembrane segment, and a relatively short cytoplasmic tail. The cytoplasmic domains do not contain intrinsic tyrosine kinase activity, and therefore signaling occurs primarily via recruitment of intracellular signaling molecules. Integrins form transmembrane connections, and the interactions between integrin cytoplasmic domains, intracellular factors (cytoplasmic proteins and intracellular signaling pathways), and membrane-anchored proteins play an important role in integrin- mediated events. There are at least 21 proteins that associate with integrin beta tails to regulate cell motility, proliferation, differentiation, and apoptosis. In this review, we will focus on 10 of these proteins and their function in integrin-mediated events.
2

T cell integrin activation by chemokines in inflammation

88%
Tanaka Y.
Archivum Immunologiae et Therapiae Experimentalis
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2000
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vol. 48
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issue 5
443-450
EN
The adhesive function of integrins is regulated through cytoplasmic signaling induced by several stimuli, whose process is designated ?inside-out signaling?. A large number of lymphocytes are recruited to the sites of inflammation where they form an essential component of the response to infection, injury, autoimmune disorders, allergy, tumor invasion, atherosclerosis and so on. The recruitment of leukocytes into tissue is regulated by a sequences of interactions between the circulating leukocytes and the endothelial cells. Leukocyte integrins play a pivotal role in leukocyte adhesion to endothelial cells. During the process, the activation of integrins by chemokines, is essential for integrin-mediated adhesion in which a signal transduced to the leukocyte converts the functionally inactive integrin to an active adhesive configuration. The present review documents the relevance of cytoplasmic signaling and cytoskeletal assembly to integrin-mediated adhesion induced by chemokines during inflammatory processes.
3

Anti-tumor chemotherapy utilizing peptide-based approaches ? apoptotic pathways, kinases, and proteasome as targets

88%
Mendoza F. J., Espino P. S., Cann K. L., Bristow N., Mc_Crea K., Los M.
Archivum Immunologiae et Therapiae Experimentalis
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2005
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vol. 53
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issue 1
47-60
EN
The pharmacological sciences are taking advantage of recent discoveries that have defined the molecular pathways governing apoptosis. These signaling cascades are frequently inactivated or distorted by mutations in cancer cells. Peptides derived from critical interaction, phosphorylation, or cleavage sites are the preferred leads (starting points) for the development of new drugs. In this review we summarize recent peptide-based approaches that target MDM2, p53, NF-?B, ErbB2, MAPK, as well as Smac/DIABLO, IAP BIR domains, and Bcl-2 interaction domains, with a specific focus on the BH3 domain. Separate parts of the review deal with proteasome inhibitors, integrin-derived peptides, and molecules that are being tested for tumor-selective delivery of anticancer drugs ('magic bullet' approach). The proteasome inhibitors and integrin-derived peptides show a variety of effects, targeting not only tumor growth, but also angiogenesis, metastasizing potential, and other cancer cell functions. The last part of this review describes approaches that use specific properties (surface receptors, increased enzymatic activities) of cancer cells in order to target them specifically. These new generations of anticancer drugs provide the foundations for therapies with fewer side effects and higher efficacy.
4

Trafficking of FoxP3+ regulatory T cells: myths and facts

75%
Kim C. H.
Archivum Immunologiae et Therapiae Experimentalis
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2007
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vol. 55
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issue 3
151-159
EN
Fork head box P3 (FoxP3+) regulatory T cells (Tregs) are specialized T cells for the prevention of hyperimmune responses and autoimmunity. Tumors and pathogens can hijack FoxP3+ Tregs to evade host immune responses. There is an increasing body of evidence that trafficking of FoxP3+ Tregs is important for their effective suppression of target cells. Because of their distinctive functions and gene expression phenotype, the migratory behavior of FoxP3+ Tregs has been somewhat mystified. The myths are that they have unique trafficking receptors and migratory behaviors that are different from those of conventional T cells. Another related myth is that FoxP3+ regulatory T cell subsets have a fixed trafficking behavior from the time they are generated in the thymus. Recent progress in trafficking receptors and the migratory behavior of FoxP3+ Tregs are reviewed here and the validity of these myths examined.
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