Journal articles: 'Cardiolipin antibody'

1

Peter, JamesB. "Cardiolipin antibody assays." Lancet 335, no. 8702 (June 1990): 1405. http://dx.doi.org/10.1016/0140-6736(90)91286-j.

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Schlame, Michael, Ivan Haller, Lisa Sammaritano, and Thomas Blanck. "Effect of Cardiolipin Oxidation on Solid-Phase Immunoassay for Antiphospholipid Antibodies." Thrombosis and Haemostasis 86, no. 12 (2001): 1475–82. http://dx.doi.org/10.1055/s-0037-1616751.

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SummaryDiagnostic assays for antiphospholipid antibodies are routinely performed on microtitre plates coated with cardiolipin. Here we show that contact between cardiolipin and NUNC-Immuno® plates leads to extensive oxidation, generating a series of peroxy-cardiolipins which were identified by electrospray ionization mass spectrometry. To investigate the impact of oxidation on the antibody assay, cardiolipin was resolved into 12 molecular species, including oxidized species and non-oxidized species with different degrees of unsaturation. All 12 species reacted under anaerobic conditions with serum from patients with primary antiphospholipid syndrome. Immune reactivity was similar for tetralinoleoyl-cardiolipin, trilinoleoyl-oleoyl-cardiolipin, and peroxycardiolipins, but somewhat lower for tristearoyl-oleoyl-cardiolipin. Oxidative treatment of cardiolipin with air, cytochrome c, or Cu2+/tert-butylhydroperoxide, either before or during the assay, did not enhance immune reactivity. Similar results were obtained with a monoclonal IgM from lupus-prone mice, that binds cardiolipin in the absence of protein cofactors. We conclude that the solid-phase assay for antiphospholipid antibodies can be supported by various oxidized and nonoxididized molecular species of cardiolipin.

3

Costello, P. B., and F. A. Green. "Cholesterol effects on the interaction of cardiolipin with anti-cardiolipin antibody." Biochimica et Biophysica Acta (BBA) - Biomembranes 896, no. 1 (January 1987): 52–56. http://dx.doi.org/10.1016/0005-2736(87)90355-5.

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Lee, Chonghwee, Hyukje Lee, Hyeryung Kwon, Hansol Im, Miyeon Yoon, and Taewon Kim. "Sneddon Syndrome with Anti-Cardiolipin Antibody." Journal of the Korean Neurological Association 39, no. 1 (February 1, 2021): 48–50. http://dx.doi.org/10.17340/jkna.2021.1.12.

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Harris, E. Nigel, and GrahamR V. Hughes. "STANDARDISING THE ANTI-CARDIOLIPIN ANTIBODY TEST." Lancet 329, no. 8527 (January 1987): 277. http://dx.doi.org/10.1016/s0140-6736(87)90099-7.

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Higashino, Masahiko, Koichi Takakuwa, Masato Arakawa, Masaki Tamura, Masako Yasuda, and Kenichi Tanaka. "Anti-cardiolipin antibody and anti-cardiolipin beta-2-glycoprotein I antibody in patients with recurrent fetal miscarriage." Journal of Perinatal Medicine 26, no. 5 (January 1998): 384–89. http://dx.doi.org/10.1515/jpme.1998.26.5.384.

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D'Agati, V., C. Kunis, G. Williams, and G. B. Appel. "Anti-cardiolipin antibody and renal disease: a report three cases." Journal of the American Society of Nephrology 1, no. 5 (November 1990): 777–84. http://dx.doi.org/10.1681/asn.v15777.

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Anti-cardiolipin antibodies have been linked to recurrent arterial and venous thrombosis in multiple organs. We present a biopsy-documented report of thrombotic renal disease apparently attributable to circulating anti-cardiolipin antibodies. One patient had primary anti-cardiolipin syndrome, one had mild SLE, and the third had a mild lupus-like syndrome. All three patients had a clinical course dominated by repeated multi-organ system thrombosis. Renal biopsy disclosed thrombosis at the level of the glomerular capillaries, arterioles, and interlobular arteries--similar to that described in other thrombotic microangiopathies. Renal thrombosis was not associated with active endocapillary proliferative lupus nephritis, suggesting a mechanism independent of subendothelial immune deposit injury. Renal presentation was variable, ranging from asymptomatic mild proteinuria to nephrotic-range proteinuria, renal insufficiency, and hypertension.

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SUMITA, TAKAYUKI. "V region gene of anti-cardiolipin antibody." Japanese Journal of Clinical Immunology 16, no. 6 (1993): 546–54. http://dx.doi.org/10.2177/jsci.16.546.

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9

Abdolreza, Abdolreza, Mohammad Shojaie, Samira Dana, and Abdoulhossain Madani. "Anti-Cardiolipin Antibody in Acute Myocardial Infarction." American Journal of Immunology 6, no. 1 (January 1, 2010): 11–14. http://dx.doi.org/10.3844/ajisp.2010.11.14.

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Kilpatrick, David C., Rose E. B. Haining, and Steven S. K. Smith. "Are cardiolipin antibody levels elevated in endometriosis?" Fertility and Sterility 55, no. 2 (February 1991): 436–37. http://dx.doi.org/10.1016/s0015-0282(16)54144-2.

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11

Costa, Renzo, Evangelia Fatourou, Debra Hoppensteadt, Jawed Fareed, and Angelos Halaris. "Cardiolipin Antibody: A Potential Biomarker for Depression." Journal of Personalized Medicine 12, no. 11 (October 24, 2022): 1759. http://dx.doi.org/10.3390/jpm12111759.

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Inflammation plays a pivotal role in the etiopathology of Major Depressive Disorder (MDD), at least in a subset of patients. It is crucial to first establish which specific inflammatory biomarkers are of clinical utility. Anti-cardiolipin antibody (aCL IgM) is an inflammatory marker that has the potential to be such a candidate but there are insufficient studies to confirm this potential. Objective: To investigate the baseline titer level and the longitudinal progression of plasma titers of aCL IgM in MDD subjects receiving antidepressant therapy in comparison to healthy control (HC) subjects; to determine if changes in aCL IgM plasma titers correlate to changes in depressive symptoms; and, to ascertain if baseline aCL IgM plasma titers could predict treatment response. Methods: Forty-eight medically healthy outpatients diagnosed with MDD were enrolled in one of two groups in two sequentially conducted clinical trials. In Group-E, patients received a 12-week regimen of escitalopram (n = 20). Those in Group-Q received a 12-week regimen of quetiapine (n = 28). The main outcome measure was plasma aCL IgM titers, the Hamilton Rating Scale for Depression (HAM-D17) and the Hamilton Rating Scale for Anxiety (HAM-A). There were 16 HC subjects. Results: When Group-Q and Group-E participants were grouped together (n = 48), MDD subjects had an elevated baseline aCL IgM (19.9 μg/ml) compared to HC subjects (8.32 μg/ml) (p = 0.006). aCL IgM correlated significantly with HAM-D17 scores at baseline in MDD subjects (p = 0.0185, r = 0.296). Examining the individual groups, Group-Q MDD patients had a significantly elevated baseline aCL IgM (p = 0.008) while Group-E’s MDD patients did not. On the other hand, only Group-E MDD patients showed a significant correlation at baseline between aCL IgM and HAM-A score (p = 0.0392, r = 0.4327); they also showed a significant inverse correlation between week 12 HAMD-17 Item #10 (Anxiety, Psychic) and week 12 aCL IgM titer (p = 0.0268, r = −0.5516). Conclusion: MDD patients had significantly higher plasma titers of aCL IgM when compared to HC subjects. Moreover, at baseline, the higher the aCL IgM titer, the higher the depression severity, as measured by HAMD-17 score. However, this study did not demonstrate that aCL IgM titers changed significantly throughout a 12-week course of antidepressant treatment and revealed no correlation between changes in depressive symptoms and changes in aCL IgM titers. Baseline aCL IgM could not predict treatment response. We conclude that, despite lacking predictive ability as regards treatment response, plasma titers of aCL IgM have a diagnostic potential in MDD that necessitates further exploration.

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Chang, Shih-Chen, Bor-Luen Chiang, Wen-Mien Wu, and Bi-Fong Lin. "Different dietary fats influence serum and tissue lipids and anti-cardiolipin antibody levels in autoimmune-prone NZB/W F1 mice." British Journal of Nutrition 81, no. 4 (April 1999): 331–40. http://dx.doi.org/10.1017/s0007114599000586.

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To investigate the influence of different dietary fats on lipids and anti-cardiolipin antibody levels, autoimmune NZB/W F1 mice were fed on diets containing 200 g dietary fat as palm oil, lard–soyabean oil (1:1, w/w), soyabean oil, rapeseed oil or fish oil/kg. In addition, each dietary fat group was divided into an early-feeding group with feeding from 2 months of age, and a late-feeding group with feeding from 5 months of age. Serum levels of triacylglycerol, phospholipid, cholesterol and anti-cardiolipin antibody were measured at regular intervals, and mice were killed at the age of 7 months for analysis of hepatic lipid and fatty acids. The results showed that hepatic triacylglycerol and cholesterol contents were lower in mice fed on fish oil than in those fed on palm oil. In contrast, hepatic phospholipid content was higher in mice of the fish oil group than in those of the other four dietary fat groups. Composition profiles for both hepatic and renal oleic acid (18:1n-9), linoleic acid (18:2n-6) and eicosapentaenoic acid (20:5n-3) were similar to those of the dietary fats in mice of both early-feeding and late-feeding groups. Fish oil intake decreased arachidonic acid (20:4n-6) concentration in kidney tissue but not in liver tissue. Serum triacylglycerol, cholesterol and phospholipid levels were lower in mice fed on fish oil than in those fed on palm oil. Immunoglobulin (Ig) M anti-cardiolipin antibody was lower for the fish oil group than for the other groups. The IgG anti-cardiolipin antibody level was significantly lower in mice fed on fish oil compared with that of the palm oil group only in the early-feeding group. There was a positive correlation between serum IgM anti-cardiolipin antibody and phospholipid levels (early-feeding group r 0·902, P < 0·05; late-feeding group r 0·894, P < 0·05). These findings suggest dietary fish oil may affect both lipid levels and anti-cardiolipin antibody, contributing to alleviation of the autoimmune process in autoimmune-prone NZB×NZW F1 mice.

13

Radic, M. Z., M. A. Mascelli, J. Erikson, H. Shan, and M. Weigert. "Ig H and L chain contributions to autoimmune specificities." Journal of Immunology 146, no. 1 (January 1, 1991): 176–82. http://dx.doi.org/10.4049/jimmunol.146.1.176.

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Abstract An Ig H chain expression vector has been constructed by using the V region of 3H9, an antibody that binds ssDNA, dsDNA, and cardiolipin. The H chain construct was transfected into six hybridoma cell lines expressing Ig L chains. All resulting H and L chain combinations had at least some affinity for ssDNA, whereas five also bound dsDNA to a similar degree as 3H9. The loss of dsDNA binding was correlated with a single amino acid difference between two V kappa 8 L chains. A further characteristic of 3H9, its immunofluorescent staining pattern, was shared by four of the recombinant antibodies, whereas its specificity for cardiolipin was shared with five. The transfections reported here show that a V kappa 3 L chain confers specificity for an RNA-associated epitope and that a V kappa 21E L chain prevents cardiolipin binding. These experiments suggest that the 3H9 H chain contributes essential determinants required for binding to DNA as well as cardiolipin but that L chains can modulate or prevent this binding. L chains may also expand the specificity of a recombinant antibody.

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CHANG, KENG-YUNG, YOW-CHII KUO, CHEUG-TANG CHIU, SHYI-SHANE WU, CHUN-YEN HUANG, CHENG-SHYONG WU, SHU-CHEN LIAW, and HUEI-HUANG HO. "Anti-cardiolipin Antibody Associated with Acute Hemorrhagic Pancreatitis." Pancreas 8, no. 5 (September 1993): 654–57. http://dx.doi.org/10.1097/00006676-199309000-00022.

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15

de Lima Ferreira Fernandes Costa, Hélio, Marcos Dias de Mourn, Rui Alberto Ferriani, Maria Inez Suva Anceschi, and José Elpídio Barbosa. "Prevalence of Anti-Cardiolipin Antibody in Habitual Aborters." Gynecologic and Obstetric Investigation 36, no. 4 (1993): 221–25. http://dx.doi.org/10.1159/000292633.

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16

Weingarten, Karen, Christopher Filippi, Denise Barbut, and Robert D. Zimmerman. "The neuroimaging features of the cardiolipin antibody syndrome." Clinical Imaging 21, no. 1 (January 1997): 6–12. http://dx.doi.org/10.1016/0899-7071(95)00044-5.

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17

MENON, G., and J. ALLT-GRAHAM. "ANAESTHETIC IMPLICATIONS OF THE ANTI-CARDIOLIPIN ANTIBODY SYNDROME." British Journal of Anaesthesia 70, no. 5 (May 1993): 587–90. http://dx.doi.org/10.1093/bja/70.5.587.

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18

Peitsch, M. C., J. Tschopp, A. Kress, and H. Isliker. "Antibody-independent activation of the complement system by mitochondria is mediated by cardiolipin." Biochemical Journal 249, no. 2 (January 15, 1988): 495–500. http://dx.doi.org/10.1042/bj2490495.

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Non-immune activation of the first component of complement (C1) by the heart mitochondrial inner membrane has been investigated. Cardiolipin, the only strong activator of C1 among phospholipids, is present in large amounts in the heart mitochondrial inner membrane. We therefore studied its contribution to C1 activation by mitochondria. The proteins of the mitochondrial inner membrane were found to activate C1 only weakly, in contrast with the phospholipid fraction which induces strong C1 activation. Furthermore, the digestion of mitochondrial inner membranes with proteolytic enzymes did not affect C1 activation. Additional support in favour of cardiolipin being the responsible activator came from competition experiments with mitochondrial creatine kinase (mt-CPK) and adriamycin, known to bind to cardiolipin. Both mt-CPK and adriamycin displaced C1q from the mitochondrial inner membrane. In addition, C1q displaced mt-CPK bound to mitoplasts.

19

NAKAMURA, Tomoaki. "Antigenicity of bacterial membrane-cardiolipin and reactivity of anti-cardiolipin antibody with bacteria and DNA." Okayama Igakkai Zasshi (Journal of Okayama Medical Association) 100, no. 1-2 (1988): 97–106. http://dx.doi.org/10.4044/joma1947.100.1-2_97.

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20

Lin, Bi-Fong, Su-Jen Jeng, Bor-Luen Chiang, and Chao-Chi Huang. "Dietary fat affects lipids and anti-cardiolipin antibody levels in autoimmune-prone NZB/W F1 mice." British Journal of Nutrition 77, no. 4 (April 1997): 657–69. http://dx.doi.org/10.1079/bjn19970063.

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Studies in autoimmune-prone NZB/W F1 mice have demonstrated that the amount of dietary fat can affect autoantibody production and the disease course of autoimmune diseases. Anti-cardiolipin antibodies have been found to play a major role in thrombus formation and the increase of abortion rate in both human lupus patients and murine lupus. The present study investigated further the effect of dietary fat on lipid and anti-cardiolipin antibody production in autoimmune-prone mice. Two groups of NZB/W F1 mice were fed on diets containing 200 g dietary fat/kg and 50 g dietary fat/kg respectively, the fat being composed of equal amounts of lard and soyabean oil. Serum levels of lipids, immunoglobulin (Ig) anti-single stranded DNA and anti-cardiolipin antibodies were followed regularly every month and mice were killed forin vitroexperiments after 5 months on the experimental diets. The results showed that serum triacylglycerol concentration was lower in mice fed on the high-fat diet than in those fed on 50 g fat/kg. There was no significant difference in hepatic lipid contents; however, the fatty acid contents were different between these two groups. Hepatic linoleic acid (18:2n−6) and arachidonic acid (20:4n−6) concentrations were higher in mice fed on the high-fat diet. There were no significant differences in serum IgM concentrations or IgM anti-cardiolipin antibody levels between these two groups. However, IgG anti-cardiolipin antibody levels were higher in mice fed on the high-fat diet at the age of 3–4 months. Total serum IgG concentration was noted to be higher, but in contrast, serum IgA was lower, in the high-dietary-fat group. These findings suggest that high dietary fat may affect lipid metabolism and autoantibody levels in autoimmune diseases

21

Kaneko, Atsushi, Kyoichi Nomura, Ryozo Ohno, Kazuhiro Kurihara, Hiroshi Yoshida, Manabu Ohnuki, Ryo Tomioka, Takeshi Hosokawa, Katsuhiko Hamaguchi, and Kunio Shimazu. "Polymyalgia Rheumatica and Myelitis associated with Anti-Cardiolipin Antibody." Nippon Ronen Igakkai Zasshi. Japanese Journal of Geriatrics 35, no. 12 (1998): 918–23. http://dx.doi.org/10.3143/geriatrics.35.918.

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Wong, Richard C. W., David Gillis, Stephen Adelstein, Karl Baumgart, Emmanuel J. Favaloro, Michelle J. Hendle, Paul Homes, et al. "Consensus guidelines on anti-cardiolipin antibody testing and reporting." Pathology 36, no. 1 (February 2004): 63–68. http://dx.doi.org/10.1080/00313020310001643615.

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Soper, C. P. R., S. A. Sampson, and N. Velasco. "Renal thrombotic microangiopathy, Campylobacter gastroenteritis and anti‐cardiolipin antibody." Nephrology Dialysis Transplantation 15, no. 8 (August 1, 2000): 1261–62. http://dx.doi.org/10.1093/ndt/15.8.1261-a.

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Kennedy, Stephen H., Barbara Nunn, Stewart A. Cederholm-Williams, and David H. Barlow. "Cardiolipin antibody levels in endometriosis and systemic lupus erythematosus." Fertility and Sterility 52, no. 6 (December 1989): 1061–62. http://dx.doi.org/10.1016/s0015-0282(16)53175-6.

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Beglova, Natalia, Alexey Kolyada, Chang-Jin Lee, and Alfredo De Biasio. "A Novel Dimeric Inhibitor That Targets Dimeric ß2GPI In ß2GPI/Anti-ß2GPI Antibody Complexes." Blood 116, no. 21 (November 19, 2010): 1142. http://dx.doi.org/10.1182/blood.v116.21.1142.1142.

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Abstract Abstract 1142 ß2GPI is a major antigen for autoantibodies associated with antiphospholipid syndrome, an autoimmune disease characterized by thrombosis and recurrent pregnancy loss. Only the dimeric form of ß2GPI generated by anti-ß2GPI antibodies is pathologically important, in contrast to monomeric ß2GPI which is abundant in plasma. Several cell-surface molecules including anionic phospholipids and ApoER2, a member of the lipoprotein receptor family, are implicated in the pathology of antiphospholipid syndrome. We created a dimeric inhibitor, A1-A1, to selectively target ß2GPI in ß2GPI/antibody complexes. This inhibitor consists of two ligand-binding A1 modules from ApoER2 connected by a flexible linker. A1-A1 disrupts the binding of ß2GPI/antibody complexes with anionic phospholipids and lipoprotein receptors. We compared the potency of A1-A1 to monomeric A1 for inhibition of the binding of ß2GPI/antibody complexes to anionic phospholipids. We tested the inhibition of ß2GPI present in human serum, ß2GPI purified from human plasma and domain V of ß2GPI. We demonstrated that when ß2GPI/antibody complexes are formed, A1-A1 is more effective than A1 in inhibition of the ß2GPI binding to cardiolipin, regardless of the source of ß2GPI. Half maximum inhibition of ß2GPI in human serum in the presence of anti-ß2GPI antibodies was achieved at 9 μM of A1-A1 and 218 μM of A1. Similarly, ß2GPI purified from plasma was inhibited to 50% by 26 μM of A1-A1 and 191 μM of A1. Also, A1-A1 strongly inhibited the binding of dimerized domain V of ß2GPI to cardiolipin compared to monomeric A1. Concentration of A1-A1 and A1 at half maximum inhibition of the binding of ß2GPI domain V to cardiolipin in the presence of dimerization antibodies was 29 μM and 204 μM, respectively. In the absence of anti-ß2GPI antibodies, A1-A1 and A1 were equally inefficient in the inhibition of the binding of monomeric ß2GPI to cardiolipin. The concentration of inhibitor at half-maximum inhibition of the binding of ß2GPI in human serum to cardiolipin was 189 μM for A1-A1 and 176 μM for A1. A novel inhibitor A1-A1 may be a starting point in the development of an effective therapeutic for antiphospholipid syndrome. Disclosures: No relevant conflicts of interest to declare.

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Koike, T., and E. Matsuura. "Anti-β2-glycoprotein I Antibody: Specificity and Clinical Significance." Lupus 5, no. 5 (October 1996): 378–80. http://dx.doi.org/10.1177/096120339600500508.

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Cardiolipin binding of IgG-class anticardiolipin antibody (aCL) depends on the existence of β2-glycoprotein I (β2-GPI). We developed an EIA system that enables detection of antibodies against β2-GPI, without the presence of cardiolipin. This system involves use of irradiated polystyrene plates, in which oxygen atoms are introduced onto the surfaces of the plates. β2-GPI bound to the surface of these plates is assumed to undergo a conformational change that exposes normally cryptic epitopes. Anti-β2-GPI antibody measured using this EIA system showed good correlation with aCL measured by conventional EIA methods and may prove useful in evaluating the risk of thrombosis and monitoring the clinical course in patients with SLE. Utilizing this EIA system and β2-GPI-deleted mutants, we found that the fourth domain of β2-GPI is involved in expression of one of the cryptic epitopes recognized by aCL. We also found that oxidized LDL are sequentially targeted by β2-GPI and aCL.

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Jizzini, Mazen, Mohsin Shah, and Kehua Zhou. "SARS-CoV-2 and Anti-Cardiolipin Antibodies." Clinical Medicine Insights: Case Reports 13 (January 2020): 117954762098038. http://dx.doi.org/10.1177/1179547620980381.

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The current COVID-19 pandemic caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has led to distinct diagnostic and management challenges for front-line healthcare workers. The risk of excessive coagulation activation leading to a cascade of thrombotic events in critically ill patients with SARS-CoV-2 is now well reported. We discuss a recent case of COVID-19 with concurrent acute pulmonary embolism and a positive cardiolipin antibody (IgM). The presence of antiphospholipid antibodies is key to diagnosing antiphospholipid syndrome (APS). However, their presence can be transient or persistent after viral infections. Serial inflammatory markers in conjunction with anti-phospholipid antibody testing is critical for the diagnosis of APS in this emerging patient population. Our case report reviews details suggestive of APS in the setting of SARS-CoV-2 and aims to provide clinical diagnostic clues that could help warrant further workup and assist with management strategies.

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Gupta, Anuj, Joshika Agarwal, Shilpi Gupta, and Anurag Singh. "Clinical significance of anti-phospholipid antibodies in Henoch Schönlein purpura." International Journal Of Community Medicine And Public Health 8, no. 8 (July 27, 2021): 4037. http://dx.doi.org/10.18203/2394-6040.ijcmph20213041.

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Background: Henoch Schönlein purpura also known as IgA vasculitis is described histologically by IgA deposition in the blood vessel walls and presents with kidney involvement, palpable purpura, arthralgia, and abdominal pain. Our study aims to evaluate the association between anti-phospholipid antibody, anti-cardiolipin antibody, anti-beta(2) glycoprotein 1 antibody and Anti-phosphatidylserine/prothrombin antibodies and IgA vasculitis. Treatment response with intravenous steroids and cyclophosphamide was also studied based on resolution of antibody titer.Methods: We conducted an observational study in three Rheumatology clinics at Ahmedabad, India. Data was collected for a period of 6 months. Diagnosis of IgA vasculitis was determined based on the International Chapel hill consensus conference 2012. Disease activity was assessed based on antibody titer, histological grading and through a pre-determined clinical form to assess objective clinical symptoms. P value of less than 0.05 was considered significantResults: Study evaluated antibody titer of 178 patients. Sixty one percent of the patient's had positive anti-phospholipid antibody titer with predominant antibody subtype as IgG. Inflammatory markers were significantly higher in patient having anti-phospholipid antibody titer. Anti-phospholipid antibody was present in 100 percent patients who had vascular thrombosis. IgG subtype of anti-cardiolipin antibody were found in 60 percent of the patients with renal complication.Conclusions: Anti-phospholipid antibody have a close association with IgA vasculitis. Anti-phospholipid antibody has a significant role in mounting inflammatory response and vascular thrombosis. Combination treatment of intravenous steroids and cyclophosphamide found to be more effective in resolution of titer

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HISASHI, KAZUTAKA. "Sensorineural deafness. II. Acute sensorineural deafness by anti-cardiolipin antibody." AUDIOLOGY JAPAN 38, no. 5 (1995): 341–42. http://dx.doi.org/10.4295/audiology.38.341.

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Kilpatrick, David C. "Factors affecting cardiolipin antibody assays: modification with polyethylene glycol compound." British Journal of Haematology 100, no. 1 (January 1998): 52–57. http://dx.doi.org/10.1046/j.1365-2141.1998.00532.x.

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Rauch, J., and AS Janoff. "Antibodies against Phospholipids other than Cardiolipin: Potential Roles for Both Phospholipid and Protein." Lupus 5, no. 5 (October 1996): 498–502. http://dx.doi.org/10.1177/096120339600500534.

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Autoantibodies to phospholipids other than cardiolipin have received less attention, to date, than anti-cardiolipin antibodies. This review focuses on these antibodies and potential roles for both phospholipid and protein in their reactivity. We review data in the literature indicating that antibodies to phosphatidylethanolamine and some lupus anticoagulant antibodies recognize phospholipid-binding proteins in association with phospholipid. Kininogens appear to be involved in the binding of antibodies to phosphatidylethanolamine, while phosphatidylserine-binding proteins, such as prothrombin and annexin V, have been implicated in lupus anticoagulant antibody recognition. These proteins bind to phospholipids that normally reside in the inner monolayer of the cell membrane, suggesting that exposure of these lipids is necessary for protein binding and antibody recognition to occur. In contrast, other autoantibodies, in particular those reactive with erythrocytes, appear to be directed at phospholipids that normally occur in the outer membrane leaflet, such as phosphatidylcholine. In summary, there is clearly accumulating evidence that antibodies to phospholipids other than cardiolipin recognize epitopes on phospholipid-binding proteins. It is not clear whether recognition of these epitopes is due to an increase in antigen density or a change in the protein or phospholipid structure, but it is likely that both protein and phospholipid structure play an important role in the in vivo interactions of these antibodies.

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Sammaritano, L. R., and M. D. Lockshin. "Pregnancy and antiphospholipid antibody." Hämostaseologie 21, no. 02 (2001): 66–76. http://dx.doi.org/10.1055/s-0037-1619506.

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SummaryThe antiphospholipid antibody syndrome is defined by anticardiolipin antibody or lupus anticoagulant and recurrent pregnancy loss or recurrent thrombosis. Approximately one-third of patients with systemic lupus erythematosus, 10-15% of women with recurrent fetal loss, and 1-2% of normal women have one or both of these antibodies. The true antigen is a phospholipid-binding protein, β2-glycoprotein I, not cardiolipin. Risk for pregnancy loss is determined by IgG isotype titer, and prior pregnancy history. Early pregnancy is often normal, but placental insufficiency produces slowed fetal growth and second trimester fetal demise. The most likely mechanism is unimpeded thrombosis within the placental circulation, possibly because antiphospholipid antibody competes with placental anticoagulant I. Heparin in subanticoagulant doses plus low dose aspirin results in fetal survival rates of over 90%. Post partum, the long-term risk of maternal arterial or venous thrombosis is high.

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Gontar, I. P., Oiga Ivanovna Emelyanova, O. A. Rusanova, I. A. Zborovskay, and N. I. Emelyanov. "TECHNIQUES OF MODIFYING LIPID ANTIGENS FOR SYNTHESIS OF DIAGNOSTIC AND THERPAEUTIC PREPARATIONS IN RHEUMATOLOGY." Russian Clinical Laboratory Diagnostics 64, no. 10 (October 15, 2019): 603–6. http://dx.doi.org/10.18821/0869-2084-2019-64-10-603-606.

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The objective of the study is to enhance sorption capacity of diagnostic agents by using cardiolipin antigens for antiphospholipid syndrome in patients with systemic lupus erythematosus (SLE). A technique of emulsion polimerization was used. Having integrated antigen nanoobjects we developed immobilized magnetocontrollable antigen nanosystems and put them to an evaluation test. The nanosystems are polyacrylamide granules with a built in antigen. To obtain stable immobilized multi-use biopharmaceuticals with targeted properties (shape, particle diameter, pore size, density) we used a modified version of emulsion polymerization method using polyacrylamide carrier gel. This method permitted a greater sorptive capacity, preserving the antigen in maximum native state, and opened up the possibility of controllable modification of nanoobjects. Cardiolipin was used as the antigen in question. Following the method described above we performed sorption of anticardiolipin antibodies from blood plasma of SLE patients who showed clinical presentations of antiphospholipid syndrome. All SLE patoents with signs of antiphospholipid syndrome showed reliably higher levels of cardiolipin antibodies compared with SLE patients without antiphospholipid syndrome signs; the antibody level was 0.365 ± 0.026 and 0.075 ± 0.003 on average, correspondingly (p < 0.001). Blood serum from 10 apparently healthy individuals served as control. The level of cardiolipin antibodies was determined before and after sorption by indirect solid phase immunoenzyme method. In the eluate we estimated total protein by Lowry method. In vitro testing showed that the obtained antigen nanosystems based on immobilized cardiolipin could effectively remove cardiolipin antibodies from whole blood of SLE patients with clinical presentations of APS to achieve the values of healthy individuals (before sorption cardiolipin antibodies 0.328 ± 0.0289; after sorption 0.059 ± 0.0170; p<0,001; sorption capacity 8.00 ± 0.390 mg/ml). The method of emulsion polymerization with consideration to hydrophobic and hydrophilic properties of lipid molecules permits obtaining and modifying biomolecules with certain properties, in a controlled fashion.

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Damodaram, P., CH Geetha, Shantiveer G. Uppin, and L. Rajasekhar. "P35 Performance of anti-cardiolipin antibodies and lupus anticoagulant assay in lupus patients with suspected anti-cardiolipin antibody syndrome." Indian Journal of Rheumatology 6, no. 3 (November 2011): S13. http://dx.doi.org/10.1016/s0973-3698(11)60145-3.

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Do Egito, Elton M. N., Alberto G. Silva-Júnior, Raiza P. S. Lucena, Maria D. L. Oliveira, and César A. S. Andrade. "Electrochemical platform for anti-cardiolipin antibody detection in human syphilitic serum." Current Research in Biotechnology 4 (2022): 58–65. http://dx.doi.org/10.1016/j.crbiot.2022.01.001.

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MARKEY, A. C., and D. M. MACDONALD. "Systemic lupus erythematosus with complement deficiency and IgA anti-cardiolipin antibody." British Journal of Dermatology 119, no. 5 (November 1988): 633–37. http://dx.doi.org/10.1111/j.1365-2133.1988.tb03475.x.

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Cheng, Hwee-Ming, Yun-Fong Ngeow, and Choon-Kook Sam. "Heat inactivation of serum potentiates anti-cardiolipin antibody binding in ELISA." Journal of Immunological Methods 124, no. 2 (November 1989): 235–38. http://dx.doi.org/10.1016/0022-1759(89)90359-1.

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Chua, I., and A. Jawad. "Acute postoperative inflammatory polyarthritis associated with a lone IgM cardiolipin antibody." Case Reports 2015, mar02 1 (March 2, 2015): bcr2014208218. http://dx.doi.org/10.1136/bcr-2014-208218.

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TURTLE, C. J., L. A. COYLE, and G. KOTSIOU. "Q-fever associated with splenic infarction and an anti-cardiolipin antibody." Australian and New Zealand Journal of Medicine 29, no. 5 (October 1999): 755–56. http://dx.doi.org/10.1111/j.1445-5994.1999.tb01635.x.

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Comer, Gail M., Shanker Mukherjee, Ranjit K. Sachdev, and David J. Clain. "Cardiolipin-fluorescent (M1) antimitochondrial antibody and cholestatic hepatitis in secondary syphilis." Digestive Diseases and Sciences 34, no. 8 (August 1989): 1298–302. http://dx.doi.org/10.1007/bf01537283.

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Arvieux, Josiane, Gilles Pernod, Véronique Regnault, Luc Darnige, and Jérôme Garin. "Some Anticardiolipin Antibodies Recognize a Combination of Phospholipids With Thrombin-Modified Antithrombin, Complement C4b-Binding Protein, and Lipopolysaccharide Binding Protein." Blood 93, no. 12 (June 15, 1999): 4248–55. http://dx.doi.org/10.1182/blood.v93.12.4248.

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Abstract The standard enzyme-linked immunosorbent assay (ELISA) for anticardiolipin antibodies (ACA) detects a heterogenous group of antibodies against cardiolipin on its own, β2-glycoprotein I (β2GPI), and, potentially, other phospholipid-binding plasma proteins from bovine or human origin. In an attempt to identify new proteic targets of ACA, we selected 6 patients who possessed cofactor-dependent ACA but no antibody to human or bovine β2GPI detectable in the β2GPI-ELISA. Three of these samples proved to recognize β2GPI in combination with cardiolipin, but not β2GPI directly immobilized on γ-irradiated polystyrene or agarose beads. In the other cases, the component required for ACA binding was purified from adult bovine serum or plasma by means of ammonium sulfate precipitation and chromatography on Phenyl-Sepharose, diethyl aminoethyl (DEAE)-cellulose, heparin-Ultrogel, and Sephacryl S-300 columns. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis coupled to N-terminal amino acid microsequencing identified the cofactors of patients no. 4, 5, and 6 ACA as lipopolysaccharide binding protein (LBP), complement C4b-binding protein (C4BP), and the thrombin-antithrombin (AT) complex, respectively. Adsorption of each of these cofactor preparations with cardiolipin liposomes led to suppression of ACA reactivity, concomitant with the loss of bands from SDS gels corresponding to sequenced material. Bacterial lipopolysaccharide (which forms high-affinity complexes with LBP) specifically neutralized the cofactor activity of the LBP preparation in a concentration-dependent manner. Bovine serum and plasma, as well as the C4BP preparation, optimally supported the binding of a rabbit anti-C4BP antiserum to immobilized cardiolipin. The binding of a rabbit anti-AT antiserum to solid-phase cardiolipin was sustained by the thrombin-AT preparation and bovine serum, but neither by bovine plasma nor by native AT, thus reproducing the behavior of patient no. 6 ACA. Taking advantage of the restricted recognition by the latter ACA of a cofactor from bovine origin appearing upon clotting, we studied the generation of such activity in human plasma supplemented with bovine AT or bovine prothrombin before clotting. In these conditions, patient no. 6 antibody binding to cardiolipin required the addition of bovine AT, whereas addition of bovine prothrombin alone was ineffective. We therefore concluded that those ACA targeted bovine AT once it has been modified/cleaved by thrombin. These findings underline the wide heterogeneity of ACA and the links that may exist between various coagulation pathways, inflammation and the complement system.

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Arvieux, Josiane, Gilles Pernod, Véronique Regnault, Luc Darnige, and Jérôme Garin. "Some Anticardiolipin Antibodies Recognize a Combination of Phospholipids With Thrombin-Modified Antithrombin, Complement C4b-Binding Protein, and Lipopolysaccharide Binding Protein." Blood 93, no. 12 (June 15, 1999): 4248–55. http://dx.doi.org/10.1182/blood.v93.12.4248.412k24_4248_4255.

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The standard enzyme-linked immunosorbent assay (ELISA) for anticardiolipin antibodies (ACA) detects a heterogenous group of antibodies against cardiolipin on its own, β2-glycoprotein I (β2GPI), and, potentially, other phospholipid-binding plasma proteins from bovine or human origin. In an attempt to identify new proteic targets of ACA, we selected 6 patients who possessed cofactor-dependent ACA but no antibody to human or bovine β2GPI detectable in the β2GPI-ELISA. Three of these samples proved to recognize β2GPI in combination with cardiolipin, but not β2GPI directly immobilized on γ-irradiated polystyrene or agarose beads. In the other cases, the component required for ACA binding was purified from adult bovine serum or plasma by means of ammonium sulfate precipitation and chromatography on Phenyl-Sepharose, diethyl aminoethyl (DEAE)-cellulose, heparin-Ultrogel, and Sephacryl S-300 columns. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis coupled to N-terminal amino acid microsequencing identified the cofactors of patients no. 4, 5, and 6 ACA as lipopolysaccharide binding protein (LBP), complement C4b-binding protein (C4BP), and the thrombin-antithrombin (AT) complex, respectively. Adsorption of each of these cofactor preparations with cardiolipin liposomes led to suppression of ACA reactivity, concomitant with the loss of bands from SDS gels corresponding to sequenced material. Bacterial lipopolysaccharide (which forms high-affinity complexes with LBP) specifically neutralized the cofactor activity of the LBP preparation in a concentration-dependent manner. Bovine serum and plasma, as well as the C4BP preparation, optimally supported the binding of a rabbit anti-C4BP antiserum to immobilized cardiolipin. The binding of a rabbit anti-AT antiserum to solid-phase cardiolipin was sustained by the thrombin-AT preparation and bovine serum, but neither by bovine plasma nor by native AT, thus reproducing the behavior of patient no. 6 ACA. Taking advantage of the restricted recognition by the latter ACA of a cofactor from bovine origin appearing upon clotting, we studied the generation of such activity in human plasma supplemented with bovine AT or bovine prothrombin before clotting. In these conditions, patient no. 6 antibody binding to cardiolipin required the addition of bovine AT, whereas addition of bovine prothrombin alone was ineffective. We therefore concluded that those ACA targeted bovine AT once it has been modified/cleaved by thrombin. These findings underline the wide heterogeneity of ACA and the links that may exist between various coagulation pathways, inflammation and the complement system.

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Kravchenko, Elena N., and Anastasiia A. Goncharova. "Correlation between indicators of hemostasis system activity and antiphospholipid antibodies levels in women with miscarriage." Gynecology 21, no. 5 (October 15, 2019): 53–58. http://dx.doi.org/10.26442/20795696.2019.5.190668.

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Aim. To study the correlation between the activity indicators of the blood coagulation system and the content of antiphospholipid antibodies in women with miscarriage, depending on the number of reproductive losses. Materials and methods. 137 cards of women with a history of pregnancy termination were analyzed, divided into 2 groups according to the principle of presence/absence of plasmapheresis in the treatment regimen at the stage of pregravid preparation, followed by ranking into 2 subgroups according to the principle of presence/absence of TORCH infection activity. Results. The highest correlation was found for the presence of autoantibodies against cardiolipin with the severity of antiphospholipid syndrome. Antibodies to b2-glyco-protein-1 were the second parameter in the level of correlation with the number of reproductive losses. The negative effect, diagnostic and pathogenetic value, first of all, of IgG is proved in comparison with IgM, IgG to cardiolipin, IgG to annexin V, IgG to cardiolipin and lupus anticoagulant. The main exogenous cause of antibody formation in AFL is an infectious agent. A key endogenous factor in antibody formation is recognized as a violation of endothelial hemostasis. Conclusion. The correlation relationships between the initial level and the dynamics of the content of antiphospholipid antibodies, the number of gestational losses, as well as a number of parameters of the hemostasis system were revealed and interpreted. An independent negative effect on the laboratory parameters of the antiphospholipid syndrome of gestational losses in an amount of more than two was revealed.

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Edberg, J. C., and R. P. Taylor. "Quantitative aspects of lupus anti-DNA autoantibody specificity." Journal of Immunology 136, no. 12 (June 15, 1986): 4581–87. http://dx.doi.org/10.4049/jimmunol.136.12.4581.

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Abstract In this study we have attempted to define the cross-reactive potential of SLE anti-DNA antibodies (in 19 representative sera and plasmas) in both the solution phase and the solid phase. We used the Farr and RBC-CF solution phase assays to measure quantitatively the ability of a variety of negatively charged structurally unrelated molecules to inhibit antibody binding to both native DNA (nDNA) and denatured DNA (dDNA). The inhibitors used were of two types: 1) phospholipids (cardiolipin, phosphatidyl glycerol, and phosphatidic acid) and 2) repeating negatively charged molecules (poly-glutamic acid, heparin sulfate, and chondroitin sulfate). We found in both assays that the phospholipids could inhibit antibody binding to nDNA and dDNA, but a large excess (about 1500-fold) of these molecules was needed relative to DNA to achieve equivalent levels of inhibition. The repeating negatively charged molecules did not inhibit DNA binding at equivalent molar levels as the phospholipids; generally, at least a 10,000-fold excess was needed relative to the nucleic acids to achieve any appreciable inhibition. Results of a dDNA binding-inhibition solid-phase ELISA for cross-reactivity of the anti-DNA antibodies gave quite similar results. Finally, we found that eight of the SLE samples did have anti-cardiolipin antibodies, as demonstrated in a cardiolipin-based ELISA. These results suggest that previous reports describing an apparent cross-reactivity of anti-DNA antibodies may not represent physiologically relevant interactions between anti-DNA antibodies and non-nucleic acid antigens.

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Chen, Xiaohong. "Study on autoimmune antibody of infertile women based on ultrasound images." Advances in Engineering Technology Research 1, no. 2 (September 23, 2022): 135. http://dx.doi.org/10.56028/aetr.1.2.135.

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Objective: to study the clinical value of reproductive immune autoantibody based on ultrasound image in the diagnosis of infertility. Methods: Eighty infertile women who were admitted to our hospital from June 2019 to May 2020 were included in the study. ELISA was used to detect the serum reproductive immunity antibodies of the patients, including anti-sperm antibody (AsAb), anti-endometrial antibody (EMAb), anti-ovarian antibody (AOAb) and anti-cardiolipin antibody (ACA). Results: the results of reproductive immune antibody test indexes of female infertility patients with different types were compared, and the difference was statistically significant (p < o. 05). conclusion: the detection of reproductive immune autoantibody in clinic can be used for the diagnosis of female infertility, and has important clinical value.

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Chen, Xiaohong. "Study on autoimmune antibody of infertile women based on ultrasound images." Advances in Engineering Technology Research 2, no. 1 (September 23, 2022): 135. http://dx.doi.org/10.56028/aetr.2.1.135.

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Objective: to study the clinical value of reproductive immune autoantibody based on ultrasound image in the diagnosis of infertility. Methods: Eighty infertile women who were admitted to our hospital from June 2019 to May 2020 were included in the study. ELISA was used to detect the serum reproductive immunity antibodies of the patients, including anti-sperm antibody (AsAb), anti-endometrial antibody (EMAb), anti-ovarian antibody (AOAb) and anti-cardiolipin antibody (ACA). Results: the results of reproductive immune antibody test indexes of female infertility patients with different types were compared, and the difference was statistically significant (p < o. 05). conclusion: the detection of reproductive immune autoantibody in clinic can be used for the diagnosis of female infertility, and has important clinical value.

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Deb, Sudip Ranjan, Ahmedul Kabir, Tanzia Khanum, Md Golam Ur Rahman, Anowar Hossain, Md Alamin, and Rafiya Afroz. "Digital Symmetrical Peripheral Gangrene: A Rare Male PresentAtion of AntiPhospholipid Anti Body Syndrome." Journal of Dhaka Medical College 24, no. 2 (September 15, 2016): 152–55. http://dx.doi.org/10.3329/jdmc.v24i2.29628.

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Anti-phospholipid antibody syndrome can be defined as the occurrence of venous and arterial thrombosis with or without recurrent miscarriage in association with laboratory evidence of persistent Antiphospholipid antibody / antibody to beta-2-Glycoprotein-1 / anti cardiolipin antibody /lupus anticoagulant (usually associated with SLE). It occurs usually in female who can present with recurrent miscarriage and fetal loss. Anti-phospholipid Antibody can be also found in some autoimmune diseases and post viral infections. Even certain drugs; e.g. phenothiazine, can cause it. Arterial thrombosis may lead to peripheral limb ischemia, stroke, and myocardial infarct. And venous thrombosis may be found in the form of DVT, pulmonary embolism & thrombosis in vessels supplying the abdominal organ.J Dhaka Medical College, Vol. 24, No.2, October, 2015, Page 152-155

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Nakamura, Motonobu, and Yoshiki Tokura. "Systemic cholesterol embolization syndrome in a patient positive for anti-cardiolipin antibody." Dermato-Endocrinology 2, no. 2 (April 2010): 58–59. http://dx.doi.org/10.4161/derm.2.2.13372.

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Ramsey-Goldman, Rosalind, Joan E. Kutzer, Lewis H. Kuller, David Guzick, A. Betts Carpenter, and Thomas A. Medsger. "Pregnancy Outcome and Anti-Cardiolipin Antibody in Women with Systemic Lupus Erythematosus." American Journal of Epidemiology 138, no. 12 (December 15, 1993): 1057–69. http://dx.doi.org/10.1093/oxfordjournals.aje.a116824.

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Kovacsovics, T., J. Tschopp, A. Kress, and H. Isliker. "Antibody-independent activation of C1, the first component of complement, by cardiolipin." Journal of Immunology 135, no. 4 (October 1, 1985): 2695–700. http://dx.doi.org/10.4049/jimmunol.135.4.2695.

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Abstract Lipid vesicles containing phospholipids known to be present in substantial amounts in mitochondrial membranes were tested for their capacity to activate C1. Among them, only cardiolipin (CL) was highly efficient in C1 activation; no such effect was observed with phosphatidylcholine, phosphatidylethanolamine, or phosphatidylinositol. CL was shown to bind specifically C1q, because only unlabeled C1q competed with 125I-C1q for binding to CL. The requirement for C1q was confirmed by the finding that only fully reconstituted macromolecular C1, containing C1q, was activated by CL. The specificity of CL-induced activation of C1 was also demonstrated by introducing adriamycin, an agent known to interact with CL. Whereas adriamycin did not decrease C1 activation induced by immune complexes, it abrogated C1 activation by CL. The latter was shown to be a strong nonimmune activator of C1, because C1-INH did not inhibit CL-induced activation. When the concentration of CL in vesicles was decreased in the presence of phosphatidylcholine, C1 activation was detected only above a critical level of 35 mol% CL, compatible with a minimal density or clustering of CL molecules in the plane of the membrane. Moreover, C1 activation by CL was modulated by the addition of cholesterol. The threshold of CL required for C1 activation was lowered by the incorporation of more than 35 mol% cholesterol into the vesicles. These results show that CL incorporated into liposomes can be a potent nonimmune activator of C1. The negatively charged phosphate groups in CL are likely candidates for Clq-binding.

Journal articles on the topic 'Cardiolipin antibody'

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