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Anti-Phospholipid Autoantibodies in Thrombosis: Cause and/or Consequence of the Disruption of the Protein C-Dependent Hemostatic Balance
Published in E. Nigel Harris, Thomas Exner, Graham R. V. Hughes, Ronald A. Asherson, Phospholipid-Binding Antibodies, 2020
Jean-Marie Freyssinet, Catherine Ravanat, Lélia Grunebaum, Marie-Louise Wiesel, Jean-Pierre Cazenave
Two recent studies (References 95 and 96) have focused attention on (β2-glycoprotein I (also termed apolipoprotein H) as a potentially essential plasma cofactor for the in vitro interaction aPL-anionic phospholipids such as cardiolipin or phosphatidylserine. However, one group found that 02-glycoprotein I behaved as an apparent antigen for aPL in ELISA, even in the absence of any anionic phospholipid,95 whereas the other one concludes that, since this cofactor is known to interact with anionic phospholipids, the complex bears antigenicity but not (β2-glycoprotein I independent of the presence of phospholipid.96 Both groups agree that when anionic phospholipids are the antigen, maximum reactivity of aPL is observed at ~4 μg/ml of cofactor, corresponding to a plasma dilution of 1/50 since the mean normal plasma concentration of (β2-glycoprotein I is 200 μg/ml. In purified systems, (β2-glycoprotein I exhibits significant anticoagulant activity in phospholipid-dependent assays only in the physiological concentration range and above.97 Furthermore, (β2-glycoprotein I has been found to interact with activated protein C.98 Taken together these results raise the question of the nature and heterogeneity of the in vivo antigenic patch recognized by aPL, thus re-emphasizing the crucial need of reference human monoclonal aPL which would allow the establishment of possible correlations between their origin/nature and pathogenic/marker character in thrombosis.
The Etiology of the Antiphospholipid Syndrome
Published in Howard J.A. Carp, Recurrent Pregnancy Loss, 2020
Sara De Carolis, Giuseppina Monteleone, Cristina Garufi, Rotem Inbar, Miri Blank, Yehuda Shoenfeld
aPL require a cofactor (apolipoprotein H or β2GP1), a negatively charged phospholipid binding protein, to exert their effects. β2GP1-dependent aPL are thought to recognize their antigen on placental tissue, inhibit growth and differentiation of trophoblasts, and cause inflammation, defective angiogenesis, and thrombosis, leading to impaired placentation.
Fibrinolytic Abnormalities and Antiphospholipid Antibodies
Published in Pia Glas-Greenwalt, Fibrinolysis in Disease Molecular and Hemovascular Aspects of Fibrinolysis, 2019
In 1990 three groups of workers independently found that some aPL would only bind to anionic phospholipids in the presence of a plasma cofactor.13-15 This cofactor was identified as β2-glycoprotein I,13 an apolipoprotein (also referred to as apolipoprotein H) known to bind to anionic phospholipids via its lysine residues in the terminal domain.16
Establishing molecular signatures of stroke focusing on omic approaches: a narrative review
Published in International Journal of Neuroscience, 2020
Abhilash Ludhiadch, Kanika Vasudeva, Anjana Munshi
Cevic et al. (2016) carried out a study on the proteins associated with cellular metabolic processes using UPLC- ESI-qTOF-MS approach. They found ALOX12 (Arachidonate 12-lipoxygenase), HRG (Histidine rich glycoproteins), MPO (Myeloperoxidase), cell signaling protein CRKL (Crk-like protein), cell adhesion protein VTN (Vitronectin), RHOA (Ras homolog gene family member A). ITGA2B (Integrin alpha 2 b), THBS1 (Thrombospondin 1), ITGB3 (Integrin beta 3), structural protein APOH (Apolipoprotein H), IGHG1 (Immunoglobulin heavy constant gamma 1), transporter protein APOA1 (Apolipoprotein A-I), IGHG3 (Immunoglobulin heavy constant 3), AMBP (Alpha-1-microglobulin/bikunin precursor) and immunity proteins C3 (Complement component 3), CLU (Clusterin) to be associated with platelet activation and response during IS [78].
Molecular diagnosis and classification of inflammatory bowel disease
Published in Expert Review of Molecular Diagnostics, 2018
Hu Zhang, Zhen Zeng, Arjudeb Mukherjee, Bo Shen
In addition to the markers discussed above, serum protein profiling is instructive in predicting the degrees of response. Meuwis et al [178]. firstly demonstrated that high levels of PF4 could predict poor response to infliximab. A model has been established for predicting positive response to infliximab with a sensitivity of 78.6%, a specificity of 80% and an accuracy of 79.3%, respectively. Gazouli and colleagues[179], however, reported no association between PF4 and response degrees to infliximab, but they found that levels of complement C3 (CO3), transthyretin and fibrinogen alpha chain (FIBA) were elevated in CD patients in clinical and serological remission compared with primary nonresponders (treated by infliximab). Moreover, they found that concentrations of some other proteins such as apolipoprotein A-I, apolipoprotein E, complement C4-B, plasminogen, serotransferrin, apolipoprotein H and clusterin were stable in patients in clinical and serological remission but were markedly increased in primary nonresponders and patients achieved clinical and serological response. Difference in serum protein profiles between responders and nonresponders may help clinicians to predict response rate of biologics.