Patent autoantibodies to cardiolipin in healthy human serum

Saenko, Vladimir; Rott, G. M.; Poverennyi, A. M.

doi:10.1007/bf00833813

Cited by 6 publications

(5 citation statements)

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“…It has previously been suggested that the interaction with DNA of so-called "cryptic" antibodies obtained after ion exchange chromatography is determined by a cofactor of non-immunoglobulin nature [5]. Our studies supported this hypothesis and demonstrated the chemical nature of this cofactor.…”

Section: Resultssupporting

confidence: 86%

“…This interaction is explained by the suggestion that the gamma-globulin pool contains cryptic natural anti-DNA antibodies which are liberated from complexes using QAE-Sephadex [2]. The properties of these "cryptic" antibodies have been studied over the last 20 years, including their interactions with many negatively charged biological structures (cardiolipin, lipopolysaccharides, phospholipids, DNA, sialic acids, etc.…”

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confidence: 99%

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Immunoglobulin: DNA cofactor interaction

2007

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The reasons for the appearance of DNA-binding activity of immunoglobulins (Ig) after chromatography on anion-exchange Sephadexes were studied. Elution of Ig from these Sephadexes with 0.5 M NaCl was found, using an orcinol method, to be associated with degradation of the matrix, with the appearance of water-soluble fragments (WSF) of Sephadex in the eluate. Degradation of the Sephadex matrix also occurred on washing of unloaded Sephadex. Monoclonal antibodies which did not initially interact with DNA acquired the ability to react with DNA after incubation with Sephadex WSF, as demonstrated using immunoenzyme analysis. It is suggested that the WSF forming on passage of Ig through anion exchange Sephadex columns interact with Ig to generate cations which can react with negatively charged antigens and, particularly DNA. 289 0091-150X/07/4106-0289

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Section: Resultssupporting

confidence: 86%

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confidence: 99%

Immunoglobulin: DNA cofactor interaction

2007

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“…Anticardiolipin antibodies react with antigen only after gel-filtration on Sephadex G-200 (pH 4.5) or ion-exchange chromatography [2], which was confirmed by others [3].…”

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confidence: 71%

Anticardiolipin antibodies dissociate from protein in thermal shock

et al. 1996

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Anticardiolipin antibodies are revealed in rat serum by solid-phase immunoenzyme assay 3 h after thermal burn of 30% of the body surface. An increase in serum concentration of the antibody after thermal burn may be due to dissociation of the antibody-protein complex. Key Words: masked antibodies; cardiolipin; thermal shock; immunoenzyme assayIt was demonstrated that an increase in serum concentration of anticardiolipin antibodies is associated with higher probability of thrombosis, spontaneous abortions, thrombocytopenia [4], stroke, and myocardial infarction [6]. Clinical manifestations associated with increased concentration of anticardiolipin antibodies were termed the antiphospholipid syndrome [5].We showed that a considerable amount of anticardiolipin antibodies in serum of healthy persons is inactivated, i.e., these antibodies are bound to serum proteins (masked). Anticardiolipin antibodies react with antigen only after gel-filtration on Sephadex G-200 (pH 4.5) or ion-exchange chromatography [2], which was confirmed by others [3].A question arises whether anticardiolipin antibodies dissociate from protein and exert their effects in vivo?We hypothesized that these antibodies dissociate under conditions of shock. While studying the properties of masked antibodies which react with bacterial endotoxins, we found that the activity of these antibodies in the serum markedly increases at the early stages of traumatic shock [ 1 ].In the present study the activity of antibodies reacting with cardiolipin was studied in rats with burn shock. Department of Radiation Biochemistry, Laboratory for the MDdeling of Radiation and Nonradiation Effects, Medical Radiology Research Center, Russian Academy of Medical Sciences, Obninsk MATERIALS AND METHODSExperiments were performed on male Wistar rats weighing 180-200 g. A IIIB degree thermal burn of 30% body surface was produced by exposure of sheared back to light from an electrical bulb. Serum was prepared 3 h after the exposure. Serum from intact rats served as the control.Solid-phase immunoassay was performed as follows. Ethanol solution of cardiolipin (50 gl, Sigma) was dried in immunological plates (Nunc) at 4~ overnight. Nonspecific binding sites were blocked by incubation with 0.3% gelatin (100 gl) in phosphate-buffered saline (PBS, pH 7.4) for 2 h at 37~ followed by washing with PBS. Incubation with rat antisera (50 gl, 1:500) was carried out for 1 h at room temperature. After washing with PBS, anticardiolipin antibodies were identified by incubation for 1 h at room temperature with biotinylated sheep anti-anticardiolipin antibodies (50 ~tl, Amersham). Streptavidin-peroxidase conjugate (Amersham) was then added in the corresponding dilution and incubated for 1 h at room temperature. After thorough washing with PBS, incubation with o-phenylenediamine was carried out for 20 min at 37~ The reaction was terminated by the addition of 1 M H,_SO 4, and light absorbance was measured at 492 nm. Three series of experiments were performed; the results were statistically processed.

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“…Thus far, very few studies that analyse the prevalence of ACA in healthy subjects have been reported. 18 An attempt of a systemic analysis of normal subjects, positive for ACA, was made by Villa et al 19 The authors have examined the subjects during a 12 month follow‐up period. Both these studies indicated that different isotypes of ACA are present in normal subjects.…”

Section: Discussionmentioning

confidence: 99%

Anticardiolipin Antibodies In Spontaneously Hypertensive Rats (Shr), Stroke‐Prone Shr And Normal Wistar Rats

Todorova¹,

Baleva²,

Nikolov³

et al. 2000

Clin Exp Pharma Physio

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1. Anticardiolipin antibodies (ACA) can be detected in the serum of patients with autoimmune disturbances, ischaemic heart disease, myocardial infarction, neurological disorders and other medical conditions. Elevated values of these autoantibodies can be associated with recurrent fetal loss, arterial and venous thrombosis and thrombocytopenia. 2. In the present study, we investigated the presence of ACA in three rat strains, namely normal Wistar rats (WR), spontaneously hypertensive rats Okamoto-Aoki (SHR) and stroke-prone SHR (SHRSP). All animals were examined at four ages: 1, 4, 10 and 12 months of age. Anticardiolipin antibodies were determined by ELISA. 3. Anticardiolipin antibody levels in normal WR, which were used as controls, were lowest at 1 month and increased significantly from the 4th month on. At the prehypertensive age (1 month), ACA levels in SHR and SHRSP were significantly higher compared with control WR, decreased with age and were significantly lower at 4, 10 and 12 months compared with age-matched WR. 4. These differences may be a result of immunological disorders in SHR.

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Patent autoantibodies to cardiolipin in healthy human serum

Cited by 6 publications

References 5 publications

Immunoglobulin: DNA cofactor interaction

Immunoglobulin: DNA cofactor interaction

Anticardiolipin antibodies dissociate from protein in thermal shock

Anticardiolipin Antibodies In Spontaneously Hypertensive Rats (Shr), Stroke‐Prone Shr And Normal Wistar Rats

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