Tags

Type your tag names separated by a space and hit enter

Gastric parietal cell antigens of 60-90, 92, and 100-120 kDa associated with autoimmune gastritis and pernicious anemia. Role of N-glycans in the structure and antigenicity of the 60-90-kDa component.
J Biol Chem. 1989 Nov 05; 264(31):18768-74.JB

Abstract

Thirty-four human sera containing parietal cell autoantibodies (PCA) specifically immunoprecipitated two antigens, with apparent molecular masses of 60-90 kDa and 100-120 kDa under nonreducing conditions and 60-90 kDa and 120-150 kDa under reducing conditions, from porcine gastric membrane extracts. A third antigen of 92 kDa was only observed in immunoprecipitates analyzed under reducing conditions. By immunoblotting, 24 of the 34 PCA-positive sera reacted with only the 60-90-kDa antigen, three reacted with a broad 60-120-kDa smear, one reacted only with a 92-kDa antigen and six did not react. Reactivity with the 60-90-kDa antigen was observed with gastric membranes from dog, pig, rat, and rabbit. Twenty PCA-negative sera did not react with these components by immunoprecipitation or immunoblotting. PCA reactivity with the 60-90-kDa antigen was abolished when the gastric membranes were (a) digested with Pronase, (b) reduced with 100 mM dithiothreitol, (c) treated with sodium periodate, or (d) digested with N-glycanase. The 60-90-kDa and 100-120-kDa components were insensitive to neuraminidase treatment. N-glycanase digestion of 125I-labeled antigens purified by immunoprecipitation and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis collapsed the 60-90-kDa antigen to a sharp 34-kDa band; the 100-120-kDa component was unaffected. These observations suggest that (i) parietal cell antigens comprise three components of 60-90, 92, and 100-120 kDa; (ii) the epitopes differ in conformational sensitivity; (iii) the 60-90-kDa antigen is a conserved molecule comprising a 34-kDa core protein extensively glycosylated with N-linked oligosaccharides; (iv) sialic acid residues are not present in the 60-90- and 100-120-kDa molecules, and (v) the carbohydrate and protein moieties of the 60-90-kDa molecule are required for antibody binding.

Authors+Show Affiliations

Department of Pathology and Immunology, Monash University Medical School, Prahran, Victoria, Australia.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

2478551

Citation

Goldkorn, I, et al. "Gastric Parietal Cell Antigens of 60-90, 92, and 100-120 kDa Associated With Autoimmune Gastritis and Pernicious Anemia. Role of N-glycans in the Structure and Antigenicity of the 60-90-kDa Component." The Journal of Biological Chemistry, vol. 264, no. 31, 1989, pp. 18768-74.
Goldkorn I, Gleeson PA, Toh BH. Gastric parietal cell antigens of 60-90, 92, and 100-120 kDa associated with autoimmune gastritis and pernicious anemia. Role of N-glycans in the structure and antigenicity of the 60-90-kDa component. J Biol Chem. 1989;264(31):18768-74.
Goldkorn, I., Gleeson, P. A., & Toh, B. H. (1989). Gastric parietal cell antigens of 60-90, 92, and 100-120 kDa associated with autoimmune gastritis and pernicious anemia. Role of N-glycans in the structure and antigenicity of the 60-90-kDa component. The Journal of Biological Chemistry, 264(31), 18768-74.
Goldkorn I, Gleeson PA, Toh BH. Gastric Parietal Cell Antigens of 60-90, 92, and 100-120 kDa Associated With Autoimmune Gastritis and Pernicious Anemia. Role of N-glycans in the Structure and Antigenicity of the 60-90-kDa Component. J Biol Chem. 1989 Nov 5;264(31):18768-74. PubMed PMID: 2478551.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Gastric parietal cell antigens of 60-90, 92, and 100-120 kDa associated with autoimmune gastritis and pernicious anemia. Role of N-glycans in the structure and antigenicity of the 60-90-kDa component. AU - Goldkorn,I, AU - Gleeson,P A, AU - Toh,B H, PY - 1989/11/5/pubmed PY - 1989/11/5/medline PY - 1989/11/5/entrez SP - 18768 EP - 74 JF - The Journal of biological chemistry JO - J Biol Chem VL - 264 IS - 31 N2 - Thirty-four human sera containing parietal cell autoantibodies (PCA) specifically immunoprecipitated two antigens, with apparent molecular masses of 60-90 kDa and 100-120 kDa under nonreducing conditions and 60-90 kDa and 120-150 kDa under reducing conditions, from porcine gastric membrane extracts. A third antigen of 92 kDa was only observed in immunoprecipitates analyzed under reducing conditions. By immunoblotting, 24 of the 34 PCA-positive sera reacted with only the 60-90-kDa antigen, three reacted with a broad 60-120-kDa smear, one reacted only with a 92-kDa antigen and six did not react. Reactivity with the 60-90-kDa antigen was observed with gastric membranes from dog, pig, rat, and rabbit. Twenty PCA-negative sera did not react with these components by immunoprecipitation or immunoblotting. PCA reactivity with the 60-90-kDa antigen was abolished when the gastric membranes were (a) digested with Pronase, (b) reduced with 100 mM dithiothreitol, (c) treated with sodium periodate, or (d) digested with N-glycanase. The 60-90-kDa and 100-120-kDa components were insensitive to neuraminidase treatment. N-glycanase digestion of 125I-labeled antigens purified by immunoprecipitation and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis collapsed the 60-90-kDa antigen to a sharp 34-kDa band; the 100-120-kDa component was unaffected. These observations suggest that (i) parietal cell antigens comprise three components of 60-90, 92, and 100-120 kDa; (ii) the epitopes differ in conformational sensitivity; (iii) the 60-90-kDa antigen is a conserved molecule comprising a 34-kDa core protein extensively glycosylated with N-linked oligosaccharides; (iv) sialic acid residues are not present in the 60-90- and 100-120-kDa molecules, and (v) the carbohydrate and protein moieties of the 60-90-kDa molecule are required for antibody binding. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/2478551/Gastric_parietal_cell_antigens_of_60_90_92_and_100_120_kDa_associated_with_autoimmune_gastritis_and_pernicious_anemia__Role_of_N_glycans_in_the_structure_and_antigenicity_of_the_60_90_kDa_component_ DB - PRIME DP - Unbound Medicine ER -