Monoclonal antibodies against plasminogen and alpha-2-antiplasmin: binding to native and modified antigens

Hattey, E.; Wojta, Johann; Binder, Bernd R.

doi:10.1016/0049-3848(87)90311-2

Cited by 20 publications

(6 citation statements)

References 18 publications

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“…Whilst Pelzer et al (1993) found a mean value of 210 6 88 ng/ml (Enzygnost R PAP, Behringwerke), Hattey et al (1987) established normality under 150 ng/ml (PAP ELISA, Technoclone). 5 6 131 .…”

Section: Discussionmentioning

confidence: 99%

“…Other authors using a variety of assays have found different results. Whilst Pelzer et al (1993) found a mean value of 210 6 88 ng/ml (Enzygnost R PAP, Behringwerke), Hattey et al (1987) established normality under 150 ng/ml (PAP ELISA, Technoclone). Meijer et al (1994) recently obtained a mean concentration of 758 ng/ml by using the PIC test from Teijin Diagnostics and a mean value of 900 6 270 ng/ml was reported by Wiman & Haegerstrand-Björkman (1993) using their own method.…”

Section: Discussionmentioning

confidence: 99%

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Development and clinical application of a new ELISA assay to determine plasmin–α₂‐antiplasmin complexes in plasma

et al. 1996

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Plasmin-2 -antiplasmin complexes (PAP) are considered good markers of fibrinolytic activation in vivo. The presence of neoantigens in these complexes offers the possibility to develop specific immunoassays to determine PAP levels. We have developed a sensitive PAP purification method in vitro by adding urokinase to fresh plasma followed by affinity chromatography to lysine-sepharose and elution with " -aminocaproic acid. This material, characterized by SDS-PAGE and Western blotting, was used to raise monoclonal antibodies (MoAbs). We describe a new enzyme-linked immunosorbent assay (ELISA) to quantify PAP complexes in plasma. The assay follows the sandwich principle and is based on two MoAbs, CPL12 and CPL15, that bind to the modified 2 -antiplasmin moiety and the plasmin moiety of the complex respectively. The calibration curve was constructed with definite concentrations of purified PAP. The lower limit of the assay is 75 ng/ml and the variation coefficients are 3 . 5% (intra-assay) and 10 . 6% (interassay). A mean value of 573 . 5 6 131 . 4 ng/ml was obtained from PAP concentration in a healthy population (n 30). Significantly higher PAP levels were observed under diverse clinical conditions in which fibrinolysis is activated: clinical sepsis, acute myocardial infarction (AMI), malignancy, diabetes, pregnancy, elderly people and thrombolytic therapy. From our results we conclude that this ELISA is suitable to measure in vivo plasma PAP levels.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Development and clinical application of a new ELISA assay to determine plasmin–α₂‐antiplasmin complexes in plasma

et al. 1996

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“…For immunofluorescence studies, the following primary antibodies were used: Leu-M3 (mouse monoclonal anti-CD14, macrophage) (21), rabbit anti-human fibrinogen (Dakopatts, Copenhagen, Denmark), mouse monoclonal Al-3 (anti-human brain TF) (22), rabbit anti-human factor XI11 a chain (Calbiochem, La Jolla, CA) (16), mouse monoclonal anti-guinea pig TTG (23), DD386/22 (mouse monoclonal anti-human fibrin D-dimer) (24), rabbit anti-human uPA and rabbit anti-human tissue PA (tPA; from Dr. H. Berger, Jr., Burroughs Wellcome, Research Triangle Park, NC) (25), and rabbit anti-human a,-PI (American Diagnostica, New York, NY) (26). Secondary antibodies were fluorescein isothiocyanate (F1TC)-conjugated goat anti-mouse immunoglobulin and FITC-conjugated goat anti-rabbit immunoglobulin (Tago, Burlingame, CA).…”

Section: Methodsmentioning

confidence: 99%

Extravascular fibrin formation and dissolution in synovial tissue of patients with osteoarthritis and rheumatoid arthritis

Weinberg

Pippen

Greenberg

1991

Arthritis & Rheumatism

155

122

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Fibrin deposition is a prominent finding in the synovium of patients with rheumatoid arthritis (RA). Macrophages are found in increased numbers in RA synovium, and these cells are known to produce a variety of procoagulant and anticoagulant molecules. Using immunohistologic techniques, the content and distribution of several important components of the coagulation system in the synovium of patients with RA, osteoarthritis (OA), or traumatic joint abnormalities requiring surgery were investigated. Samples from 3 patients from each category were examined in detail. RA synovium (compared with that of patients with OA or joint trauma) had increased numbers of macrophages and increased expression/content of fibrinogen, tissue factor, factor XIII, tissue transglutaminase, cross‐linked fibrin (fibrin D dimer), urokinase‐type plasminogen activator, and α2–plasmin inhibitor. Macrophage content in RA synovium was increased in both the lining cell areas and the interstitial cell areas. Fibrinogen was distributed throughout the tissue in all samples and was greater in RA synovium. In trauma and OA synovia, tissue factor was seen only in association with vessels (endothelial cells), but in RA synovium, it was markedly increased throughout the tissues. While fibrin D dimer was seen in small amounts in synovial lining cell areas of trauma and OA synovia, it was present in increased amounts in the lining cell and interstitial cell areas of RA synovium. Factor XIII and tissue transglutaminase were present in scant amounts in trauma and OA synovia, but there were increased amounts of both (especially tissue transglutaminase) in RA synovium in the vessel, lining cell, and interstitial cell areas. Urokinase and α2–plasmin inhibitor were also markedly increased in RA synovium. These results suggest that in inflamed synovium, there is ongoing extravascular tissue fibrin formation and dissolution that correlates with the degree of inflammation and macrophage content. Extravascular coagulation/fibrinolysis in RA represents a potential target for therapeutic intervention in this disease.

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“…Plasminogen is a multi-domain protein consisting of 5 kringle domains and a serine protease domain. Several antibodies to kringles 1-3 and kringle 4 have been reported, as have antibodies that distinguish Glu-and Lysplasminogens (25,26), and plasmin/a2-antiplasmin complexes. This study is the first report of antibodies mapping to the kringle 5-B chain segment of plasminogen (residues Val442-Asn790).…”

Section: Discussionmentioning

confidence: 97%

Inhibition of Plasminogen Activation by Monoclonal Antibodies to the Kringle 5-B Chain Segment of Human Plasminogen

Church

Messier²

1991

Hybridoma

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Three murine monoclonal antibodies (designated alpha Pg-28, alpha Pg-96, and alpha Pg-247) against human plasminogen were prepared. All three antibodies bound plasminogen and the elastase-digestion product of plasminogen consisting of residues Val442-Asn790 (miniplasminogen). The epitopes recognized by each antibody were distinct. Antibodies alpha Pg-96 and alpha Pg-247 blocked tissue plasminogen activator-dependent lysis in a fibrin plate assay while antibody alpha Pg-28 had no effect. Antibody alpha Pg-96 blocked urokinase- and tissue plasminogen activator-catalyzed, and streptokinase-mediated, plasminogen activation. Antibodies alpha Pg-28 and alpha Pg-247 partially inhibited tissue plasminogen activator-catalyzed plasminogen activation. Antibodies alpha Pg-28 and alpha Pg-247 also inhibited streptokinase-mediated plasminogen activation, but not urokinase-catalyzed activation. Antibody alpha Pg-247 inhibited plasmin catalysis of substrate S-2251 by decreasing the VMAX and increasing the KM of plasmin for the synthetic substrate S-2251 four-fold. The other antibodies had no significant effect on plasmin activity. This differential inhibition of plasminogen activation suggests that activation by urokinase, tissue plasminogen activator, and streptokinase possibly involve distinct regions of miniplasminogen structure.

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Monoclonal antibodies against plasminogen and alpha-2-antiplasmin: binding to native and modified antigens

Cited by 20 publications

References 18 publications

Development and clinical application of a new ELISA assay to determine plasmin–α₂‐antiplasmin complexes in plasma

Development and clinical application of a new ELISA assay to determine plasmin–α₂‐antiplasmin complexes in plasma

Extravascular fibrin formation and dissolution in synovial tissue of patients with osteoarthritis and rheumatoid arthritis

Inhibition of Plasminogen Activation by Monoclonal Antibodies to the Kringle 5-B Chain Segment of Human Plasminogen

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Monoclonal antibodies against plasminogen and alpha-2-antiplasmin: binding to native and modified antigens

Cited by 20 publications

References 18 publications

Development and clinical application of a new ELISA assay to determine plasmin–α2‐antiplasmin complexes in plasma

Development and clinical application of a new ELISA assay to determine plasmin–α2‐antiplasmin complexes in plasma

Extravascular fibrin formation and dissolution in synovial tissue of patients with osteoarthritis and rheumatoid arthritis

Inhibition of Plasminogen Activation by Monoclonal Antibodies to the Kringle 5-B Chain Segment of Human Plasminogen

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Development and clinical application of a new ELISA assay to determine plasmin–α₂‐antiplasmin complexes in plasma

Development and clinical application of a new ELISA assay to determine plasmin–α₂‐antiplasmin complexes in plasma