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      Peptidase inhibitors in tick physiology : Peptidase inhibitors in tick physiology

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          Most cited references146

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          RGD and other recognition sequences for integrins.

          Proteins that contain the Arg-Gly-Asp (RGD) attachment site, together with the integrins that serve as receptors for them, constitute a major recognition system for cell adhesion. The RGD sequence is the cell attachment site of a large number of adhesive extracellular matrix, blood, and cell surface proteins, and nearly half of the over 20 known integrins recognize this sequence in their adhesion protein ligands. Some other integrins bind to related sequences in their ligands. The integrin-binding activity of adhesion proteins can be reproduced by short synthetic peptides containing the RGD sequence. Such peptides promote cell adhesion when insolubilized onto a surface, and inhibit it when presented to cells in solution. Reagents that bind selectively to only one or a few of the RGD-directed integrins can be designed by cyclizing peptides with selected sequences around the RGD and by synthesizing RGD mimics. As the integrin-mediated cell attachment influences and regulates cell migration, growth, differentiation, and apoptosis, the RGD peptides and mimics can be used to probe integrin functions in various biological systems. Drug design based on the RGD structure may provide new treatments for diseases such as thrombosis, osteoporosis, and cancer.
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            The cystatins: protein inhibitors of cysteine proteinases.

            The last decade has witnessed enormous progress of protein inhibitors of cysteine proteinases concerning their structures, functions and evolutionary relationships. Although they differ in their molecular properties and biological distribution, they are structurally related proteins. All three inhibitory families, the stefins, the cystatins and the kininogens, are members of the same superfamily. Recently determined crystal structures of chicken cystatin and human stefin B established a new mechanism of interaction between cysteine proteinases and their inhibitors which is fundamentally different from the standard mechanism for serine proteinases and their inhibitors.
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              α-2-Macroglobulin: a physiological guardian.

              Alpha macroglobulins are large glycoproteins which are present in the body fluids of both invertebrates and vertebrates. Alpha-2-macroglobulin (α2 M), a key member of alpha macroglobulin superfamily, is a high-molecular weight homotetrameric glycoprotein. α2 M has many diversified and complex functions, but it is primarily known by its ability to inhibit a broad spectrum of proteases without the direct blockage of the protease active site. α2 M is also known to be involved in the regulation, transport, and a host of other functions. For example, apart from inhibiting proteinases, it regulates binding of transferrin to its surface receptor, binds defensin and myelin basic protein, etc., binds several important cytokines, including basic fibroblast growth factor (bFGF), platelet-derived growth factor (PDGF), nerve growth factor (NGF), interleukin-1β (IL-1β), and interleukin-6 (IL-6), and modify their biological activity. α2 M also binds a number of hormones and regulates their activity. α2 M is said to protect the body against various infections, and hence, can be used as a biomarker for the diagnosis and prognosis of a number of diseases. However, this multipurpose antiproteinse is not "fail safe" and could be damaged by reactive species generated endogenously or exogenously, leading to various pathophysiological conditions. Copyright © 2012 Wiley Periodicals, Inc.
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                Author and article information

                Journal
                Medical and Veterinary Entomology
                Med Vet Entomol
                Wiley
                0269283X
                June 2018
                June 2018
                November 07 2017
                : 32
                : 2
                : 129-144
                Affiliations
                [1 ]Centro de Biotecnologia; Universidade Federal do Rio Grande do Sul; Porto Alegre RS Brazil
                [2 ]Faculdade de Veterinária; Universidade Federal do Rio Grande do Sul; Porto Alegre RS Brazil
                [3 ]Department of Zoology; Abdul Wali Khan University; Mardan Pakistan
                [4 ]Escola de Enfermagem de Ribeirão Preto; Universidade de São Paulo, Ribeirão Preto; SP Brazil
                [5 ]Departamento de Farmacociências; Universidade Federal de Ciências da Saúde de Porto Alegre; RS Brazil
                [6 ]Instituto Nacional de Ciência e Tecnologia em Entomologia Molecular; Rio de Janeiro, RJ Brazil
                [7 ]Laboratório de Química e Função de Proteínas e Peptídeos-CBB and Unidade de Experimentação Animal; Universidade Estadual do Norte Fluminense Darcy Ribeiro; Campos dos Goytacazes RJ Brazil
                [8 ]Departamento de Bioquímica; Universidade Federal do Rio Grande do Sul, Porto Alegre; Porto Alegre Brazil
                Article
                10.1111/mve.12276
                a4caa9fa-934c-4425-bd2c-f32e0a88e44f
                © 2017

                http://doi.wiley.com/10.1002/tdm_license_1.1

                http://onlinelibrary.wiley.com/termsAndConditions#vor

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