Academic literature on the topic 'RGDS'

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Journal articles on the topic "RGDS"

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Shebuski, R. J., D. E. Berry, D. B. Bennett, et al. "Demonstration of Ac-Arg-Gly-Asp-Ser-NH2 as an Antiaggregatory Agent in the Dog by Intracoronary Administration." Thrombosis and Haemostasis 61, no. 02 (1989): 183–88. http://dx.doi.org/10.1055/s-0038-1646556.

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SummaryThis study compared the anti-platelet effect of Ac-RGDS-NH2 which is a peptide fragment from fibrinogen to Ac-RGES-NH2 in which the aspartic acid (D) of Ac-RGDS-NH2 has been replaced by glutamic acid (E). When Ac-RGDS-NH2 was infused intracoronary at concentrations of 100–400 mM, acute platelet dependent thrombus formation in the dog coronary artery was inhibited. However, infusion of Ac-RGES-NH2 intracoronary at similar concentrations to Ac-RGDS-NH2 failed to inhibit platelet dependent thrombus formation in the dog. Ac-RGDS-NH2 and Ac-RGES-NH2 were also tested for their ability to inhibit collagen-induced platelet aggregation in vitro. Ac-RGDS-NH2 elicited concentration-dependent inhibition of collagen-induced aggregation with no effect of Ac-RGES-NHz otr collagen-induced platelet aggregation. Thus, Ac-RGDS-NH2 is an effective antiplatelet agent after intracoronary administration in the dog and also inhibits collagen-induced platelet aggregation in vitro. Ac-RGDS-NH2 is a specific inhibitor of platelet aggregation as replacement of the aspartic acid in Ac-RGDS-NH2 with glutamic acid results in complete loss of biological activity.
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Plow, EF, MD Pierschbacher, E. Ruoslahti, G. Marguerie, and MH Ginsberg. "Arginyl-glycyl-aspartic acid sequences and fibrinogen binding to platelets." Blood 70, no. 1 (1987): 110–15. http://dx.doi.org/10.1182/blood.v70.1.110.110.

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Abstract Human fibrinogen has an Arg-Gly-Asp-Ser (RGDS) sequence at residues 572- 575 of its A alpha-chain. Although RGDS-containing peptides inhibit fibrinogen binding to stimulated platelets, these peptides also inhibit platelet binding of human fibrinogen fragment X and rat fibrinogen, which lack RGDS sequences corresponding to A alpha 572–575. Thus competition between free RGD-containing peptides and internal RGDS sequence at A alpha 572–575 is not the basis for their inhibition of fibrinogen binding to platelets. Addition of a Thr to the carboxy- terminus and an Asn to the amino-terminus of the RGDS sequence, the amino acids corresponding to A alpha 576 and 571 respectively, reduced the inhibitory potency of RGDS-containing peptides by fourfold to tenfold. Arg-Gly-Asp-Phe (RGDF) corresponds to A alpha 95–98, and the RGDF peptide was an effective inhibitor of fibrinogen binding, fourfold to fivefold more potent than RGDS. Thus, local primary structure may play an important role in regulating the capacity of RGD sequences in proteins to interact with specific adhesion receptors.
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Plow, EF, MD Pierschbacher, E. Ruoslahti, G. Marguerie, and MH Ginsberg. "Arginyl-glycyl-aspartic acid sequences and fibrinogen binding to platelets." Blood 70, no. 1 (1987): 110–15. http://dx.doi.org/10.1182/blood.v70.1.110.bloodjournal701110.

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Human fibrinogen has an Arg-Gly-Asp-Ser (RGDS) sequence at residues 572- 575 of its A alpha-chain. Although RGDS-containing peptides inhibit fibrinogen binding to stimulated platelets, these peptides also inhibit platelet binding of human fibrinogen fragment X and rat fibrinogen, which lack RGDS sequences corresponding to A alpha 572–575. Thus competition between free RGD-containing peptides and internal RGDS sequence at A alpha 572–575 is not the basis for their inhibition of fibrinogen binding to platelets. Addition of a Thr to the carboxy- terminus and an Asn to the amino-terminus of the RGDS sequence, the amino acids corresponding to A alpha 576 and 571 respectively, reduced the inhibitory potency of RGDS-containing peptides by fourfold to tenfold. Arg-Gly-Asp-Phe (RGDF) corresponds to A alpha 95–98, and the RGDF peptide was an effective inhibitor of fibrinogen binding, fourfold to fivefold more potent than RGDS. Thus, local primary structure may play an important role in regulating the capacity of RGD sequences in proteins to interact with specific adhesion receptors.
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Hirano, Yoshiaki, Yoshihiro Kando, Toshio Hayashi, Kunio Goto, and Akio Nakajima. "Synthesis and cell attachment activity of bioactive oligopeptides: RGD, RGDS, RGDV, and RGDT." Journal of Biomedical Materials Research 25, no. 12 (1991): 1523–34. http://dx.doi.org/10.1002/jbm.820251209.

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Donaldson, D. J., J. T. Mahan, and G. N. Smith. "Newt epidermal cell migration over collagen and fibronectin involves different mechanisms." Journal of Cell Science 90, no. 2 (1988): 325–33. http://dx.doi.org/10.1242/jcs.90.2.325.

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Effects of the synthetic peptides, Arg-Gly-Asp-Ser (RGDS), the amino acid sequence representing the fibroblast attachment site in fibronectin, and Arg-Gly-Glu-Ser (RGES), on collagen- and fibronectin-mediated migration in newt epidermal cells were compared. When RGDS at 50 micrograms ml-1 was included in the incubation medium of skin explants, migration in fibronectin-coated dishes was almost totally blocked. In type I collagen-coated dishes, this concentration of RGDS also inhibited migration, but to a lesser degree than on fibronectin. With 250 micrograms ml-1 of RGES in the medium, the reverse was true. Here, migration on collagen was practically non-existent, while migration on fibronectin was affected only moderately. Collagen-mediated migration was sensitive to RGDS even when the peptide was added after migration on the coated substratum was well underway. At a coating concentration of 10 micrograms ml-1 CB3, a cyanogen bromide fragment of the collagen alpha 1(I) chain, which contains no RGD sequences, was as good a migration substratum as intact collagen applied at the same coating concentration. At lower concentrations intact collagen was somewhat better than equivalent concentrations of CB3. The presence of RGDS in the medium throughout an experiment inhibited migration in CB3-coated dishes in a manner similar to its effect in dishes coated with collagen. On both substrata there appeared to be a peptide-sensitive and a peptide-insensitive component to migration. The inhibitory effect of RGES on CB3-mediated migration was also similar to its effect in collagen-coated dishes.(ABSTRACT TRUNCATED AT 250 WORDS)
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Hirano, Yoshiaki, Motoya Okuno, Toshio Hayashi, Kunio Goto, and Akio Nakajima. "Cell-attachment activities of surface immobilized oligopeptides RGD, RGDS, RGDV, RGDT, and YIGSR toward five cell lines." Journal of Biomaterials Science, Polymer Edition 4, no. 3 (1993): 235–43. http://dx.doi.org/10.1163/156856293x00546.

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Kouns, WC, D. Kirchhofer, P. Hadvary, et al. "Reversible conformational changes induced in glycoprotein IIb-IIIa by a potent and selective peptidomimetic inhibitor." Blood 80, no. 10 (1992): 2539–47. http://dx.doi.org/10.1182/blood.v80.10.2539.2539.

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Abstract Platelet glycoprotein (GP) IIb-IIIa inhibitors may become useful antithrombotic agents. Ro 4–5054 is a low molecular weight, noncyclic, peptidomimetic inhibitor that is three orders of magnitude more potent than RGDS in inhibiting fibrinogen binding to purified GPIIb-IIIa and in preventing platelet aggregation. Comparisons of RGDS and Ro 4–5054 in cell adhesion assays showed that, in contrast to RGDS, Ro 4–5054 was highly selective GPIIb-IIIa inhibitor. Effects of RGDV and Ro 4– 5054 on the conformation and activation state of GPIIb-IIIa were also examined. RGDV and Ro 4–5054 induced conformational changes in purified inactive GPIIb-IIIa as determined by binding of the monoclonal antibody D3GP3 (D3). These conformational alterations were not reversed after inhibitor removal, as indicated by the continued exposure of the D3 epitope and a newly acquired ability to bind fibrinogen. Similarly, RGDV and Ro 4–5054 induced conformational changes in GPIIb-IIIa on the intact platelet. However, after removal of the inhibitors, exposure of the D3 epitope was fully reversed and the platelets did not aggregate in the absence of agonist. Thus, while RGD(X) peptides and Ro 4–5054 transformed purified inactive GPIIb-IIIa into an irreversibly activated conformer, the effects of these inhibitors were reversible on the intact platelet. This suggests that factors present in the platelet membrane or cytoplasm may regulate in part the ability of the complex to shift between active and inactive conformers.
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Kouns, WC, D. Kirchhofer, P. Hadvary, et al. "Reversible conformational changes induced in glycoprotein IIb-IIIa by a potent and selective peptidomimetic inhibitor." Blood 80, no. 10 (1992): 2539–47. http://dx.doi.org/10.1182/blood.v80.10.2539.bloodjournal80102539.

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Platelet glycoprotein (GP) IIb-IIIa inhibitors may become useful antithrombotic agents. Ro 4–5054 is a low molecular weight, noncyclic, peptidomimetic inhibitor that is three orders of magnitude more potent than RGDS in inhibiting fibrinogen binding to purified GPIIb-IIIa and in preventing platelet aggregation. Comparisons of RGDS and Ro 4–5054 in cell adhesion assays showed that, in contrast to RGDS, Ro 4–5054 was highly selective GPIIb-IIIa inhibitor. Effects of RGDV and Ro 4– 5054 on the conformation and activation state of GPIIb-IIIa were also examined. RGDV and Ro 4–5054 induced conformational changes in purified inactive GPIIb-IIIa as determined by binding of the monoclonal antibody D3GP3 (D3). These conformational alterations were not reversed after inhibitor removal, as indicated by the continued exposure of the D3 epitope and a newly acquired ability to bind fibrinogen. Similarly, RGDV and Ro 4–5054 induced conformational changes in GPIIb-IIIa on the intact platelet. However, after removal of the inhibitors, exposure of the D3 epitope was fully reversed and the platelets did not aggregate in the absence of agonist. Thus, while RGD(X) peptides and Ro 4–5054 transformed purified inactive GPIIb-IIIa into an irreversibly activated conformer, the effects of these inhibitors were reversible on the intact platelet. This suggests that factors present in the platelet membrane or cytoplasm may regulate in part the ability of the complex to shift between active and inactive conformers.
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Lankhof, H., YP Wu, T. Vink, et al. "Role of the glycoprotein Ib-binding A1 repeat and the RGD sequence in platelet adhesion to human recombinant von Willebrand factor." Blood 86, no. 3 (1995): 1035–42. http://dx.doi.org/10.1182/blood.v86.3.1035.1035.

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Abstract To assess the relative importance of the glycoprotein (GP) Ib binding domain and the RGDS binding site in platelet adhesion to isolated von Willebrand factor (vWF) and to collagen preincubated with vWF, we deleted the A1 domain yielding delta A1-vWF and introduced an aspartate- to-glycine substitution in the RGDS sequence by site-directed mutagenesis (RGGS-vWF). Recombinant delta A1-vWF and RGGS-vWF, purified from transfected baby hamster kidney cells, were compared with recombinant wild-type vWF (WT-vWF) in platelet adhesion under static and flow conditions. Purified mutants were coated on glass or on a collagen type III surface and exposed to circulating blood in a perfusion system. Platelet adhesion under static condition, under flow conditions, and in vWF-dependent adhesion to collagen has an absolute requirement for GPIb-vWF interaction. The GPIIb/IIIa-vWF interaction is required for adhesion to coated vWF under flow conditions. Under static condition and vWF-dependent adhesion to collagen, platelet adhesion to RGGS-vWF is similar as to WT-vWF, but platelet spreading and aggregation are abolished.
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Lankhof, H., YP Wu, T. Vink, et al. "Role of the glycoprotein Ib-binding A1 repeat and the RGD sequence in platelet adhesion to human recombinant von Willebrand factor." Blood 86, no. 3 (1995): 1035–42. http://dx.doi.org/10.1182/blood.v86.3.1035.bloodjournal8631035.

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To assess the relative importance of the glycoprotein (GP) Ib binding domain and the RGDS binding site in platelet adhesion to isolated von Willebrand factor (vWF) and to collagen preincubated with vWF, we deleted the A1 domain yielding delta A1-vWF and introduced an aspartate- to-glycine substitution in the RGDS sequence by site-directed mutagenesis (RGGS-vWF). Recombinant delta A1-vWF and RGGS-vWF, purified from transfected baby hamster kidney cells, were compared with recombinant wild-type vWF (WT-vWF) in platelet adhesion under static and flow conditions. Purified mutants were coated on glass or on a collagen type III surface and exposed to circulating blood in a perfusion system. Platelet adhesion under static condition, under flow conditions, and in vWF-dependent adhesion to collagen has an absolute requirement for GPIb-vWF interaction. The GPIIb/IIIa-vWF interaction is required for adhesion to coated vWF under flow conditions. Under static condition and vWF-dependent adhesion to collagen, platelet adhesion to RGGS-vWF is similar as to WT-vWF, but platelet spreading and aggregation are abolished.
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Dissertations / Theses on the topic "RGDS"

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Guven, Sinan. "Integrated Biomimetic Scaffolds For Soft Tissue Engineering." Master's thesis, METU, 2006. http://etd.lib.metu.edu.tr/upload/3/12607436/index.pdf.

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Tissue engineering has the potential to create new tissue and organs from cultured cells for transplantation. Biodegradable and biocompatible scaffolds play a vital role in the transfer of the cultured cells to a new tissue. Various scaffolds for soft tissue engineering have been developed, however there is not any structure totally mimicking the natural extracellular matrix (ECM), ready to use. In this study biodegradable and biocompatible scaffolds were developed from natural polymers by tissue engineering approach and tested in vitro. Scaffolds (SCAF) were prepared with freeze drying and composed of chitosan, gelatin and dermatan sulfate. Polymer solutions were treated with different stirring rates (500 rpm and 2000 rpm), freezing temperatures (-20 &deg<br>C and -80 &deg<br>C) and molding (cylindrical mold and petri dish) to achieve porous structure in order to provide sufficient space for cell growth and extracellular matrix production. Among the prepared scaffolds at different conditions, the scaffolds prepared at 500 rpm and frozen at -80 &deg<br>C, (SCAF-1), was chosen for further studies. These scaffolds achieved 0.512 MPa tensile strength, with 9.165 MPa tension modulus and 3.428 MPa compression modulus. Besides in lysozyme containing degradation medium they conserved their integrity and lost about 30 % of their initial weight in 30 days period. Mechanical and enzymatic degradation tests showed that scaffolds have physical integrity for the tissue engineering applications. To mimic the natural tissue and enhance cell growth, biologically active arginine &amp<br>#8211<br>glycine - aspartic acid - serine (RGDS) peptides and platelet derived growth factor-BB (PDGF-BB) were immobilized on the SCAF-1. Fibroblast cells were seeded on the scaffolds containing RGDS, (SCAF-1-RGDS), and PDGF-BB, (SCAF-1-RGDS-PDGF), and incubated in media either free of serum or containing serum. Scaffolds immobilized with RGDS and PDGF-BB had the highest attached cell number by the day 15. Florescence microscopy studies also indicated that RGDS and RGDS-PDGF modified scaffolds were more suitable than controls, (SCAF-1), for cell growth and proliferation. According to scanning electron microscopy (SEM) results, modified scaffolds demonstrated better cell morphology and attachment of cells. Based on the obtained results, it can be concluded that RGDS-PDGF immobilized chitosan-gelatin-dermatan sulfate systems have a great potential to be used as a scaffold for soft tissue engineering applications.
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Stumpf, da Silva Taisa Regina. "Delivery Systems to Enhance Neural Regeneration in the Central Nervous System." Thesis, Université d'Ottawa / University of Ottawa, 2019. http://hdl.handle.net/10393/39391.

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Leed, Maren. "Keeping the warfighting edge : an empirical evaluation of Army officers' tactical expertise over the 1990s /." Santa Monica, CA : RAND, 2000. http://www.rand.org/publications/RGSD/RGSD152/.

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Kilgore, Meredith L. "Effects of trial design on participation and costs in clinical trials : with an examination of cost analysis methods and data sources /." Santa Monica, Calif. : Pardee RAND Graduate School, 2004. http://www.rand.org/publications/RGSD/RGSD179.

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Souza, Keith Seixas de. "WS&i*-RGPS: uma abordagem de engenharia de requisitos orientada a serviços Web baseada nos metamodelos RGPS." Universidade de São Paulo, 2014. http://www.teses.usp.br/teses/disponiveis/100/100131/tde-04022015-133853/.

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Recentemente, por conta do dinamismo existente no ambiente de negócio no qual as organizações devem adequar-se mais rapidamente às mudanças, os Sistemas de Informação (SIs) precisam também adequar-se para continuar agregando valor. Diante desse cenário e do uso de serviços eletrônicos distribuídos na rede para o desenvolvimento de sistemas, faz-se necessário o surgimento de novas abordagens em engenharia de sistemas. Sendo assim, surge a disciplina de Engenharia de Requisitos Orientada a Serviços (EROS) que trata da definição de processos e metodologias para captar os requisitos de serviços tanto do ponto de vista de consumidores de serviço quanto de fornecedores de serviço. No contexto de EROS, este trabalho explora alternativas às descrições sugeridas para os metamodelos RGPS (do inglês: Role, Goal, Process and Service) uma abordagem em EROS propondo uma nova definição que visa, principalmente, incorporar à RGPS as vantagens de outros modelos já estabelecidos na literatura. Sendo assim, a nova abordagem aqui proposta, chamada de WS&i*-RGPS, para a descrição das camadas Papel e Meta, propõe o uso do framework i*. E, para a descrição das camadas Processo e Serviço, a nova abordagem propõe o uso de WS-BPEL/WSDL. Esse trabalho apresenta também uma comparação sistemática entre a abordagem WS&i*-RGPS e outras abordagens semelhantes identificadas na literatura EROS. A comparação sistemática entre as abordagens em EROS, incluindo a nova abordagem aqui proposta, considera três parâmetros comparativos e identifica que a abordagem WS&i*-RGPS cobre mais parâmetros que as abordagens em EROS que se baseiam nos metamodelos RGPS, indicando que WS&i*-RGPS é uma alternativa melhor às soluções inicialmente propostas pelos autores dos metamodelos RGPS.<br>Due to the recent business environment dynamism in which organizations must quickly adapt to the changes, Information Systems also need to adapt to these changes in order to keep adding value. Taking into account this scenario and the use of electronic services distributed on the network to develop systems, the advent of new approaches in Systems Engineering is necessary. Therefore, a new discipline, Service-Oriented Requirements Engineering (SORE), was proposed, which deals with the definition of processes and methodologies in order to capture services requirements beneath two different perspectives: service consumers and service providers. In SORE context, this work aims at exploring some alternatives for those descriptions proposed by the Role, Goal, Process and Service (RGPS) meta-models, proposing a new approach called WS&i*-RGPS in order to incorporate to RGPS the advantages of other models well established in the literature. Accordingly, in order to describe the Role and Goal layers, this new approach proposes the use of the i* framework. Additionally, in order to describe the Process and Service layers, this new approach proposes the use of WS-BPEL/WSDL languages. This work also presents a systematic comparison among SORE approaches, including WS&i*-RGPS. This comparison considers three comparative parameters and identifies that WS&i*-RGPS covers more parameters than other approaches in SORE that uses RGPS metamodels. These results indicates WS&i*-RGPS as a better alternative comparing it to other RGPS approaches.
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Thumshirn, Georgette. "Multivalente zyklische RGD-Peptide und RGD-Mimetika für den Einsatz in Tumordiagnostik und Tumortherapie." [S.l.] : [s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=96988950X.

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Engrand, Philippe. "Calix[4]arènes fonctionnels pour ancrage sur polymère naturel et antennisation par le tripeptide RGD préparé par synthèse convergente." Thesis, Nancy 1, 2008. http://www.theses.fr/2008NAN10143/document.

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Ce travail porte sur la valorisation du calix[4]arène comme complexant de métaux de transition, immobilisé sur un matériau, et comme vecteur de principe actifs, aptes à interagir avec des récepteurs cellulaires. En premier lieu, la monofonctionnalisation sélective d’un calix[4]arène, sur sa partie haute ou sur sa partie basse est réalisée. Les fonctions nitro, amine, adéhyde, et alcène ont été incorporées sur la partie basse, via un bras espaceur, et un bras acide a été incorporé sur la partie haute. Ces calix[4]arènes monofonctionnalisés se déclinent en trois séries de composés, dépendant du degré et de la nature des substituants sur la partie basse : tétrol, triméthoxy et trisbipyridyle. Le second objectif est le greffage d’un calix[4]arène pourvu d’une fonction amine, sur un polymère naturel, cellulose ou dextran. Un mode opératoire reproductible a été mis au point, qui a permis d’obtenir un calix[4]arène complexant de l’ion Cu(I), immobilisé sur cellulose en poudre ou sur dextran. L'évaluation du taux de greffage par RMN et dosage UV-Vis en présence de Cu+ est décrite pour les dextrans. Enfin, nous avons incorporé sur la partie haute du calix[4]arène d'antennes de reconnaissance cellulaire de type RGD, préparées par synthèse convergente en solution. Une chimiothèque de tripeptides RGD, modulés sur les parties C- et N-terminales, a été obtenue avec de bons rendements. Ces peptides ont fait l’objet d’une évaluation biologique (adhésion cellulaire). Nous avons ainsi préparé des calix[4]arènes, de conformation conique, antennisés par le dipeptide GD et le tripeptide RGD, destinés à élaborer des modèles de vecteurs supramoléculaire de principes actifs<br>The aim of this present work is dedicated to the valorization of calix[4]arene as a transition-metal complexing agent, grafted on a polymeric material, and as a drug carrier, displaying a cell recognition peptidic sequence. We describe selective monofunctionalization of a calix[4]arene, at the upper rim or at the lower rim. Nitro, amino, aldehyde and alcene functions were incorporated on the calix[4]arene lower rim, via a spacer. In the same way, an acid arm was also incorporated on the calix[4]arne upper rim. We made those monofunctionalized calix[4]arenes available into three series, depending on the number and the nature of substituent on the three residual OH groups of the calix[4]arne carried function : tetrol, trimethoxy and trisbipyridyl. The second goal is dedicated to the grafting of an amino-fonctionalized calix[4]arene, on a natural polymer, such as cellulose or dextran. We have developped a method allowing to access to a new polymeric complexing agent. We also describe the grafting-ratio, calculated by NMR, UV-Vis and titration with Cu+. The third goal is dedicated to the grafting of the cell-recognizing RGD sequence, prepared in solution by a gram-scale convergent synthesis. A RGD analogue library, functionalized by variable groups on the C- and N- terminations, were obtained with interestly yields. Those peptides were involved into a biological evaluation (cellular adhesion). Thus, cone-conformed calix[4]arene incorporating the GD or RGD peptide sequence were elaborated as preliminary models for the access to new drug-carrier molecular devices
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Shanks, Ryan H. Dohlman Henrik G. "RGS domain-independent Sst2 action." Chapel Hill, N.C. : University of North Carolina at Chapel Hill, 2008. http://dc.lib.unc.edu/u?/etd,1923.

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Thesis (M.S.)--University of North Carolina at Chapel Hill, 2008.<br>Title from electronic title page (viewed Dec. 11, 2008). "... in partial fulfillment of the requirements for the degree of Master of Science in the Department of Pharmacology." Discipline: Pharmacology; Department/School: Medicine.
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Stein, Bradley D. "Drug and alcohol treatment services among privately insured individuals in managed behavioral health care." Santa Monica, CA : RAND, 2003. http://www.rand.org/publications/RGSD/RGSD170/RGSD170.pdf.

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Melamid, Elan. "What works? integrating multiple data sources and policy research methods in assessing need and evaluating outcomes in community-based child and family service systems /." Santa Monica, Calif. : RAND, 2002. http://www.rand.org/publications/RGSD/RGSD161/RGSD161.pdf.

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Books on the topic "RGDS"

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Figueiredo, Antonio Borges de. Salário-maternidade no RGPS. Editora LTr, 2007.

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ʼJig rten rgas poʼi spro gtam. Tshe-riṅ-rgyal-mtshan, 2000.

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Bianco, Dânae Dal. O benefício de pensão por morte do RGPS. LTr, 2012.

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Bar-khams Re-dkar-sog-gsum gyi lo rgus. Bod gźuṅ phyi dril Snar-thaṅ par khaṅ du par skrun źus], 1999.

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Portinho, José Gomes. Achegas à Araripe: Guerra civil no RGS. M.P. Dornelles, 1990.

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Su, Wei. Characterization of N-GAIP, a novel RGS protein. National Library of Canada, 1998.

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Yager, Loren. Life after RGS: Thoughts on becoming a "suit". RAND, 1992.

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Marçal, João Batista. Primeiras lutas operárias no RGS: Origens do sindicalismo rio-grandense. Livraria do Globo, 1985.

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Mello, Sergio Renato de. Comentário e interpretação da Lei previdenciária no Regime Geral da Previdência Social (RGPS). LTr, 2013.

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Goldstein, Melvyn C. Pha yul gyi phan bdeʼi ched du: Bkra-śis-tshe-riṅ gi lo rgus. Bod-kyi Dpe-mdzod-khaṅ, 2010.

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Book chapters on the topic "RGDS"

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Zhao, Ming, Shi-qi Peng, Meng-shen Cai, Chao-shu Tang, and Chang-ling Li. "Antiplatelet and vasodilation effects of RGDS." In Peptides. Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-010-9066-7_52.

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Rechichi, A., S. Sartori, A. Caporale, et al. "Development of a RGDS-peptide modified polyurethane for tissue regeneration." In Advances in Experimental Medicine and Biology. Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-73657-0_114.

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Kasuya, Yuji, Yukio Inomata, Hideki Gakumazawa, Keiji Fujimoto, and Haruma Kawaguchi. "Rgds-Carrying Latex Particles for Cell Activation and Integrin Separation." In Advanced Biomaterials in Biomedical Engineering and Drug Delivery Systems. Springer Japan, 1996. http://dx.doi.org/10.1007/978-4-431-65883-2_52.

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Samanen, J., F. E. Ali, T. Romoff, et al. "SK&F 106760: Reinstatement of high receptor affinity in a peptide fragment (RGDS) of a large glycoprotein (fibrinogen) through conformational constraints." In Peptides 1990. Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3034-9_324.

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Guo, Tianruo, David Tsai, Siwei Bai, et al. "Insights from Computational Modelling: Selective Stimulation of Retinal Ganglion Cells." In Brain and Human Body Modeling 2020. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-45623-8_13.

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AbstractImprovements to the efficacy of retinal neuroprostheses can be achieved by developing more sophisticated neural stimulation strategies to enable selective or differential activation of specific retinal ganglion cells (RGCs). Recent retinal studies have demonstrated the ability to differentially recruit ON and OFF RGCs – the two major information pathways of the retina – using high-frequency electrical stimulation (HFS). However, there remain many unknowns, since this is a relatively unexplored field. For example, can we achieve ON/OFF selectivity over a wide range of stimulus frequencies and amplitudes? Furthermore, existing demonstrations of HFS efficacy in retinal prostheses have been based on epiretinal placement of electrodes. Other clinically popular techniques include subretinal or suprachoroidal placement, where electrodes are located at the photoreceptor layer or in the suprachoroidal space, respectively, and these locations are quite distant from the RGC layer. Would HFS-based differential activation work from these locations? In this chapter, we conducted in silico investigations to explore the generalizability of HFS to differentially active ON and OFF RGCs. Computational models are particularly well suited for these investigations. The electric field can be accurately described by mathematical formulations, and simulated neurons can be “probed” at resolutions well beyond those achievable by today’s state-of-the-art experimental techniques.
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Martemyanov, Kirill A., Pooja Parameswaran, Irene Aligianis, et al. "RGS Proteins." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101174.

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Martemyanov, Kirill A., Pooja Parameswaran, Irene Aligianis, et al. "RGS Protein Family." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_527.

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Siderovski, David P., and Adam J. Kimple. "RGS Protein Family." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_527.

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Pons, Jean-François, Mamadou Sow, Frédéric Lamaty, et al. "New RGD amphiphilic cyclic peptide and new RGD-mimetic constrained diketopiperazines." In Peptides Frontiers of Peptide Science. Springer Netherlands, 2002. http://dx.doi.org/10.1007/0-306-46862-x_69.

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Bauch, Jürgen, and Rüdiger Rosenkranz. "RGS - Röntgengrobstrukturinspektion X-ray Radiography." In Physikalische Werkstoffdiagnostik. Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-53952-1_13.

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Conference papers on the topic "RGDS"

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Charon, M. H., L. Tranqui, A. Andrieux, G. Hudry-Clergeon, and G. Marguerie. "FIBRINOGEN BINDING TO ENDOTHELIAL CELLS AND INTERFERING PEPTIDES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644735.

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Fibrinogen interacts with platelets and endothelial cells via specific binding sites. While the platelet fibrinogen receptor has been identified and was found to be associated with GPIIb-IIIa, the binding site on endothelial cells has not been characterized yet. The platelet GPIIb-IIIa belongs to the newly identified cytoadhesin family which includes immunologicaly related receptors interacting with RGD containing proteins. A cytoadhesin has recently been described on endothelial cells and the possibility that fibrinogen might interact with this glycoprotein was examined. Peptides corresponding to γ and α chains sequences were synthesized and their capacity to inhibit fibrinogen binding to endothelial cells and platelets were compared. Analogues of the γ chain from His 400 to Val 411 produced an inhibition similar to that observed for fibrinogen platelet interaction, suggesting that the structure function relationship of γ peptides is identical in both systems. In contrast synthetic analogues corresponding to the a chain and including RGD yielded slightly different results. While RGD alone was inactive on platelet, this tripeptide was active on endothelial cells. RGDS and RGDF corresponding to α 572-575 and α 95-98 partially or fully inhibited fibrinogen binding to endothelial cells but the structure activity relationship was different when compared to that observed for platelets. Addition of the N and C sequences adjacent to RGDS reduced the activity of this peptide whereas the activity of RGDF analogues was not modified by addition of N and C-sequences. In contrast platelet fibrinogen binding decreased with these RGDF analogues. These results suggest that fibrinogen endothelial cell binding is mediated by an RGD adhesion receptor with subtle differences in the recognition selectivity of the ligand, which is controled by the surrounding sequence.
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Parise, L. V., B. Steiner, L. Nannizzi, and D. A. Phillips. "PEPTIDES FROM FIBRINOGENAND FIBRONECTIN CHANGE THE CONFORMATIONOF PURIFIED PLATELET GLYCOPROTEIN IIb-IIIa." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643697.

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Specific amino acid sequences in fibrinogen and fibronectin appear to mediate the binding of these ligands to the glycoprotein (GP) IIb-IIIacomplex in platelets. Thesesequences include LGGAKQAGDV from the y chain of fibrinogen, and RGD(S) from the a chain of fibrinogenand the cell-binding domain of fibronectin. Several recent reports suggest thatfibrinogen and/or peptides with these sequences cause clustering of GPIIb-IIIa on the platelet surface and Na+/H+ exchange in epinephrine-stimulated platelets. Thus, it is possible that occupancy of specific sites on GP Ilb-IIIa affects its conformation, initiating such events. In this study,we determined whether LGGAKQAGDV, RGDS, and related peptides affect the conformation of purified platelet GP IIb-IIIa. Conformational changes in GP IIb-IIIa were evaluated bychanges in proteolytic susceptibility and hydrodynamic properties. Thepurified GP IIb-IIIa complex was fund to be resistant to proteolysis bythrombin. However, pretreatment of GP IIb-IIIa with various peptidesincreased the susceptibility ofGP libα to thrombin-induced proteolysis,as quantitated onpolyacryfamide gels.The order of potency of these peptides was RGDS&lt;LGGAKQAGDV &lt; KGDS &lt; RGES. This order of potency agrees with that for the abilityof these peptides to inhibit 125I-fibrinogen binding to platelets. The effect of the peptides on proteolysis was time-, temperature-, and concentration-dependent; RGDS Induced a half-maximal effect at ˜60μM. Evaluation of the hydrodynamic properties of GP IIb-IIIa showed that LGGAKQAGDV orRGDS, but not RGES, decreased thesedimentation coefficient of GP IIb-IIIa from 8.5S to 7.7 S or7.4, S,respectively. This changewas accompanied by an increase in theStoke’s radius from 73 A to 84 A. These results suggestthat LGGAKQAGDV andRGDS alterthe conformationof the purified GPIIb-IIIa heterodimer complex by causing it to unfold.This change in conformation may be related to changesin the distribution and function of GP IIb-IIIaon the platelet surface that occurwith occupancy ofligand binding sites.
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Taki, Y., Y. Morita, S. Nishimura, A. Hirata, T. Koga, and E. Nakamachi. "Development of Surface Treatment Technique With Photolytic Macromolecule Including RGDS Peptide." In ASME 2016 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2016. http://dx.doi.org/10.1115/imece2016-66466.

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Arg-Gly-Asp-Ser (RGDS) coating is one of effective methods to improve the cell adhesive property of the scaffold surface. However, it is difficult to regulate the RGDS quantity and distribution, and to visualize RGDS distribution. The purpose of this study was to develop a surface treatment technique that the RGDS quantity can be regulated with the ultraviolet rays irradiation and the RGDS distribution can be visualized with the fluorescence. P(MMA-g-ANP-RGDS) and P(HEMA-g-ANP-RGDS) were respectively synthesized by radical copolymerization of methylmethacrylate (MMA) and 2-hydroxyethylmethacrylate (HEMA) with peptide-macromonomer containing photo-labile linker (3-amino-3-(2-nitrophenyl)propionic acid (ANP)) and RGDS. Each polymer film was produced by using spin-coater, and then ultraviolet rays was irradiated to the each film through the glass mask with three different ultraviolet rays transmissivity of 0 %, 30 % and 60 %. In both polymer films, the RGDS quantity can be regulated by ultraviolet rays irradiation, and the luminance decreased same as the RGDS quantity. Adherent osteoblast-like cells were not observed on P(HEMA-g-ANP-RGDS) film, but the number of adherent osteoblast-like cells was increased with increasing the RGDS quantity on the P(MMA-g-ANP-RGDS) film. In conclusion, we accomplished to develop the surface treatment technique with P(MMA-g-ANP-RGDS) to regulate and visualize the RGDS quantity and distribution.
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Harfenist, E. J., M. A. Packham, and J. F. Mustard. "EFFECTS OF CELL ADHESION PEPTIDE, Arg-Gly-Asp-Ser (RGDS), ON RESPONSES OF WASHED PLATELETS FROM HUMANS, RABBITS AND RATS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643592.

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Fibrinogen (Fbg) is a cofactor in the aggregation of human platelets, and washed platelets do not aggregate to a significant extent in response to ADP unless Fbg is added to the suspension; however, exogenous Fbg is not required for ADP-induced aggregation of washed platelets from rabbits or rats. Since, with human platelets, Arg-Gly-Asp-Ser (RGDS) inhibits aggregation and the binding of 125I-Fbg to ADP-stimulated platelets, its effects on the responses of rabbit and rat platelets were studied in an attempt to elucidate the differences in Fbg requirements of platelets from the three species. Aggregation and Fbg binding were studied using washed platelets suspended in Tyrode solution containing albumin, apyrase and 2 mM Ca2+. 50 μM RGDS caused over 80% inhibition of the aggregation of human platelets stimulated with 9 yM ADP in the presence of 0.2 yM Fbg, but only 3-9% inhibition of the ADP-induced aggregation of rabbit or rat platelets regardless of whether exogenous Fbg was added. 50 yM RGDS also inhibited the aggregation of human platelets stimulated with thrombin (0.9 U/mL), but produced no more than 3% inhibition with rabbit or rat platelets. The binding of 125I-Fbg to ADP-stimulated human platelets was inhibited by 80-90% by 30 yM RGDS, but even at 50 μM, RGDS inhibited Fbg binding to rabbit or rat platelets by only 15-27%. The differences were due to the species of platelets, since, with both human and rabbit platelets, human Fbg could be replaced by rabbit Fbg without significantly changing the results. RGDS, added to human platelets that had been aggregated with thrombin, did not cause deaggregation, but did partially inhibit aggregation when added within 1 min; this inhibitory effect was less than when RGDS was added before thrombin, and decreased progressively as the length of time before the addition of RGDS was increased. These observations indicate a difference in aggregation mechanism between human platelets and those from rabbits and rats, and are consistent with a Fbg-independent component to the aggregation of rabbit and rat platelets.
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Cohen, I., and J. G. White. "DIFFERENT SITES FOR FIBRINOGEN AND FIBRIN RECEPTORS ON PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643521.

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Platelet stickiness and aggregation depend on availability of surface membrane glycoprotein Ilb-IIIa complex to bind fibrinogen. The development of isometric tension in platelet-rich clots is a manifestation of fibrin binding to the cells as well as platelet contractile activity. The possibility that fibrinogen and fibrin may bind to different portions of the GPIIb-IIIa complex has apparently not been considered. In order to determine whether the receptors for the fibrinogen and fibrin on the GPIIb-IIIa complex are identical, we investigated the effect of various monoclonal antibodies to the Ilb-IIIa complex and the tetrapeptide Arg-Gly-Asp-Ser (RGDS), a recognition site on fibrinogen for IIb-IIIa, on the development of isometric tension and ultrastructure of platelet-fibrin clots. Monoclonal antibodies A2A6 and 7E3 decreased the maximal tension, as well as the rate of tension development. Platelets and fibrin were oriented longitudinally in antibody treated clots, but the concentrations of fibrin and platelet aggregates determined by morphometry were significantly reduced. T10 and 10E5 increased tension, while AP2 and PAC1 had no substantial effect. Increasing concentrations of RGDS from 62.5 pM to 500 pM resulted in greater maximal tension and rate of tension development, reaching a five-fold increase when 500 pM RGDS was used. RGDS did not affect the Mg-stimulated platelet actomyosin ATPase activity. Morphometry revealed increased concentrations of oriented fibrin and platelet aggregates in RGDS-treated clots. Results of this study confirm the different topography of the epitopes on the Ilb-IIIa complex and provide evidence for different receptor sites for fibrinogen and fibrin on the IIb-IIIa complex
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Gustafson, E. J., H. Lukasiewicz, A. H. Schmaier, S. Niewiarowski, and R. W. Colman. "FIBRINOGEN BINDS TO HUMAN NEUTROPHILS AT A SITE DISTINCT FROM GPIIb/IIIa." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643850.

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Many observations suggest a potential role for neutrophils in the modulation of hemostasis and thrombosis. Arterial thrombi are characterized by the presence of large numbers of neutrophils lining the perimeter of platelet aggregates. While investigating binding of high molecular weight kininogen (HMWK) to neutrophils, we found that fibrinogen (Fb) could inhibit binding of 125I-HMWK as well as displace HMWK already bound to neutrophils. We therefore initiated studies to determine whether Fb could bind to human neutrophils. Both Zn++ and Ca++ were required for maximal binding of 125I-Fb to neutrophils. Binding did not occur with Ca++ (ZmM) alone and was only 1/3 the maximal amount with Zn++ (50 μM) alone. At 4° the amount of 125I-Fb bound to neutrophils reached a plateau by 15 minutes and remained at this level over the next 30 minutes. At 23° and 37° the amount of 125I-Fb bound peaked by 4 minutes and then decreased over the next 30 minutes indicating receptor-mediated internalization. Excess Fb inhibited binding of 125I-Fb to neutrophils while prekal1ikrein, factor XII, and fibronectin did not. Binding of 125I-Fb was 99% reversible at 4° within 10 minutes with a 50-fold molar excess of Fb and 90% displaceable by excess HMWK. The apparent Kd was approximately 0.45 μM. Arg-Gly-Asp-Ser (RGDS) is a tetrapeptide common to Fb, fibronectin, vitronectin and other cel 1-attachment proteins. Fb has been demonstrated to bind to the glycoprotein IIb/111 a (GPIIb/IIIa) complex which is the platelet membrane receptor for RGDS. Although this RGDS-GPIIb/IIIa interaction occurs with Fb binding to platelets, it is apparently not involved with Fb binding to monocytes. To investigate if Fb binding to neutrophils involved this interaction of GPIIb/II la -RGDS we performed further studies. Binding of 125I-Fb to neutrophils was not inhibited by RGDS nor was it inhibited by a monoclonal antibody (10E5) to the platelet GPI I b/IIIa complex. In addition, the amount of 125I-Fb that hound to neutrophils from a patient with Glanzman's thrombosthenia was the same as that bound to normal neutrophils. These studies indicate that human neutrophils specifically bind Fb at a site similar to HMWK and distinct from GPIIb/IIIa.
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Hantgan, R. R. "LOCALIZATION OF THE DOMAINS OF FIBRIN INVOLVED IN BINDING TO PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643773.

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The molecular basis of platelet-fibrin interactions has been investigated by using synthetic peptides as potential inhibitors of binding fibrin protofibrils and fibrinogen to ADP-stimulated platelets, adhesion of fibrin fibers to the platelet surface, and platelet-mediated clot retraction. Synthetic peptides RGDS and HHLGGAKQAGDV, corresponding to regions of the fibrinogen α and γ chains previously identified as platelet recognition sites, inhibited the binding of radiolabelled soluble fibrin oligomers to ADP-stimulated platelets with IC50 values of 12 and 40 μM, respectively. The IC50 values obtained with fibrinogen as the ligand were 3-fold higher. Synthetic GPRP and GHRP, corresponding to the N-terminal sequences of the fibrin α and β chains, were minimally effective in blocking soluble fibrin oligomer binding to ADP-stimulated platelets. The extent of fibrin:platelet adhesion was determined with a microfluorimetric technique which measures the quantity of fluorescein-labelled fibrin attached to the surface of platelets. The signal obtained from the brightly fluorescent platelet:fibrin adducts was time- and concentration-dependent, and was fully inhibited by a monoclonal antibody directed against the glycoprotein II:IIIa complex (HP1-1D, kindly provided by Dr. W. Nichols). Inhibition of fibrin:platelet adhesion by RGDS, HHGGAKQAGDV, and GHRP all exhibited a similar, linear dependence on the peptide concentration, reaching 1/2 maximum at about 200 μM, suggesting nonspecific effects. GPRP inhibited fibrin assembly but did not appear to have specific effects on fibrin:platelet adhesion. The time course of clot retraction was followed by right angle light scattering intensity measurements. Only RGDS affected clot retraction, causing a 4-fold decrease in rate at 230 μM. These results indicate that fibrinogen and fibrin protofibrils, which are obligatory intermediates in the fibrin assembly pathway, share a set of common platelet recognition sites located at specific regions of the α and γ chains of the multinodular fibrin(ogen) molecules. The RGDS site is also involved in mediating interactions between the three dimensional fibrin network and ADP-stimulated platelets.
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Nievelstein, P. F. E. M., M. Ottenhof-Rovers, M. D. Pierschbacher, and J. J. Sixma. "THE ARG-GLY-ASP(SER) SEQUENCE OF FIBRONECTIN, AND THE GLYCOPROTEIN IIB-IIIA COMPLEX ARE NOT INVOLVED IN FIBRONECTIN DEPENDENT PLATELET ADHESION IN FLOW." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643590.

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Activated blood platelets interact with fibronectin through it to the glycoprotein IIb-IIIa(GPIIb-IIIa)-complex. The cell attachment site of fibronectin with its crucial arg-gly-asp-(-ser) (RGD(S))sequence is involved in this binding. We have studied the importance of this interaction for the fibronectin dependence of platelet adhesion under flow conditions. An RGDS-containing hexapeptide (GRGDSP) was compared with a non-reactive control peptide (GRGESP). The GRGDSP-peptide inhibited thrombin induced aggregation and adhesion under static conditions at 0.1 mM. This concentration had no effect on platelet adhesion to nonfibrillar collagen type I in flow. GRGDSP at 1 mM had a significant inhibitory effect at 1500 s™1 (8.8 ± 1.4 111In platelets* 105 /cm2, versus 19.8 ± 0.5 for the control). At lower shear rates of 800 and 300 s™1 , where platelet adhesion is also fibronectin dependent, no significant differences were obtained (respectively 11.7 ± 1.1 versus 15.2 ± 2.1, and 11.4 ± 1.0 versus 13.1 ± 0.7).The relation between GPIIb-IIIa and fibronectin dependence was investigated with platelets of a patient with Glanzmann’s thrombasthenia and monoclonal antibodies to GPIIb-IIIa, using endothelial cell matrix (ECM) as a surface. Platelets of normal controls or a patient with Glanzmann’s thrombasthenia showed a inhibition of adhesion in fibronectin free plasma, after the ECM had been preincubated with anti-fibronectin F(ab’)2, of respectively _J5 and 30 percent at 300 s™1 , and 43 and 65 percent at 1300 s™1 . Incubation of platelets with anti GPIIb-IIIa showed inhibition of platelet adhesion at high shear rates. Dependence on fibronectin for platelet adhesion was still observed, even though separate experiments had shown that these anti GPIIb-IIIa antibodies could block binding of radiolabeled fibronectin to thrombin activated platelets. These data suggest the existence of a second binding system from the RGD/GPIIb-IIIa system separate for the interaction of platelets with fibronectin, which may only function when fibronectin is present on a surface.
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Dekkers, BG, IS Bos, R. Gosens, AJ Halayko, J. Zaagsma, and H. Meurs. "Inhibition of Airway Smooth Muscle Remodeling in an Animal Model of Chronic Asthma by the Integrin-Blocking Peptide RGDS." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a5600.

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Timmons, Sheila, and Jack Hawiger. "REGULATION OF PLATELET RECEPTORS FOR FIBRINOGEN AND VON WILLEBRAND FACTOR BY PROTEIN KINASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644674.

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Positive and negative regulation of platelet receptors for adhesive proteins, fibrinogen (F) and von Willebrand Factor (vWF) determines whether binding of these ligands will or will not take place. We have shown previously that ADP stimulates and cyclic AMP inhibits binding of F and vWF to human platelets. Now we show that positive regulation of F and vWF binding to platelets via the glycoprotein 11b/1111a complex is dependent on platelet Protein Kinase C, a calcium- and phospholipid-dependent enzyme. A potent activator of Protein Kinase C, phorbol-12-myristoyl-13-acetate (PMA) induced saturable and specific binding of F and vWF which was inhibited by synthetic peptides, gamma chain .dodecapeptide (gamma 400-411) and RGDS. The phosphorylation of 47kDa protein (P47), a marker of Protein Kinase C activation in platelets, preceded binding of F and vWF induced with PMA as well as with ADP and thrombin. Sphingosine, an inhibitor of Protein Kinase C, blocked binding of F and vWF to platelets stimulated with PMA, ADP, and thrombin. Inhibition of binding was concentration-dependent and it was accompanied by inhibition of platelet aggregation. Thus, stimulation of Protein Kinase C is required for exposure of platelet receptors for adhesive proteins whereas inhibition of Protein Kinase C prevents receptorexposure. Protein Kinase C fulfills the role of an intraplatelet signal transducer, regulating receptors for adhesive proteins, and constitutes a target for pharmacologic modulation of the adhesive interactions of platelets.
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Reports on the topic "RGDS"

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Casal, Ignacio. Metástasis, integrinas y cadherinas RGD. Sociedad Española de Bioquímica y Biología Molecular (SEBBM), 2016. http://dx.doi.org/10.18567/sebbmdiv_anc.2016.11.1.

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Hint, C. RGD # A-9 Complete Characterization. Office of Scientific and Technical Information (OSTI), 2020. http://dx.doi.org/10.2172/1682520.

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Kwok, Ron. Enhanced RADARSAT Geophyiscal Processor System (RGPS) Products over the SHEBA Ice Camp. Defense Technical Information Center, 2001. http://dx.doi.org/10.21236/ada625934.

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Kwok, Ron. Enhanced RADARSAT Geophyiscal Processor System (RGPS) Products over the SHEBA Ice Camp. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada621251.

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Coverdell, B. L. Analysis of the Retained Gas Sample (RGS) Extruder Assembly. Office of Scientific and Technical Information (OSTI), 1995. http://dx.doi.org/10.2172/273634.

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Liu, Shuang. Novel Approach to Prepare {sup 99m}Tc-Based Multivalent RGD Peptides. Office of Scientific and Technical Information (OSTI), 2012. http://dx.doi.org/10.2172/1053772.

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