Affinity of IgG-insulin antibodies to human (recombinant DNA) insulin and porcine insulin in insulin-treated diabetic individuals with and without insulin resistance.
The affinity of human (recombinant DNA) insulin and porcine insulin to preformed IgG-insulin antibodies of insulin-treated diabetic individuals was studied in 29 insulin-treated diabetic patients. The binding of 125I-human insulin and 125I-porcine insulin with antibodies was similar in the group of patients without insulin resistance (N = 25). The sera of insulin-resistant diabetic patients (N = 4), containing very high IgG-insulin immunoglobulins, showed a significantly lower affinity for human insulin compared with porcine insulin (P less than 0.01). All four patients with insulin-antibody-mediated insulin resistance were positive for HLA-DR4, but negative for -DR3, supporting the concept of an immunogenetically transferred anti-insulin immune response in insulin-treated diabetic individuals. Based on the reduced binding of human insulin to IgG-antibodies of very high titers in patients with insulin resistance, a potential therapeutic advantage of human insulin therapy can be expected in such infrequent cases of immunologic insulin resistance.
D000293:Adolescent; D000328:Adult; D000818:Animals; D003922:Diabetes Mellitus, Type 1 / Q000188:drug therapy* / Q000276:immunology; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology*; D007328:Insulin / Q000276:immunology* / Q000627:therapeutic use; D007330:Insulin Antibodies; D007333:Insulin Resistance; D008875:Middle Aged; D011994:Recombinant Proteins / Q000276:immunology / Q000627:therapeutic use; D013552:Swine
D007074:Immunoglobulin G; D007328:Insulin; D007330:Insulin Antibodies; D011994:Recombinant Proteins