Surface Markers of Fibrinogen and Its Physiologic Derivatives Revealed by Antibody Probes

Plow, Edward F.; Edgington, Thomas S.

doi:10.1055/s-2007-1005041

Cited by 39 publications

(13 citation statements)

References 77 publications

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“…Antibodies raised against site (epitope) y 385-410 interact with the intact fibrinogen molecule suggesting that this epitope is exposed. [66][67] For the above reasons we decided to compare effect of Fragments D, and D, on the fibrinogen-induced aggregation and on binding of lzSI-fibrinogen to chymotrypsin-treated platelets (FIG. 4 a,b) .…”

Section: -Fibrinoqen Addedmentioning

confidence: 99%

Fibrinogen Interaction With Platelet Receptors*†

Niewiarowski

Kornecki

Budzynski

et al. 1983

Annals of the New York Academy of Sciences

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In summary: Incubation of platelets with ADP or proteolytic enzymes (chymotrypsin or pronase) results in an exposure of two classes of specific binding sites on platelet surface: low and high affinity fibrinogen receptors. Fibrinogen interaction with these receptors results in platelet aggregation. High affinity fibrinogen receptors are not exposed on thrombasthenic platelets stimulated by ADP but are rendered available on chymotrypsin-treated thrombasthenic platelets; low affinity receptors cannot be exposed by ADP or chymotrypsin on these platelets. Availability of high affinity fibrinogen receptors on thrombasthenic platelets may depend on the residual glycoprotein IIIa. Fibrinogen receptors appear to be associated with glycoproteins IIb, IIIa and a 66,000 Mr platelet membrane component that is exposed during proteolysis of platelet membranes. Some of the platelet-binding sites on the fibrinogen molecule appear to be associated with the COOH-terminal portion of the gamma chain (gamma 374-411). Additional binding sites may also be located in the COOH-terminal portion of the A alpha chain. The conformation of the fibrinogen molecule may be important in its interaction with platelets. Platelet aggregation may result from bridging platelets by fibrinogen molecule in the presence of bivalent cations. In conclusion, platelet interaction with fibrinogen is a complex process involving different binding sites of the fibrinogen molecule. Our own data and review of literature suggest that platelet-interaction with fibrinogen is of major significance in hemostasis.

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Section: -Fibrinoqen Addedmentioning

confidence: 99%

Fibrinogen Interaction With Platelet Receptors*†

Niewiarowski

Kornecki

Budzynski

et al. 1983

Annals of the New York Academy of Sciences

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“…plasma or serum have been reported (Budzyski et al, 1979;Plow & Edgington, 1982;Walenga et (11, 1983). However, these methods are not suited to the rapid screening of large numbers of samples.…”

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confidence: 99%

Serum crosslinked fibrin (XDP) and fibrinogen/fibrin degradation products (FDP) in disorders associated with activation of the coagulation or fibrinolytic systems

et al. 1985

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Soluble crosslinked fibrin derivatives (XDP) in serum were determined by enzyme immunoassay utilizing monoclonal antibodies and compared with serum fibrinogen/fibrin degradation products (FDP) assayed by conventional techniques. In healthy subjects and patients with miscellaneous disorders not usually associated with activation of the haemostasis mechanism, mean XDP levels were 45 and 70 ng/ml respectively. However, elevated levels of XDP occurred in conditions commonly associated with intravascular and possibly extravascular activation of the coagulation system. Markedly raised mean XDP values (677-6900 ng/ml) occurred in treated pulmonary embolism, disseminated neoplasia, severe inflammatory disorders and complicated postoperative states, and lesser but significant elevation (mean 150-400 ng/ml) in treated venous thrombosis, uneventful postsurgical states, localized neoplasia, liver disease and symptomatic arterial disease. Levels during initial streptokinase therapy (mean 24 000 ng/ml) fell tenfold as treatment was continued. The degree of XDP elevation over normal values was significantly higher than that of FDP in conditions with a propensity for venous thrombosis (post-operative states, disseminated neoplasia and inflammatory diseases) than in liver disease, localized neoplasia or patients receiving heparin therapy for venous thromboembolism.

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“…The specificity of NIBn 178 was unusual in that, while it showed a high affinity for X-oligomers. it also exhibited a much weaker a n i t y for fibrinogen but did not bind to fibrin fragments X. Y, D, E or DD-E. Fragment X differs from fibrinogen in that the former lacks the C-terminal portion of the Aa-chains (Gaffney & Dobos, 1971;Plow & Edgington, 1982). However, the same C-terminal sequence is also missing from the a-chains of the X-oligomers and therefore cannot contain the binding site for NIBn 178.…”

Section: Discussionmentioning

confidence: 97%

Monoclonal antibodies to crosslinked fibrin degradation products (XL‐FDP) I. CHARACTERIZATION AND PRELIMINARY EVALUATION IN PLASMA

et al. 1988

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Monoclonal antibodies (mabs) were raised against X-oligomers, the earliest soluble fragments released from crosslinked fibrin (XL-FN), by the action of plasmin. Two of the mabs (NIBn 52 and NIBn 123) were monospecific for X-oligomers in that they showed no binding to fibrinogen, the plasmic fragments of fibrinogen (D and E) and non-crosslinked fibrin (X, Y, D and E), or the terminal digestion product of XL-FN, fragment DD-E. One other mab (NIBn 178) was panspecific for X-oligomers in that it exhibited a weak affinity for fibrinogen. The mabs were used to develop a two-site immunoradiometric assay (IRMA) and an enzyme-linked immunospecific assay (ELISA) which permitted the specific measurement of X-oligomers directly in plasma, rather than in serum. This immunoassay is a true assay of fibrinolysis as distinct from fibrinogenolysis and may be a potential aid in the diagnosis and evaluation of thrombosis. In preliminary studies, the assay detected low levels of X-oligomers in normal plasma and elevated levels in patients with disseminated intravascular coagulation.

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Surface Markers of Fibrinogen and Its Physiologic Derivatives Revealed by Antibody Probes

Cited by 39 publications

References 77 publications

Fibrinogen Interaction With Platelet Receptors*†

Fibrinogen Interaction With Platelet Receptors*†

Serum crosslinked fibrin (XDP) and fibrinogen/fibrin degradation products (FDP) in disorders associated with activation of the coagulation or fibrinolytic systems

Monoclonal antibodies to crosslinked fibrin degradation products (XL‐FDP) I. CHARACTERIZATION AND PRELIMINARY EVALUATION IN PLASMA

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