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1.

001-es BibID:BIBFORM094533
Első szerző:Prodan, Calin I.
Cím:Coated-platelets retain amyloid precursor protein on their surface / Calin I. Prodan, Robert Szasz, Andrea S. Vincent, Elliott D. Ross, George L. Dale
Dátum:2006
ISSN:0953-7104
Megjegyzések:Coated-Platelets are a subset of platelets produced by dual-agonist activation with collagen plus thrombin and are characterized by strong retention of several procoagulant, alpha-granule proteins on the cell surface. In this report we demonstrate that coated-platelets also retain full-length amyloid precursor protein (APP) on their surface in contrast to the cleavage of APP in platelets activated with a single agonist. In addition, western blot analysis indicated that APP is derivatized during coated-platelet synthesis. We subsequently measured coated-platelet production in patients with Alzheimer's disease (AD). Twenty-two AD patients showed a wide distribution of coated-platelet values; however the least impaired AD patients produced coated-platelets at a level significantly above that of aged controls (41.0 +/- 9.9 vs. 28.7 +/- 11.4%; mean +/- 1SD; p = 0.017). These findings suggest that coated-platelets may be a model of aberrant APP processing in early AD patients.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
COAT platelets
amyloid
Megjelenés:Platelets. - 17 : 1 (2006), p. 56-60. -
További szerzők:Szász Róbert (1972-) (belgyógyász, haematológus) Vincent, Andrea S. Ross, Elliott D. Dale, George L.
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2.

001-es BibID:BIBFORM042217
035-os BibID:PMID:15591217
Első szerző:Reményi Gyula (belgyógyász, haematológus)
Cím:Role of mitochondrial permeability transition pore in coated-platelet formation / Gyula Remenyi, Robert Szasz, Paul Friese, George L. Dale
Dátum:2005
ISSN:1079-5642
Megjegyzések:OBJECTIVE:Coated-platelets are a subset of cells observed during costimulation of platelets with collagen and thrombin. Important characteristics of coated-platelets include retention of multiple alpha-granule proteins and expression of phosphatidylserine on the cell surface. The mitochondrial permeability transition pore (MPTP) is a key step in apoptosis and is suggested to be involved in some forms of platelet activation. The objective of this study was to examine the role of MPTP in the synthesis of coated-platelets.METHODS AND RESULTS:Flow cytometric analysis of coated-platelet production was used to examine the impact of pharmacological effectors of MPTP formation. Cyclosporin A, coenzyme Q, and bongkrekic acid all inhibit MPTP formation as well as production of coated-platelets. Phenylarsine oxide and diamide, both potentiators of MPTP formation, stimulate coated-platelet synthesis. Atractyloside, another inducer of MPTP formation, does not affect the percentage of coated-platelets synthesized; however, it does increase the level of phosphatidylserine exposed on the surface of coated-platelets.CONCLUSIONS:These findings indicate that MPTP formation is an integral event in the synthesis of coated-platelets. Although the exact function of the MPTP remains to be determined, these data support a growing body of evidence that apoptosis-associated events are vital components of the platelet activation process. Formation of coated-platelets involves a complex set of activation events initiated by dual agonist activation. The mitochondrial permeability transition pore (MPTP) is a key intermediate in apoptosis and has been suggested to impact platelet activation. This report demonstrates that MPTP formation is essential to production of coated-platelets.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
coated platelet
mitochondrial permeability transition pore
coenzyme Q
phosphatidylserine
cyclosporin A
phenylarsine oxide
diamide
külföldön készült közlemény
Megjelenés:Arteriosclerosis Thrombosis and Vascular Biology. - 25 : 2 (2005), p. 467-471. -
További szerzők:Szász Róbert (1972-) (belgyógyász, haematológus) Friese, Paul Dale, George L.
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3.

001-es BibID:BIBFORM094531
Első szerző:Szász Róbert (belgyógyász, haematológus)
Cím:COAT platelets / Robert Szasz, George L. Dale
Dátum:2003
ISSN:1065-6251
Megjegyzések:Purpose of review: COAT platelets are a recently described subpopulation of cells resulting from simultaneous activation with collagen and thrombin. The complete process by which COAT platelets are produced is still not clear, although significant recent progress has been made. Recent findings: COAT platelets retain several procoagulant proteins on their surface by a previously unrecognized mechanism involving transglutaminase mediated conjugation of serotonin to released alpha-granule proteins. Fibrinogen and thrombospondin have been found to bind serotonin-conjugated proteins and thereby provide the requisite link for stabilization of serotonin-derivatized, procoagulant proteins on COAT platelets. Summary: Multivalent interactions, resulting from traditional receptor interactions and binding of conjugated serotonin by fibrinogen and thrombospondin, result in exceptionally strong retention of procoagulant alpha-granule proteins on the surface of COAT platelets. The physiologic significance of this new subclass of platelets remains to be determined.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
COAT platelets
Megjelenés:Current Opinion in Hematology. - 10 : 5 (2003), p. 351-355. -
További szerzők:Dale, George L.
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4.

001-es BibID:BIBFORM094530
Első szerző:Szász Róbert (belgyógyász, haematológus)
Cím:Thrombospondin and fibrinogen bind serotonin-derivatized proteins on COAT-platelets / Robert Szasz, George L. Dale
Dátum:2002
ISSN:0006-4971
Megjegyzések:Activation of platelets with 2 agonists, collagen and thrombin, reveals a subpopulation of cells referred to as COAT-platelets (collagen and thrombin activated). These cells are enriched in several membrane-bound, procoagulant proteins, including fibrinogen, thrombospondin, factor V, von Willebrand factor, and fibronectin. alpha-Granule proteins bound to COAT-platelets are derivatized with serotonin by a transglutaminase-mediated process, and the interaction of conjugated serotonins with unidentified serotonin binding sites on the platelet surface enhances retention of these proteins. We now demonstrate that both thrombospondin and fibrinogen provide the requisite serotonin binding sites. Thrombospondin and fibrinogen were identified using photoreactive cross-linking to an albumin-(serotonin)(6) conjugate during COAT-platelet production. We subsequently verified that biotin-albumin-(serotonin)(6) binds in vitro to thrombospondin, fibrinogen, and fibrinogen fragment D in a saturable manner. These data support a model for COAT-platelets where serotonin-derivatized procoagulant proteins interact with their respective receptors (eg, fibrinogen with glycoprotein IIb/IIIa or factor V with phosphatidylserine) as well as serotonin binding sites on fibrinogen and thrombospondin, resulting in a stable, multivalent complex on the cell surface.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
COAT platelets
serotonin
platelets
thrombospondin
Megjelenés:Blood. - 100 : 8 (2002), p. 2827-2831. -
További szerzők:Dale, George L.
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Intézményi repozitóriumban (DEA) tárolt változat
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