Autism-specific maternal autoantibodies recognize critical proteins in developing brain.

Autism spectrum disorders (ASDs) are neurodevelopmental in origin, affecting an estimated 1 in 88 children in the United States. We previously described ASD-specific maternal autoantibodies that recognize fetal brain antigens. Herein, we demonstrate that lactate dehydrogenase A and B (LDH), cypin, stress-induced phosphoprotein 1 (STIP1), collapsin response mediator proteins 1 and 2 (CRMP1, CRMP2) and Y-box-binding protein to comprise the seven primary antigens of maternal autoantibody-related (MAR) autism. Exclusive reactivity to specific antigen combinations was noted in 23% of mothers of ASD children and only 1% of controls. ASD children from mothers with specific reactivity to LDH, STIP1 and CRMP1 and/or cypin (7% vs 0% in controls; P<0.0002; odds ratios of 24.2 (95% confidence interval: 1.45-405)) had elevated stereotypical behaviors compared with ASD children from mothers lacking these antibodies. We describe the first panel of clinically significant biomarkers with over 99% specificity for autism risk thereby advancing our understanding of the etiologic mechanisms and therapeutic possibilities for MAR autism.

[Antibodies to enzymes of purine metabolism as a factor of gastrointestinal tract lesions in systemic scleroderma].

Antibodies to Adenosine Deaminase (AD) and Guanin Deaminase (GDA) were founded in sera of systemic sclerosis (SS) patients, their concentration positive correlated with activity of disease. Increased levels of antibodies to AD and GDA correlated with the severity of gastrointestinal tract injury (especially pancreatitis and hepatitis). It is shown that level of antibodies to AD and GDA differs reliable from contents of these antibodies, in sera of healthy persons. It is shown that AD enzymatic activity was decreased, while activity of GDA was increased. The antibodies to enzymes may be one of the possible causes of change of enzymes activity in sera of SS patients. The method of immunoenzyme determination of level of antibodies to AD, G on the basis of immobilized form of magnet sorbent was developed for immune diagnostics of SS.

Purification of human liver guanase and characterization of antibody against it by immunoblotting.

Guanase was purified from human liver and its specific antibody was raised in rabbits. The enzyme was purified 1200-fold from the crude liver extract; the specific activity of the purified enzyme was 91.50 units/mg. The purified enzyme gave two distinct peaks on high pressure liquid ion exchange chromatography. The materials in both peaks had a molecular weight of 100,000, and were concluded to be isozymes with different pH optima for guanine. The antiserum completely inhibited the activity of the liver enzyme. It formed a single precipitin line with the human liver extract. On immunoblotting, it bound specifically to the one band with guanase activity, but to no other bands of protein. Thus, this antiserum for human liver guanase should be suitable for use in immunohistochemical demonstration of guanase and determination of this enzyme by radioimmunoassay.

Characterization of antibody against human liver guanase by immunoblotting and immunohistochemical staining of human liver guanase by a direct labeling antibody-enzyme method.

Human liver guanase was purified and a specific antibody against it was raised in rabbits. The antiserum formed a single precipitin line with human liver extract, and also completely inhibited the activity of the liver enzyme. An immunoblotting study showed that the antibody bound specifically to one band of protein with guanase activity and not to other proteins. Therefore, we concluded that this antiserum against the liver enzyme was suitable for use in immunohistochemical demonstration of guanase. In tissue sections, the immunohistochemical reaction with this antibody was positive in the same locations as the histochemical guanase reaction with DAB (3,3'-diaminobenzidine tetrahydrochloride).