Academic literature on the topic 'Adhesion receptors; Glycoproteins'
Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles
Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Adhesion receptors; Glycoproteins.'
Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.
You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.
Journal articles on the topic "Adhesion receptors; Glycoproteins"
1
Ruhl, Stefan, John O. Cisar, and Ann L. Sandberg. "Identification of Polymorphonuclear Leukocyte and HL-60 Cell Receptors for Adhesins of Streptococcus gordonii and Actinomyces naeslundii." Infection and Immunity 68, no. 11 (November 1, 2000): 6346–54. http://dx.doi.org/10.1128/iai.68.11.6346-6354.2000.
Full textAbstract:
ABSTRACT Interactions of oral streptococci and actinomyces with polymorphonuclear leukocytes (PMNs), mediated by sialic acid- and Gal/GalNAc-reactive adhesins, respectively, result in activation of the PMNs and thereby may contribute to the initiation of oral inflammation. Sialidase treatment of PMNs or HL-60 cells abolished adhesion ofStreptococcus gordonii but was required for adhesion ofActinomyces naeslundii. The same effects of sialidase were noted for adhesion of these bacteria to a major 150-kDa surface glycoprotein of either PMNs or undifferentiated HL-60 cells and to a 130-kDa surface glycoprotein of differentiated HL-60 cells. These glycoproteins were both identified as leukosialin (CD43) by immunoprecipitation with a specific monoclonal antibody (MAb). Adhesion of streptococci and actinomyces to a 200-kDa minor PMN surface glycoprotein was also detected by bacterial overlay of untreated and sialidase-treated nitrocellulose transfers, respectively. This glycoprotein was identified as leukocyte common antigen (CD45) by immunoprecipitation with a specific MAb. CD43 and CD45 both possess extracellular mucinlike domains in addition to intracellular domains that are implicated in signal transduction. Consequently, the interactions of streptococci and actinomyces with the mucinlike domains of these mammalian cell surface glycoproteins result not only in adhesion but, in addition, may represent the initial step in PMN activation by these bacteria.
2
Norris, W. E. "Evidence for a second class of membrane glycoprotein involved in cell adhesion." Journal of Cell Science 93, no. 4 (August 1, 1989): 631–40. http://dx.doi.org/10.1242/jcs.93.4.631.
Full textAbstract:
It is believed that transmembrane relationships exist between the cytoskeleton and the extracellular matrix through integral membrane proteins, almost certainly glycoproteins, which would act as transmembrane receptors. Such receptors would include those involved in cell adhesion. I have been able to isolate a detergent-soluble fraction from chick embryo fibroblasts that is enriched in these integral membrane proteins by making use of their amphipathic character to phase-separate them in the detergent Triton X-114. Antisera raised to this fraction had biological activities interfering with cell adhesion and motility. A 45 X 10(3) Mr glycoprotein unique to this fraction appears to be responsible for this biological activity and is a candidate for a transmembrane receptor involved in cell adhesion.
3
Watson, Steve. "Collagen Receptor Signaling in Platelets and Megakaryocytes." Thrombosis and Haemostasis 82, no. 08 (1999): 365–76. http://dx.doi.org/10.1055/s-0037-1615855.
Full textAbstract:
IntroductionThe extracellular matrix protein, collagen, plays a primary role in hemostasis. Collagen fibers provide an important site for adhesion of platelets to the exposed subendothelium, trapping them at the site of vascular damage and enabling the formation of a monolayer of cells over the damaged area. Collagen fibers also stimulate platelet activation, leading to inside-out regulation of the integrin glycoprotein (GP) IIb-IIIa (also known as αIIbβ3), secretion from dense and α granules, generation of thromboxanes, and expression of procoagulant activity, all of which support the hemostatic process. The role of collagen in supporting platelet adhesion to the subendothelium is mediated through indirect and direct interactions. The indirect interaction is mediated through von Willebrand factor (vWF), which binds to the GP Ib-IX-V complex on the platelet surface.1-3 The interaction with vWF is critical for platelet adhesion at medium to high rates of flow because of the fast rate of association between vWF and GP Ib-IX. The importance of this interaction is demonstrated by the severe bleeding problems experienced by individuals with functional impairment of vWF (von Willebrand disease) or GP Ib-IX (Bernard-Soulier syndrome). At low rates of flow, collagen fibers are able to support adhesion in the absence of vWF through a direct interaction with a number of platelet surface glycoproteins i.e. collagen receptors,4,5 this also serves to support vWF-dependent adhesion at higher rates of flow by preventing dissociation. Crosslinking of platelet surface glycoproteins by collagen also generates intracellular signals, leading to platelet activation.The number of proteins on the platelet surface proposed to be collagen receptors is approaching double figures, but it is generally accepted that the integrin GP Ia-IIa (also known as α2β1) and glycoprotein VI (GP VI) are among the most important of these, playing critical roles in adhesion and activation, respectively6 (Fig. 1). This is illustrated by the mild bleeding problems of patients with a low level of expression or the presence of autoantibodies to GP Ia-IIa and the spontaneous, severe bleeding episodes that are occasionally seen in patients whose platelets are deficient in GP VI.6 There is evidence, however, that other collagen receptors have supporting roles in adhesion and activation. For example, GP VI supports platelet adhesion to collagen7 and GP IV, also known as CD36, may also play a similar role.8 The role of the recently cloned collagen receptor p65 in adhesion is not known. Evidence that the interaction of collagen with receptors, such as GPIV and p65, is of less importance than for interactions with GP Ia-IIa, and GP VI is provided by the absence of individuals with bleeding problems caused by deficiencies in these proteins. This is illustrated most clearly for GP IV, which is absent in 3% to 5 % of the Japanese population, and yet such individuals display no major vascular problems.Due to the large number of glycoproteins that bind collagen on the platelet surface, it has been difficult to gain a full understanding of the role of individual collagen receptors in adhesion and activation responses. This is complicated further by the interactions between vWF and GP Ib-IX-V, vWF or fibrinogen to activated GP IIb-IIIa especially as both glycoprotein receptors generate intracellular signals. The relative importance of individual collagen receptors in adhesion also varies with the rate of flow and between collagen types. A full discussion of platelet adhesion to collagen is beyond the scope of this article, and the reader is referred to a number of excellent recent reviews for further information.4-6,9,10 The present chapter focuses on the signaling events generated by the activation (or more correctly crosslinking) of platelet surface glycoproteins by collagen and the implications that this has for platelet activation under normal and diseased conditions.
4
Rahman, Shah, Mairaj Ansari, Pratibha Gaur, Imtiyaz Ahmad, Chandrani Chakravarty, Dileep Verma, Anshika Sharma, et al. "The Immunomodulatory CEA Cell Adhesion Molecule 6 (CEACAM6/CD66c) Is a Protein Receptor for the Influenza A Virus." Viruses 13, no. 5 (April 21, 2021): 726. http://dx.doi.org/10.3390/v13050726.
Full textAbstract:
To establish a productive infection in host cells, viruses often use one or multiple host membrane glycoproteins as their receptors. For Influenza A virus (IAV) such a glycoprotein receptor has not been described, to date. Here we show that IAV is using the host membrane glycoprotein CD66c as a receptor for entry into human epithelial lung cells. Neuraminidase (NA), a viral spike protein, binds to CD66c on the cell surface during IAV entry into the host cells. Lung cells overexpressing CD66c showed an increase in virus binding and subsequent entry into the cell. Upon comparison, CD66c demonstrated higher binding capacity than other membrane glycoproteins (EGFR and DC-SIGN) reported earlier to facilitate IAV entry into host cells. siRNA mediated knockdown of CD66c from lung cells inhibited virus binding on cell surface and entry into cells. Blocking CD66c by antibody on the cell surface resulted in decreased virus entry. We found that CD66c is a specific glycoprotein receptor for influenza A virus that did not affect entry of non-IAV RNA virus (Hepatitis C virus). Finally, IAV pre-incubated with recombinant CD66c protein when administered intranasally in mice showed decreased cytopathic effects in mice lungs. This publication is the first to report CD66c (Carcinoembryonic cell adhesion molecule 6 or CEACAM6) as a glycoprotein receptor for Influenza A virus.
5
Luzak, Boguslawa, Jacek Golanski, Marcin Rozalski, Magdalena A. Boncler, and Cezary Watala. "Inhibition of collagen-induced platelet reactivity by DGEA peptide." Acta Biochimica Polonica 50, no. 4 (December 31, 2003): 1119–28. http://dx.doi.org/10.18388/abp.2003_3636.
Full textAbstract:
Direct interactions between collagen, the most thrombogenic component of the extracellular matrix, and platelet surface membrane receptors mediate platelet adhesion and induce platelet activation and aggregation. In this process two glycoproteins are crucial: integrin alpha2beta1, an adhesive receptor, and GPVI, which is especially responsible for signal transduction. Specific antagonists of the collagen receptors are useful tools for investigating the complexity of platelet-collagen interactions. In this work we assessed the usefulness of DGEA peptide (Asp-Gly-Glu-Ala), the shortest collagen type I-derived motif recognised by the collagen-binding integrin alpha2beta1, as a potential antagonist of collagen receptors. We examined platelet function using several methods including platelet adhesion under static conditions, platelet function analyser PFA-100TM, whole blood electric impedance aggregometry (WBEA) and flow cytometry. We found that DGEA significantly inhibited adhesion, aggregation and release reaction of collagen activated blood platelets. The inhibitory effect of DGEA on static platelet adhesion reached sub-maximal values at millimolar inhibitor concentrations, whereas the specific blocker of alpha2beta1 - monoclonal antibodies Gi9, when used at saturating concentrations, had only a moderate inhibitory effect on platelet adhesion. Considering that 25-30% of total collagen binding to alpha2beta1 is specific, we conclude that DGEA is a strong antagonist interfering with a variety of collagen-platelet interactions, and it can be recognised not only by the primary platelet adhesion receptor alpha2beta1 but also by other collagen receptors.
6
Vainionpää, Noora, Yamato Kikkawa, Kari Lounatmaa, Jeffrey H. Miner, Patricia Rousselle, and Ismo Virtanen. "Laminin-10 and Lutheran blood group glycoproteins in adhesion of human endothelial cells." American Journal of Physiology-Cell Physiology 290, no. 3 (March 2006): C764—C775. http://dx.doi.org/10.1152/ajpcell.00285.2005.
Full textAbstract:
Laminin α5-chain, a constituent of laminins-10 and -11, is expressed in endothelial basement membranes. In this study we evaluated the roles of α5 laminins and Lutheran blood group glycoproteins (Lu), recently identified receptors of the laminin α5-chain, in the adhesion of human dermal microvascular and pulmonary artery endothelial cells. Field emission scanning electron microscopy and immunohistochemistry showed that the endothelial cells spread on laminin-10 and formed fibronectin-positive fibrillar adhesion structures. Immunoprecipitation results suggested that the cells produced fibronectin, which they could use as adhesion substratum, during the adhesion process. When the protein synthesis during the adhesion was inhibited with cycloheximide, the formation of fibrillar adhesions on laminin-10 was abolished, suggesting that laminin-10 does not stimulate the formation of any adhesion structures. Northern and Western blot analyses showed that the cells expressed Mr78,000 and 85,000 isoforms of Lu. Quantitative cell adhesion assays showed that in the endothelial cell adhesion to laminin-10, Lu acted in concert with integrins β1and αvβ3, whereas in the adhesion to laminin-10/11, Lu and integrin β1were involved. In the cells adhering to the α5 laminins, Lu and the integrins showed uniform cell surface distribution. These findings indicate that α5 laminins stimulate endothelial cell adhesion but not the formation of fibrillar or focal adhesions. Lu mediates the adhesion of human endothelial cells to α5 laminins in collaboration with integrins β1and αvβ3.
7
Law, Debbie, Lisa Nannizzi-Alaimo, Kyra Cowan, K. S. Srinivasa Prasad, Vanitha Ramakrishnan, and David Phillips. "Signal Transduction Pathways for Mouse Platelet Membrane Adhesion Receptors." Thrombosis and Haemostasis 82, no. 08 (1999): 345–52. http://dx.doi.org/10.1055/s-0037-1615852.
Full textAbstract:
IntroductionThe study of genetic bleeding disorders provided the first link between platelet functions and specific membrane glycoproteins. Two examples are well known and have been the subject of numerous reviews. First, Glanzmann’s thrombasthenia is a bleeding disorder caused by a defect of platelet aggregation in which the glycoprotein αIIbβ3 (GP IIb-IIIa) is either lacking or is expressed but is defective.1 We now know that αIIbβ3 exists on the surface of unstimulated platelets in an inactive form but, through a process known as “inside-out” signaling, responds to platelet stimulation to become a receptor for soluble fibrinogen and von Willebrand factor (vWF) to mediate platelet aggregation. αIIbβ3 is also known to bind immobilized fibrinogen and, through a process known as “outside-in” signaling, to induce platelet stimulation.2 A second example is Bernard-Soulier syndrome, a bleeding disorder caused by the failure of platelets to bind to subendothelial matrices due to the lack of or defective GP Ib-IX-V.3 It is now known that GP Ib-IX-V binds to vWF to mediate the adhesion of unstimulated platelets to injured blood vessel walls.4,5 GP Ib-IX-V interactions also induce platelet stimulation, a process mediated by signaling through GP Ib-IX-V.6 The mechanisms responsible for the binding of adhesive proteins to αIIbβ3 and GP Ib-IX-V are beginning to be understood and, as such, targets for therapeutic intervention have been identified. Three parenteral αIIbβ3 antagonists have demonstrated a therapeutic benefit in large-scale clinical trials of acute coronary syndromes, including unstable angina, non Q-wave myocardial infarction, and percutaneous intervention, and are now commercially available.7 Many orally available αIIbβ3 antagonists are presently in clinical trials. Although GP Ib antagonists have not been pursued as aggressively, animal studies have shown that they do have a proven antithrombotic benefit.8 Despite these advances in the understanding of glycoprotein ligand binding and development of therapeutic antagonists of adhesive protein receptors, the mechanisms responsible for transducing signals through these receptors have remained elusive.It is now established that signal transduction reactions through αIIbβ3 and GP Ib-IX-V are not only involved in platelet aggregation to cause vessel occlusions, but also that glycoprotein signaling affects thrombus growth and stability, as well as the biology and perhaps the pathology of the vessels in which aggregates occur. In one example, platelet-derived growth factor (PDGF), secreted in response to αIIbβ3 signaling from the α-granules of aggregated platelets, is a primary smooth muscle cell mitogen and is believed to be involved not only in the response to vascular injury but also in atherosclerotic lesion progression.9,10 In another example, CD 154 (previously termed CD40 ligand) redistributes from α-granule membranes to the surface of aggregated platelets in response to αIIbβ3 signaling.11 CD 154 is an important inflammatory mediator that induces the release of cytokines from endothelial and smooth muscle cells, initiates vascular inflammation, and participates in atherosclerotic lesion progression.12 A third example involves the assembly of prothrombinase and factor Xase on the surface of aggregated platelets, enabling platelet thrombi to be procoagulant and accounting for the apparent anticoagulant activity of αIIbβ3 antagonists.13,14 In addition, platelet aggregates also display fibrinogen and vWF bound to platelet membrane glycoproteins that function to recruit additional platelets and, therefore, enhance thrombus growth.15 More recent data also indicate that platelet aggregation induces de novo protein synthesis.16,17 These and other events are secondary to the initial adhesion and aggregation reactions of platelets and are consequences of signaling reactions induced by the adhesion and aggregation receptors. Thus, characterization of the membrane glycoprotein signal transduction pathways has become essential, not only to understand platelet function, but also to determine whether there are additional ways by which platelet-mediated pathologies can be regulated.Platelet membrane glycoprotein signaling reactions either do not occur in nucleated cells normally used for transfection studies or are insufficiently characterized. Accordingly, the use of genetics to study mechanisms of platelet adhesive protein receptor signaling has been limited. The advent of technologies that facilitate genetic manipulations in the mouse genome has produced new ways to define protein function and determine the structure-function relationships of individual proteins and is proving of value in unraveling signal transduction pathways in platelets. Although one should always be cautious in extrapolating data from mouse to human platelets (as demonstrated by the PAR receptors, see below), it is impressive that much of what has been learned about platelets appears to apply to both mouse and human. Indeed, this review summarizes the status of genetic manipulations of the mouse genome that have contributed to our understanding of platelet membrane adhesion receptor signaling in platelets.
8
Wayner, E. A., W. G. Carter, R. S. Piotrowicz, and T. J. Kunicki. "The function of multiple extracellular matrix receptors in mediating cell adhesion to extracellular matrix: preparation of monoclonal antibodies to the fibronectin receptor that specifically inhibit cell adhesion to fibronectin and react with platelet glycoproteins Ic-IIa." Journal of Cell Biology 107, no. 5 (November 1, 1988): 1881–91. http://dx.doi.org/10.1083/jcb.107.5.1881.
Full textAbstract:
We have identified monoclonal antibodies that inhibit human cell adhesion to collagen (P1H5), fibronectin (P1F8 or P1D6), and collagen and fibronectin (P1B5) that react with a family of structurally similar glycoproteins referred to as extracellular matrix receptors (ECMRs) II, VI, and I, respectively. Each member of this family contains a unique alpha subunit, recognized by the antibodies, and a common beta subunit, each of approximately 140 kD. We show here that ECMR VI is identical to the fibronectin receptor (FNR), very late antigen (VLA) 5, and platelet glycoproteins Ic-IIa and shall be referred to as FNR. Monoclonal antibodies to FNR inhibit lymphocyte, fibroblast, and platelet adhesion to fibronectin-coated surfaces. ECMRs I, II, and FNR were differentially expressed in platelets, resting or activated lymphocytes, and myeloid, epithelial, endothelial, and fibroblast cell populations, suggesting a functional role for the receptors in vascular emigration and selective tissue localization. Tissue staining of human fetal skin localized ECMRs I and II to the basal epidermis primarily, while monoclonal antibodies to the FNR stained both the dermis and epidermis. Experiments carried out to investigate the functional roles of these receptors in mediating cell adhesion to complex extracellular matrix (ECM) produced by cells in culture revealed that complete inhibition of cell adhesion to ECM required antibodies to both the FNR and ECMR II, the collagen adhesion receptor. These results show that multiple ECMRs function in combination to mediate cell adhesion to complex EMC templates and predicts that variation in ECM composition and ECMR expression may direct cell localization to specific tissue domains.
9
Doig, Peter, William Paranchych, Parimi A. Sastry, and Randall T. Irvin. "Human buccal epithelial cell receptors of Pseudomonas aeruginosa: identification of glycoproteins with pilus binding activity." Canadian Journal of Microbiology 35, no. 12 (December 1, 1989): 1141–45. http://dx.doi.org/10.1139/m89-189.
Full textAbstract:
Adherence of Pseudomonas aeruginosa to a patient's epithelial surface is thought to be an important first step in the infection process. Pseudomonas aeruginosa is capable of attaching to epithelial cells via its pili, yet little is known about the epithelial receptors of this adhesin. Using nitrocellulose replicas of polyacrylamide gels of solubilized human buccal epithelial cells (BECs), glycoproteins (Mz: 82 000, and four bands between 40 000 and 50 000) that bound purified pili from P. aeruginosa strain K (PAK) were identified by immunoblotting with a pilus-specific monoclonal antibody that does not affect pilus binding to BECs (PK3B). All pilus-binding glycoproteins were surface localized, as determined by surface radioiodination of intact BECs. Binding of pili to all of the glycoproteins was inhibited by Fab fragments of monoclonal antibody PK99H, which inhibits PAK pili binding to BECs by binding to or near the binding domain of the pilus, but not by Fab fragments of monoclonal antibody PK41C, which binds to PAK pilin but does not inhibit pili binding to BECs, demonstrating that pilus binding to these glycoproteins is likely via the same region of the pilus that binds to intact BECs. Periodate oxidation of the blot eliminated pili binding to all glycoproteins, indicating that a carbohydrate moiety is an important determinant for pilus-binding activity. However, not all of the glycoproteins exhibited the same degree of sensitivity to periodate oxidation. Furthermore, monosaccharide inhibition of pilus binding to BECs implicated L-fucose and N-acetylneuraminic acid as receptor moieties.Key words: Pseudomonas aeruginosa, pili, receptor, adhesion.
10
Brown, M. J., and L. M. Loew. "Electric field-directed fibroblast locomotion involves cell surface molecular reorganization and is calcium independent." Journal of Cell Biology 127, no. 1 (October 1, 1994): 117–28. http://dx.doi.org/10.1083/jcb.127.1.117.
Full textAbstract:
Directional cellular locomotion is thought to involve localized intracellular calcium changes and the lateral transport of cell surface molecules. We have examined the roles of both calcium and cell surface glycoprotein redistribution in the directional migration of two murine fibroblastic cell lines, NIH 3T3 and SV101. These cell types exhibit persistent, cathode directed motility when exposed to direct current electric fields. Using time lapse phase contrast microscopy and image analysis, we have determined that electric field-directed locomotion in each cell type is a calcium independent process. Both exhibit cathode directed motility in the absence of extracellular calcium, and electric fields cause no detectable elevations or gradients of cytosolic free calcium. We find evidence suggesting that galvanotaxis in these cells involves the lateral redistribution of plasma membrane glycoproteins. Electric fields cause the lateral migration of plasma membrane concanavalin A receptors toward the cathode in both NIH 3T3 and SV101 fibroblasts. Exposure of directionally migrating cells to Con A inhibits the normal change of cell direction following a reversal of electric field polarity. Additionally, when cells are plated on Con A-coated substrata so that Con A receptors mediate cell-substratum adhesion, cathode-directed locomotion and a cathodal accumulation of Con A receptors are observed. Immunofluorescent labeling of the fibronectin receptor in NIH 3T3 fibroblasts suggests the recruitment of integrins from large clusters to form a more diffuse distribution toward the cathode in field-treated cells. Our results indicate that the mechanism of electric field directed locomotion in NIH 3T3 and SV101 fibroblasts involves the lateral redistribution of plasma membrane glycoproteins involved in cell-substratum adhesion.
Dissertations / Theses on the topic "Adhesion receptors; Glycoproteins"
1
Hyland, Robert H. "Heterodimer formation and activation of the leukocyte integrins." Thesis, University of Oxford, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.365411.
Full text
2
Andrieux, Annie. "Diversité structurale et fonctionnelle des cytoadhésines cellulaires." Grenoble 1, 1988. http://www.theses.fr/1988GRE10054.
Full textBooks on the topic "Adhesion receptors; Glycoproteins"
1
Barros, Rodrigo José Saraiva de, Tereza Cristina de Brito Azevedo, Carla de Castro Sant’Anna, Marianne Rodrigues Fernandes, Leticia Martins Lamarão, and Rommel Mario Rodríguez Burbano. Grupos sanguíneos e anticorpos anti-eritrocitários de importância transfusional. Brazil Publishing, 2020. http://dx.doi.org/10.31012/978-65-5861-112-7.
Full textAbstract:
Immunohematology is an area dedicated to the study of the interactions of the immune system and blood cells in transfusion practice. Blood transfusion is a therapeutic technique that has been widely used since the 17th century. The transfusion medicine aims to repair the pathological needs of blood components in the living organism, be it red blood cells, plasma, platelets, clotting factors, among others. Despite being a therapeutic means, transfusion of blood components can be considered at risk because it is a biological material and due to the transfusion immunological reactions that can be caused during or after the moment of transfusion. In the surface structure of red blood cells, numerous molecules of a protein, glycoprotein or glycolipid nature are found, which are also called membrane antigens that make up structures and perform transport functions, as receptors, as adhesion, enzymatic and / or complement regulatory molecules. The formation of these antigens occurs by an approximate amount of 39 genes involved in their production, of which 282 different antigens are organized in more than 30 blood group systems. This antigenic diversity is a major cause of the formation of irregular anti-erythrocyte antibodies. Therefore, with the increase in blood transfusions in surgeries, transplants and clinical treatment of cancer and other chronic diseases, a significant increase in the occurrence of alloimmunizations in polytransfused patients began to be observed. Such biological phenomena motivated us to carry out this study and the antigenic diversity motivated us to elaborate this small compendium where we also describe the main blood groups.
Book chapters on the topic "Adhesion receptors; Glycoproteins"
1
Holmes, Kathryn V., and Richard K. Williams. "Characterization and Expression of the Glycoprotein Receptor for Murine Coronavirus." In Microbial Adhesion and Invasion, 69–76. New York, NY: Springer New York, 1992. http://dx.doi.org/10.1007/978-1-4612-2924-7_6.
Full text
2
Calvete, Juan José. "Elements for a Structural/Functional Model of Human Platelet Plasma Membrane Fibrinogen Receptor, the Glycoprotein IIb/IIIa Complex (Integrin αIIb/β3)." In Cell Adhesion Molecules, 63–91. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2830-2_6.
Full text
3
Douville, Philippe, and Salvatore Carbonetto. "Extracellular Matrix Adhesive Glycoproteins and Their Receptors in the Nervous System." In Neurobiology of Glycoconjugates, 383–409. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-5955-6_13.
Full text
4
K. Poddar, Mrinal, and Soumyabrata Banerjee. "Molecular Aspects of Pathophysiology of Platelet Receptors." In Platelets. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.92856.
Full textAbstract:
Receptor is a dynamic instrumental surface protein that helps to interact with specific molecules to respond accordingly. Platelet is the smallest in size among the blood components, but it plays many pivotal roles to maintain hemostasis involving its surface receptors. It (platelet) has cell adhesion receptors (e.g., integrins and glycoproteins), leucine-rich repeats receptors (e.g., TLRs, glycoprotein complex, and MMPs), selectins (e.g., CLEC, P-selectin, and CD), tetraspanins (e.g., CD and LAMP), transmembrane receptors (e.g., purinergic—P2Y and P2X1), prostaglandin receptors (e.g., TxA2, PGH2, and PGI2), immunoglobulin superfamily receptors (e.g., FcRγ and FcεR), etc. on its surface. The platelet receptors (e.g., glycoproteins, protease-activated receptors, and GPCRs) during platelet activation are over expressed and their granule contents are secreted (including neurotransmitters, cytokines, and chemokines) into circulation, which are found to be correlated with different physiological conditions. Interestingly, platelets promote metastasis through circulation protecting from cytolysis and endogenous immune surveillance involving several platelets receptors. The updated knowledge about different types of platelet receptors in all probable aspects, including their inter- and intra-signaling mechanisms, are discussed with respect to not only its (platelets) receptor type but also under different pathophysiological conditions.
5
Clemetson, Kenneth J. "Platelet membrane glycoproteins." In Receptors of Cell Adhesion and Cellular Recognition, 231–67. Elsevier, 1996. http://dx.doi.org/10.1016/s1874-5342(96)80025-0.
Full text
6
Saltzman, W. Mark. "Cell Adhesion." In Tissue Engineering. Oxford University Press, 2004. http://dx.doi.org/10.1093/oso/9780195141306.003.0011.
Full textAbstract:
The external surface of the cell consists of a phospholipid bilayer which carries a carbohydrate-rich coat called the glycocalyx; ionizable groups within the glycocalyx, such as sialic acid (N-acetyl neuraminate), contribute a net negative charge to the cell surface. Many of the carbohydrates that form the glycocalyx are bound to membrane-associated proteins. Each of these components— phospholipid bilayer, carbohydrate-rich coat, membrane-associated protein—has distinct physicochemical characteristics and is abundant. Plasma membranes contain ∼50% protein, ∼45% lipid, and ∼5% carbohydrate by weight. Therefore, each component influences cell interactions with the external environment in important ways. Cells can become attached to surfaces. The surface of interest may be geometrically complex (for example, the surface of another cell, a virus, a fiber, or an irregular object), but this chapter will focus on adhesion between a cell and a planar surface. The consequences of cell–cell adhesion are considered further in Chapter 8 (Cell Aggregation and Tissue Equivalents) and Chapter 9 (Tissue Barriers to Molecular and Cellular Transport). The consequences of cell–substrate adhesion are considered further in Chapter 7 (Cell Migration) and Chapter 12 (Cell Interactions with Polymers). Since the growth and function of many tissue-derived cells required attachment and spreading on a solid substrate, the events surrounding cell adhesion are fundamentally important. In addition, the strength of cell adhesion is an important determinant of the rate of cell migration, the kinetics of cell–cell aggregation, and the magnitude of tissue barriers to cell and molecule transport. Cell adhesion is therefore a major consideration in the development of methods and materials for cell delivery, tissue engineering, and tissue regeneration. The most stable and versatile mechanism for cell adhesion involves the specific association of cell surface glycoproteins, called receptors, and complementary molecules in the extracellular space, called ligands. Ligands may exist freely in the extracellular space, they may be associated with the extracellular matrix, or they may be attached to the surface of another cell. Cell–cell adhesion can occur by homophilic binding of identical receptors on different cells, by heterophilic binding of a receptor to a ligand expressed on the surface of a different cell, or by association of two receptors with an intermediate linker. Cell–matrix adhesion usually occurs by heterophilic binding of a receptor to a ligand attached to an insoluble element of the extracellular matrix.
7
"RODENT CEA-RELATED GLYCOPROTEINS ARE RECEPTORS FOR MURINE CORONAVIRUSES." In Cell Adhesion and Communication Mediated by the CEA Family, 202–19. CRC Press, 1998. http://dx.doi.org/10.1201/9781482283402-16.
Full text
8
Webert, Kathryn E., and John G. Kelton. "Disorders of platelet number and function." In Oxford Textbook of Medicine, 4506–18. Oxford University Press, 2010. http://dx.doi.org/10.1093/med/9780199204854.003.220603.
Full textAbstract:
Platelets are released from megakaryocytes in the bone marrow and circulate for 5 to 10 days before being cleared by the cells of the reticuloendothelial system. They play a critical role in haemostasis, with key features being (1) adhesion—when the wall of a blood vessel is damaged, platelets adhere to exposed collagen and other components of the subendothelium via the glycoprotein Ib receptor and other adhesive receptors; followed by (2) activation—release of thrombin, adenosine diphosphate, and arachidonic acid, which is converted by a cascade of enzymes into platelet activating agents including thromboxane A...
9
Colin Hughes, R. "Adhesive glycoproteins and receptors." In Glycoproteins II, 507–70. Elsevier, 1997. http://dx.doi.org/10.1016/s0167-7306(08)60627-4.
Full text
10
Karim, Zubair A., and Fadi T. Khasawneh. "Platelet Function Disorders." In Emerging Applications, Perspectives, and Discoveries in Cardiovascular Research, 117–37. IGI Global, 2017. http://dx.doi.org/10.4018/978-1-5225-2092-4.ch007.
Full textAbstract:
Platelets play an important role in thrombosis and hemostasis. Moreover, platelet dysfunction due to congenital and acquired etiologies is also one of the most common causes of bleeding encountered in clinical practice. Mostly, platelet function disorders are deficiencies of glycoprotein mediators of adhesion and aggregation, whereas defects of primary receptors for stimuli include those of the P2Y12 ADP receptor. Studies on inherited defects of (1) secretion for storage organelles (dense and alpha-granules), (2) the platelet cytoskeleton, and (3) the generation of pro-coagulant activity have allowed for the identification of genes directly and/or indirectly controlling specific functional responses. This chapter will review recent advances in the molecular characterization of platelet function defects, the spectrum of clinical manifestations of these disorders and their management.
Conference papers on the topic "Adhesion receptors; Glycoproteins"
1
Hawiger, J. "PLATELET RECEPTOR RECOGNITION DOMAINS AND THEIR SYNTHETIC PEPTIDE ANALOGS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643726.
Full textAbstract:
Adhesive molecules and their receptorsplay an essential role in hemostasis and thrombosis. Platelet thrombi are formed through the interaction of cell adhesion molecules (CAMs) with intercellular adhesion molecules (IAMs)and substrate adhesion molecules (SAMs). Platelet CAMs encompass membrane glycoproteins lb, lib, Ilia,and possibly la and IV, which constitutemembrane receptors for IAMs(e.g., fibrinogen) and for SAMs encompassingvon Willebrand Factor (vWF), fibronectin, vitronectin, collagen, and thrcmbospondin. Receptorfunction of platelet CAMs can be specific,i.e., only one adhesive protein among IAMs and SAMs is selected forbinding as exemplified by GPIb and vWF. Alternatively,more than one adhesive protein can interact with platelet CAMs comprising the GPIIb/IIIa complex.This common adhesive receptor mechanism switched on by thrombin, ADP, phorbol ester or ionophore A23187 is turned off by a rise in intraplatelet cyclic AMP which provides a negative control.Fibrinogen, the most abundant adhesiveprotein in plasma, interacts with platelet CAMs via receptor recognition domains on gamma and alpha chains. Pinpointing platelet receptor recognition domain to a carboxy-terminal segment of the gamma chain encompassing residues 400-411gave rise to a series of synthetic peptide analogs which do not interfere with themetabolic pathways of platelets but blockbinding of I fibrinogen to its receptors on stimulated platelets, inhibit their aggregation in vitro, and formation of a platelet thrombus in vivo. The alpha chain of human fibrinogen contains the sequenceRGD (residues 95-97 and 572-574). Synthetpeptide analogs of the RGD sequence, which constitute the "cell adhesion site" of fibronectin, also inhibit binding of 125I-fibrinogen to stimulated platelets. However, these synthetic peptides are not "specific" for fibrinogen chains because thealpha chain of human fibrinogen which hasnosequence homology with gamma 400-411 is prevented by a peptide gamma 400-411 from interaction with platelet receptors. Viceversa, the human gamma chain is blocked by tetrapeptide RGDS not expressed in the human gamma chain. Interaction of human vWF with human platelets is blocked by synthetic peptide analogs of gamma 400-411 (not present in vWF)and of RGD sequence (present in vWF).These synthetic peptides inhibite "common" receptor pathwaystimulated with ADP, thrombin, or phorbolester, but they do not interfere with binding of 125I-vWF via a "specific" pathvoy induced with ristocetin and involving GPIb.The design of synthetic peptide analogs which inhibit platelet receptors for adhesive molecules includes the following considerations: ligand specificity (is thepeptide inhibitory toward binding of one or more adhesive molecules?),cell speciicity (is the peptide specific for platelets or does it perturb the adhesive properties of other cells, e.g.,endothelium?);the hydrophilic character; protection against degradation by peptidases; and a sufficiently long half-life to achieve platelet inhibitory potency in vivo without overloading the blood with excessive amounts of peptide.This is accomplished by constructing a peptide-albumin conjugate with ahalf-life extended at least 30 times.Whenpeptides are modeled with predominantly hydrophilic or hydrophobic residues, only the hydrophilic peptide remained active to block the platelet receptor. This agreed with the general observation that sequences on adhesive molecules that are knownto interact with cellular receptors have a hydrophilic rather than a hydrophobic character. Furthermore, changing the charge of synthetic peptides toward the negative reduced the reactivity, whereas introducing additional arginine residues enhanced the reactivity toward platelet receptors. Localization of the functionally important binding domain in the flexible segment of an adhesive protein increases the likelihood that the synthetic peptide will assume the conformation mimicking such a domain in the native adhesive protein. Structure-function studies of the receptor recognition domains on adhesive molecules led to development of a new class of platelet inhibitors acting at the membranereceptors responsible for anchoring of platelets to the vessel wall and linking them to each other.
2
Altieri, Dario C., Rossella Bader, and Pier M. Mannucci. "STRUCTURAL DIVERSITY AMONG CELLULAR ADHESION RECEPTORS: FIBRINOGEN BINDING IS A NOVEL BIOLOGICAL PROPERTY OF THE MONOCYTE DIFFERENTIATION ANTIGEN OKM1." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643851.
Full textAbstract:
A family of related glycoproteins (GP) mediate the interaction between the circulating adhesive proteins and a variety of cells (cytyoadhesins). In this study we have compared two cell-surface antigens which share the property to bind fibrinogen: the platelet GP IIb/IIIa, prototype of the cytoadhesins, and the receptor for fibrinogen costitutively synthesized by monocytes. Two anti-GP IIb/IIIa monoclonal antibodies (Mabs) (LJP9, LJP5), recognizing functionally distinct epitopes of the GP IIb/IIIa did not react with monocytes nor inhibited 125I-fibrinogen binding to monocytes. Similarly, an Arg-Gly-Asp containing peptide which completely abolished platelet-fibrinogen interaction, had no effect on monocytes. Structurally, the monocyte fibrinogen receptor was dimeric and composed of two subunits with molecular weight (Mr) of 155,000 and 95,000. This structural organization was different from that of the GP IIb/IIIa (Mr= 116,000), but in close analogy with the family of leukocyte differentiation antigens OKM1, LFA-1. Therefore, this possible relationship was investigated. A Mab to OKM1 antigen (10 μg/ml) completely suppressed fibrinogen binding to monocytes while it was ineffective on plateles. Iodinated monocyte lysate subjected to immunoprecipitation with OKM1 Mab (60 μg/ml) showed a dimeric antigen with the same molecular size of the monocyte fibrinogen receptor. Moreover, preclearing of the monocyte lysate with OKM1 Mab removed the immunoprecipitate corresponding to the monocyte fibrinogen receptor. These data indicate that the immunologic differentiation antigen OKM1, in addition to function as a complement receptor, displays also the novel biological adhesion property to mediate the binding of fibrinogen to monocytes.
3
Kantak, Ameya, Yuri Lvov, David K. Mills, James G. Spaulding, and Steven A. Jones. "Platelet Function Assessment in a Microfabricated Device." In ASME 2002 International Mechanical Engineering Congress and Exposition. ASMEDC, 2002. http://dx.doi.org/10.1115/imece2002-33135.
Full textAbstract:
Although platelets are small and simple in shape, they are complicated in their physiologhy. Their alpha granules and dense bodies secrete a large number of agents that are involved in haemostasis, and the glycoproteins on their surfaces form the linkages with proteins like fibrinogen, fibronectin, collagen and von Willebrand factor that are necessary for adhesion and aggregation (Frojmovic, 1998). Diseases such as heart attack (Meade, 1992), stroke (Harker, 1998) and eclampsia (Schindler et al., 1990), can be the result of pathologies in platelets. Although devices have been recently developed to diagnose platelet function (Nicholson et al., 1998), there is still a need for devices that can examine the multiple factors of platelet physiology that affect thrombus formation. Because fluid shear is a key factor in platelet adhesion and aggregation (Colantuoni et al., 1977), it is necessary to test platelet function under conditions of flow. Also, because of the large number of adhesion receptors and secreted agents that make up a platelet’s physiology, a complete diagnosis of platelet function should be performed on a variety of substrates.
4
Sakariassen, S. K., E. Fressinaud, D. Meyer, J. J. Sixma, and R. H. Baumgartner. "RHEOLOGY AND PLATELET-SURFACE ADHESION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643987.
Full textAbstract:
The process of platelet adhesion to sites of vascular injury is pivotal for the arrest of bleeding. The same process may, on the other hand, lead to formation of mural thrombi and may play a role in atherogenesis through the release of platelet-derived growth factor. The events of platelet-surface adhesion may be divided into initial attachment and the subsequent spreading on the surface. These interactions are mediated by a variety of factors, including glycoproteins (GP) in the platelet membrane, von Willebrand factor (vWF) in plasma, and the composition of the surface.However, in most instances their effects on adhesion are dependent on the shear rate.We have investigated the importance of some of these factors in flowing blood at shear rates ranging from those present in large arteries (≃ 200 sec-1) to those present in the microcirculation (≃2600 sec-1). We used annular- and parallel-plate-perfusion chambers with de-endothelial-ized human arteries and collagen-coated surfaces, respectively. A highly reactive surface, such as formed by collagen fibrils, triggers rapid platelet adhesion and thrombus growth on the upstream portion of the surface. This rapid consumption of platelets depletes the boundary layer of the blood flow of platelets, resulting in fewer platelets to adhere further downstream. This effect is most pronounced at shear rates below 650 sec-1, i.e., at conditions with low radial transport of platelets. This phenomenon, apparently physical in nature, we have termed "axial dependence."Deficiency of GPIb results in impaired initial attachment of platelets to subendothelium, a defect which virtually abolishes initial attachment at shear rates above 500 sec-1. However, inhibition of binding of ADP to its putative 100Kd GP receptor by the adenosine analogue 5'-p-fluoro-sulfonyl-adenosine completely prevents initial attachment of platelets. Conversely, deficiency of GPIIb/IIIa results in partially impaired platelet spreading (20-50%), but only at shear rates above 1000 sec-1; deficiency of GPIa results in no platelet spreading, independent of the shear rate. The importance of GPIb and GPIIb/IIIa in adhesion was further demonstrated by experiments using monoclonal antibodies to either GPIb or GPIIb/IIIa.Addition of these antibodies to blood from healthy subjects duplicates the effects found in the natural deficiency states. Furthermore, we used two monoclonal antibodies to vWF, which specifically inhibit either ristocetin-induced binding of vWF to GPIb or thrombin/ADP-induced binding of vWF to GPIIb/IIIa. Each of these antibodies inhibits ≃ 90% of adhesion at 2600 sec-1 shear rate, while no effect is seen at 650 sec-1. Inhibition of binding of vWF, fibronectin, and fibrinogen to GPIIb/IIIa by a dodecapeptide of the γ-carboxy terminus of fibrinogen inhibits ≃ 30% of adhesion in normal blood at 2600 sec-1 shear rate. No effect is present at 650 sec-1 shear rate.These experiments indicate that (1) ADP and/or its putative receptor and GPIb are involved in the early phase of adhesion, whereas (2) GPIa and GPIIb/IIIa are involved in the spreading reaction. It is also apparent that (3) GPIb and GPIIb/IIIa act as receptors for vWF in the process of bridging the platelet to sites of vascular injury, and that (4) vWF is required for both initial attachment and spreading. (5) The shear rate has an unambiguous role in these complex interactions and in the "axial dependence" phenomenon.
5
Phillips, David R., Laurence A. Fitzgerald, Leslie V. Parise, and Israel F. Charo. "The Platelet Membrane Glycoprotein IIb-III a Complex: Member of a Superfamily of Adhesive Protein Receptors." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643727.
Full textAbstract:
The glycoprotein (GP) IIb-IIIa complex isthe receptor for fibrinogen,fibronectin and von Willebrand factor on the surface of activated platelets that mediates platelet aggregation.The GP IIb-IIIa complex contains two subunits; an a subunit, GP IIb, and a smaller 8 subunit, GP IIIa. To identify the subunits of GP IIb-IIIa responsible for fibrinogen binding, we examined the ability of purified subunitsto bind to immobilized fibrinogen. Both the GP IIb and the GP III a subunits have fibrinogen binding activity, suggesting that fibrinogen binds to multiple sites onthe GP I Ib-IIIa complex.A GP Ilb-IIIa-like complex has been identified on endothelial cells which is immunoreactive with antibodies raised against platelet GP IIb-III a. This complex binds a similar broadspectrum of adhesive proteins as plateletGP IIb-IIIa and appears to mediate the attachment of endothelial cells to the extracellular matrix. We have established, however, that while GP Ilia in endothelial cells is the same primary translation product as platelet GP Ilia, the endothelialcell "GP lib" is a different, but closely related, protein from platelet GP lib. This close relationship of the receptors on these two cells is reflective of recent observations in several laboratories which have shown that a wide variety of cells contain surface glycoproteins which have structural and functionalsimilarities to the GP IIb-IIIa complexinplatelets and the "GP IIb-IIIa-like" complex in endothelial cells.These glycoproteins, which have been termed "integrins" or "cytoadhesins", are complexes of highly homologous a and 8 subunits, mediate cell-cell or cel 1-substrata interactions, and may also bind the RGD sequence on adhesive proteins. Although in vertebrates this family includes at least ten receptor complexes, there are only three known 8 subunits, each of which defines a subset of receptors. One is GP IIIa, the 8 subunit for GP IIb-IIIa and the vitronectin receptor; another is the 8 subunit for the fibronectin receptors and the very late antigens on lymphocytes; the third is the 8subunit of the Mac-1, LFA-1, and P150/95 antigens on leukocytes. These three 6 subunits have been cloned and sequenced. Each contains 746-777 amino acids, a singletransmembrane domain near the carboxy terminus, 56 cysteines in identical positionsof the proteins, 31 of which are clustered into four repeats, and an overall identity in 45-47% of their amino acids. The asubunits are more diverse in size but appear to have a similar degree of homology.The available sequence information indicates that they contain a single transmembrane domain near their carbody terminii and four tandem repeats near their amino terminii which include sequences indicativeof four Ca2+-binding sites. These may account for the known Ca2+-binding properties of GP IIb. GP I Ib-IIIa and the other adhesive protein receptors therefore appear to have two membrane insertion sites, one on each subunit,with short cytoplasmic domains derived from the carboxy terminii of the two subunits. The amino terminii along with most ofthe mass of these proteins is extracellular. It can be anticipated that the highlyhomologous sequences between GP IIb-IIIa and the other adhesive protein receptors will help identify the functional domainswhich have been conserved since their evolutionary divergences.
6
Polack, B., A. Duperray, and R. Berthier. "PLATELET AND ENDOTHELIAL CELL CYTOADHESINS ARE BIOSYNTHESIZED AND PROCESSED VIA SIMILAR PATHWAYS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642815.
Full textAbstract:
The cytoadhesin family represents a group of heterodimeric adhesion receptors with common structural, fonctional and immunochemical properties. Platelet and endothelial cell (EC) GPIIbIII a related proteins exemplify two members of this family. In the present study the biosynthesis and processing of EC GPIIbIII a were examined and compared with that of platelet GPIIbIIIa to verify whether the diversity of these cytoadhesins was related to post translational events.Endothelial cells of human umbilical cord vein origin were metabolicaly labeled with 35S-methionine. The newly synthesized proteins were analyzed and immunoprecipitated with polyclonal antibodies against the purified platelet GPIIbllla complex and the isolated GPIIb and GPIIIa. Under non-reducing conditions three bands were detected at 135 kD, 125 kD and 90kD with the anti GPIIbIIIa. Samples obtained from pulse chase experiments and analysed under non reducing conditions indicated that the 135 kD band derived from the 125 kD band. Under reducing conditions the 135 kD generated two bands at 118 kD and 25 kD. The 125 KD band also gave a 118 kD band and the 90 kD band shifted to 100 kD. These results indicated that the mature form of 135 kD is composed of two polypeptidic chains which derive from a common single chain precursor similar to that observed in the megakaryocyte. The mature protein and the precursor molecule were not recognised by anti GPIIb antibodies. Also immunoprecipitated by polyclonal anti GPIIIa antibodies was a single chain protein of 100kD. In addition, endoglycosidase treatement showed that both EC GPIIIa and platelet GPIIIa were glycosylated protein of the high mannose type.These results indicate that although structural differences exists between platelet and endothelial cell GPIIbllla, the two membrane glycoproteins have a similar cellular transit.
7
Piotrowicz, Randolph S., Kenneth M. Yamada, and Kunicki J. Kunicki. "HUMAN PLATELET GLYCOPROTEIN Ic-IIa IS AN ACTIVATION-INDEPENDENT FIBRONECTIN RECEPTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643911.
Full textAbstract:
Human platelets express the membrane glycoprotein (GP) heterodimer GPIIb-IIIa, which functions as an activation-dependent fibronectin (Fn) receptor. We have immunopurified the components of an activation-independent Fn receptor (FR) from human platelets employing a well-characterized rabbit polyclonal antibody raised against the beta chain of the chicken embryo fibroblast (CEF) FR (anti-band 3). This antibody crossreacts with antigen(s) expressed on both chicken thrombocytes and human platelets and inhibits the binding of both normal and thrombasthenic platelets (lacking GPIIb-IIIa) to Fn-coated surfaces in the absence of platelet activation.A monoclonal antibody directed against GPIIb-IIIa (AP2) partially inhibits the adhesion of normal platelets to Fn, but the combination of AP2 and anti-band 3 results in a level of inhibition greater than that obtained with either antibody alone. Thus, the presence of the FR alone is sufficient for the observed normal to enhanced binding of thrombasthenic platelets to Fn, whereas adhesion of normal platelets involves the synergistic action of the FR and GPIIb-IIIa. The adhesion of platelets to Fn mediated by the FR is inhibited by the tetrapeptide RGDS.Immunopurified FR appears to be a complex of two proteins: an alpha chain with an apparent molecular weight of 155/130 KD (nonreduced/reduced) and a beta chain with an apparent molecular weight of 125/147 KD. The alpha chain is composed of two subunits, dissociated by reduction, with electrophoretic mobilities identical to platelet glycoproteins previously designated lea and IcB. The beta chain comigrates with that platelet glycoprotein known as GPIIa. In an immunoblot assay, anti-band 3 binds to GPIIa but not to GPIc. The fact that anti-band 3 iramunoprecipitates both GP therefore suggests that they exist in a complex.Our findings establish GPIc-IIa as yet another platelet glycoprotein receptor complex and pave the way for future studies of the relative role of GPIIb-IIIa and GPIc-IIa in the adhesion of platelets to physiologic surfaces.
8
Charo, I. F., L. A. Fitzgerald, D. Meyer, L. S. Bekeart, and D. R. Phillips. "PLATELET GLYCOPROTEIN IIb-IIIa-LIKE PROTEINS MEDIATE ENDOTHELIAL CELL ATTACHMENT TO ADHESIVE MATRIX PROTEINS AND ARE UP-REGULATED BY PHORBOL ESTERS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642816.
Full textAbstract:
Human endothelial cells (EC) express glycoproteins that are similar to the platelet glycoprotein IIb-IIIa complex (GP IIb-IIIa), the platelet receptor for adhesive proteins. Although GP IIb—IIIa is abundant in both platelets and EC, its only known function is to mediate platelet aggregation. The present study tests the hypotheses that EC attachment to adhesive proteins in the extracellular matrix is mediated by the GP IIb-IIIa-1ike proteins. Endothelial cells attached well to glass slides that were previously coated with adhesive proteins, but not albumin. To determine whether GP IIb-IIIa was involved, EC adherence was measured in the presence and absence of a GP IIb-IIIa monoclonal antibody (7E3) which inhibits fibrinogen (Fg) binding to platelets. The attachment of EC to Fg and von Willebrand factor (vWf), but not fibronectin (Fn) coated slides, was completely inhibited by 7E3. Attachment to vitronectin was partially inhibited. In contrast, EC attachment to Fn was specifically inhibited by a Fn-receptor antibody. Endothelial cell adherence to vWf was also inhibited by a monoclonal antibody (Mab9) against the GP IIb-IIIa binding domain of vWf, but not by antibodies agains.t other portions of vWf. We have further found that 7E3 disrupts monolayers of endothelial cells by detaching the cells from their extracellular matrix. EC incubated in phorbol myris-tate.acetate (PMA) increase in size and appear more tightly adherent to their extracellular matrix. To determine if PMA increases synthesis of cellular receptors for matrix proteins, we have used cDNA probes to measure the mRNA levels of the large subunit of the Fn-receptor (FnRα) and GP IIIa in EC. After a 4 hour incubation in the presence of PMA (10 nM), there was a 2-fold increase in the mRNA levels of both FnRα and GP IIIa, as well as increased cell spreading on the matrix. We conclude: i) the GP Ilb-IIIa complex in EC is a surface receptor for specific adhesive proteins, and is distinct from the FnR, and ii) both GP IIIa and FnRα synthesis are increased by PMA, which causes a concomittant change in cell morphology.
9
Feghhi, Shirin, Adam D. Munday, Wes W. Tooley, Jose A. Lopez, and Nathan J. Sniadecki. "E-Beam Nanopost Arrays Reveal That Glycoprotein Ib-IV-X Complex and Von Willebrand Factor Interactions Transmit Platelet Cytoskeletal Forces." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14694.
Full textAbstract:
We have developed a new tool to measure the contractility of single platelets. This tool consists of an array of nano-scale polydimethylsiloxane (PDMS) posts. Von Willebrand factor (VWF) and a recombinant protein encompassing the GPIb-IX-V binding region of VWF (A1 domain) were used to study the role of GPIb-VWF interactions in platelet contractility. Platelets were treated with AK2 and 7E3 antibodies to block platelet adhesion through receptors GPIb and α IIbβ 3, respectively. Platelets treated with these antibodies showed reduced spread area and forces in comparison to untreated platelets on VWF. Furthermore, platelets were able to generate contractile forces on substrates coated with A1 domain of VWF. These results suggest that platelet contractile forces can be transmitted through a non-integrin receptor, such as GPIb.
10
Nachman, R. L., R. L. Silverstein, and A. S. Asch. "THROMBOSPONDIN: CELL BIOLOGY OF AN ADHESIVE GLYCOPROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644653.
Full textAbstract:
Thrombospondin (TSP), a multifunctional 450 KD glycoprotein is a secretory product of thrombin stimulated platelets. It is a major component of the platelets alpha granule constituting approximately 3% of total platelet protein. Thrombospondin does not circulate in appreciable concentrations ∽0 100 ng/ml); however, the tissue distribution is broad. In addition to its expression on the membrane of activated platelets, the protein is synthesized by fibroblasts endothelial cells, glial cell smooth muscle cells alveolar pneumocytes mononuclear phagocytes and various tumor cells. TSP is a major constituent of the extracellular matrix and has been demonstrated in the vessel wall, basement membrane and glandular connective tissue. Fibroblasts, smooth muscle cells and endothelial cells in tissue culture incorporate TSP into the extracellular matrix. Matrix TSP is under cell-cycle regulatory control. Mesenchymal cells in the proliferative phase synthesize greater amounts of TSP than non growing cells. Platelet derived growth factor induces smooth muscle cell and glial cell synthesis of TSP. Atheromatous lesions contain increased amounts of TSP compared to normal vessels emphasizing the potential role of TSP in the interaction of proliferating cells with the matrix. TSP binds specifically, saturably, and reversibly to mouse peritoneal macrophages and to cells of the monocyte-like human cell line U937. Binding was time dependent and was optimal in the presence of both Ca++ and Mg++. PMA stimulated U937 cells and activated macrophages bound TSP to an equivalent extent as resting cells. The TSP binding site on the surface of U937 cells and peripheral blood monocytes mediates the adhesive interaction between these cells and thrombin-stimulated platelets. Using a sensitive rosetting assay we found that monocytes were not rosetted by resting platelets while >90% were rosetted by thrombin-stimulated platelets. Monoclonal and polyclonal anti-TSP antibodies markedly inhibited rosetting as did TSP itself. Antifibronectin or non-immune control antibodies did not inhibit rosetting, nor did fibronectin, fibrinogen, the fibronectinadhesion tetrapeptide arg-gly-asp-ser (RGDS), or heparin. The TSP membrane receptor, an 88 KD glycoprotein, formely known as GPIV has been identified in platelets, endothelial cells, monocytes and a variety of tumor cells. TSP may thus serve as a molecular bridge linking activated platelets with monocytes at sites of early vascular injury. Such interactions involving the TSP receptor complex may be of critical importance in the regulation of thrombosis and the initiation of atherosclerosis.