IgA With altered carbohydrate structure as a tumor-associated marker in serum of cancer patients
Serum IgA1 contains O‐linked carbohydrate structures, whereas other immuno‐globulins contain only N‐linked structures. An assay was developed which detects IgA1 by measuring the DGalβ(1–3) DGalNAc structures O‐linked to the IgA1 hinge region. Fifty percent of the serum specimens from cancer patients...
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| Published in | Journal of clinical laboratory analysis Vol. 2; no. 4; pp. 225 - 234 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
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New York
Wiley Subscription Services, Inc., A Wiley Company
1988
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| Abstract | Serum IgA1 contains O‐linked carbohydrate structures, whereas other immuno‐globulins contain only N‐linked structures. An assay was developed which detects IgA1 by measuring the DGalβ(1–3) DGalNAc structures O‐linked to the IgA1 hinge region. Fifty percent of the serum specimens from cancer patients tested were elevated compared to 1% of the total normal serum specimens tested by this assay. The assay combines antibody (anti‐human IgA) and lectin and measures the DGalβ(1–3)DGalNAc structure in the IgA1 molecule accessible to lectin binding. Three lectins were compared–the lectins from Bauhinia purpurea alba, Maclura pomifera, and peanut agglutinin (PNA). PNA in the assay discriminated best between serum specimens from normal subjects and cancer patients and was chosen as the lectin component in the assay. The anti‐IgA‐PNA enzyme immunoassay was evaluated in a retrospective study of cancer patients. A panel of 845 serum specimens was tested and the results analyzed at three cutoff R values. The R value of a specimen is the ratio of the assay absorbance obtained for that test specimen with respect to the assay absorbance obtained for a pool of normal human sera. At a cutoff R value of 2.38, 1% normals and 26% benigns were elevated. The following cancer specimens had elevated R values: 52% lung, 60% colon, 43% head and neck, 35% breast, 64% kidney, 38% bladder, 43% prostate, 8% ovarian, and 67% pancreas. Further testing showed a significant percentage of serum specimens from patients with cirrhosis, pancreatitis, or ulcerative colitis also had elevated R values. No correlation of this assay was observed with CEA levels. The results suggest that the carbohydrate structure of serum IgA1 is altered by malignancies and that measurement of this altered IgA may supplement CEA testing. |
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| AbstractList | Serum IgA1 contains O‐linked carbohydrate structures, whereas other immuno‐globulins contain only N‐linked structures. An assay was developed which detects IgA1 by measuring the DGalβ(1–3) DGalNAc structures O‐linked to the IgA1 hinge region. Fifty percent of the serum specimens from cancer patients tested were elevated compared to 1% of the total normal serum specimens tested by this assay. The assay combines antibody (anti‐human IgA) and lectin and measures the DGalβ(1–3)DGalNAc structure in the IgA1 molecule accessible to lectin binding. Three lectins were compared–the lectins from Bauhinia purpurea alba, Maclura pomifera, and peanut agglutinin (PNA). PNA in the assay discriminated best between serum specimens from normal subjects and cancer patients and was chosen as the lectin component in the assay. The anti‐IgA‐PNA enzyme immunoassay was evaluated in a retrospective study of cancer patients. A panel of 845 serum specimens was tested and the results analyzed at three cutoff R values. The R value of a specimen is the ratio of the assay absorbance obtained for that test specimen with respect to the assay absorbance obtained for a pool of normal human sera. At a cutoff R value of 2.38, 1% normals and 26% benigns were elevated. The following cancer specimens had elevated R values: 52% lung, 60% colon, 43% head and neck, 35% breast, 64% kidney, 38% bladder, 43% prostate, 8% ovarian, and 67% pancreas. Further testing showed a significant percentage of serum specimens from patients with cirrhosis, pancreatitis, or ulcerative colitis also had elevated R values. No correlation of this assay was observed with CEA levels. The results suggest that the carbohydrate structure of serum IgA1 is altered by malignancies and that measurement of this altered IgA may supplement CEA testing. Serum IgA 1 contains O‐linked carbohydrate structures, whereas other immuno‐globulins contain only N‐linked structures. An assay was developed which detects IgA 1 by measuring the DGalβ(1–3) DGalNAc structures O‐linked to the IgA 1 hinge region. Fifty percent of the serum specimens from cancer patients tested were elevated compared to 1% of the total normal serum specimens tested by this assay. The assay combines antibody (anti‐human IgA) and lectin and measures the DGalβ(1–3)DGalNAc structure in the IgA 1 molecule accessible to lectin binding. Three lectins were compared–the lectins from Bauhinia purpurea alba, Maclura pomifera , and peanut agglutinin (PNA). PNA in the assay discriminated best between serum specimens from normal subjects and cancer patients and was chosen as the lectin component in the assay. The anti‐IgA‐PNA enzyme immunoassay was evaluated in a retrospective study of cancer patients. A panel of 845 serum specimens was tested and the results analyzed at three cutoff R values. The R value of a specimen is the ratio of the assay absorbance obtained for that test specimen with respect to the assay absorbance obtained for a pool of normal human sera. At a cutoff R value of 2.38, 1% normals and 26% benigns were elevated. The following cancer specimens had elevated R values: 52% lung, 60% colon, 43% head and neck, 35% breast, 64% kidney, 38% bladder, 43% prostate, 8% ovarian, and 67% pancreas. Further testing showed a significant percentage of serum specimens from patients with cirrhosis, pancreatitis, or ulcerative colitis also had elevated R values. No correlation of this assay was observed with CEA levels. The results suggest that the carbohydrate structure of serum IgA 1 is altered by malignancies and that measurement of this altered IgA may supplement CEA testing. Serum IgA sub(1) contains O-linked carbohydrate structures, whereas other immunoglobulins contain only N-linked structures. An assay was developed which detects IgA sub(1) by measuring the DGal beta (1-3) DGalNAc structures O-linked to the IgA sub(1) hinge region. Fifty percent of the serum specimens from cancer patients tested were elevated compared to 1% of the total normal serum specimens tested by this assay. The results suggest that the carbohydrate structure of serum IgA sub(1) is altered by malignancies and that measurement of this altered IgA may supplement CEA testing. |
| Author | Schenck, Jay R. Matias, Matthew S. Henslee, Jerry G. Michael Hass, G. Tomita, Joseph T. Rittenhouse, Harry G. |
| Author_xml | – sequence: 1 givenname: Jerry G. surname: Henslee fullname: Henslee, Jerry G. organization: Cancer and Cell Biology Research, Abbott Diagnostic Division, Abbott Laboratories, North Chicago, Illinois – sequence: 2 givenname: Harry G. surname: Rittenhouse fullname: Rittenhouse, Harry G. organization: Cancer and Cell Biology Research, Abbott Diagnostic Division, Abbott Laboratories, North Chicago, Illinois – sequence: 3 givenname: Matthew S. surname: Matias fullname: Matias, Matthew S. organization: Cancer and Cell Biology Research, Abbott Diagnostic Division, Abbott Laboratories, North Chicago, Illinois – sequence: 4 givenname: G. surname: Michael Hass fullname: Michael Hass, G. organization: Cancer and Cell Biology Research, Abbott Diagnostic Division, Abbott Laboratories, North Chicago, Illinois – sequence: 5 givenname: Jay R. surname: Schenck fullname: Schenck, Jay R. organization: Cancer and Cell Biology Research, Abbott Diagnostic Division, Abbott Laboratories, North Chicago, Illinois – sequence: 6 givenname: Joseph T. surname: Tomita fullname: Tomita, Joseph T. organization: Cancer and Cell Biology Research, Abbott Diagnostic Division, Abbott Laboratories, North Chicago, Illinois |
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| Cites_doi | 10.1002/1097-0142(19870115)59:2<203::AID-CNCR2820590204>3.0.CO;2-P 10.1177/019459988309100205 10.1016/0003-9861(81)90273-3 10.1111/j.1365-2559.1985.tb02783.x 10.1073/pnas.69.12.3673 10.1016/S0008-6215(00)84587-5 10.1172/JCI110777 10.1177/30.2.7037937 10.1093/labmed/16.9.556 10.1016/0003-2697(87)90507-0 10.1002/1097-0142(19811015)48:8<1776::AID-CNCR2820480814>3.0.CO;2-R 10.1093/ajcp/81.5.569 10.1002/ijc.2910370509 10.1042/bst0120754 10.1016/0968-0004(85)90012-X 10.1016/S0021-9258(19)40790-4 10.1016/S0021-9258(19)42101-7 10.1146/annurev.iy.02.040184.000535 10.1073/pnas.79.6.2051 10.1007/BF00222491 10.1136/gut.27.2.117 10.1016/0304-419X(83)90006-9 10.1016/0003-2697(77)90408-0 10.1016/0016-5085(79)90279-8 10.1002/ijc.2910390112 10.1002/1097-0142(19871001)60:7<1636::AID-CNCR2820600736>3.0.CO;2-C 10.1111/j.1432-1033.1981.tb06188.x 10.1016/0003-2697(87)90275-2 10.1177/22.12.1084 10.1056/NEJM198310133091503 10.1042/bst0120591 10.1016/S0008-6215(00)84089-6 10.1038/316452a0 10.1016/S0021-9258(18)34116-4 10.1016/0022-4804(76)90124-4 10.1002/ijc.2910370504 |
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Nakane PK, Kawaoi A: Peroxidase-labeled antibody: A new method Jf conjugation. J Histochem Cytochem 22: 1084-1091, 1974. Pierce-Cretel A, Pamblanco M, Strecker G, Montreuil J, Spik G: Heterogeneity of the glycans O-glycosidically linked to the hinge region of secretory immunoglobulins from human milk. Eur J Biochem 114: 169-178, 1981. Hsu S, Raine L: Versatility of biotin-labeled lectins and avidin-biotin-peroxidase complex for localization of carbohydrate in tissue sections. J Histochem Cytochem 30: 157-161, 1982. Allen HJ, Johnson EAZ, Matta KL: Binding-site specificity of lectins from Bauhinia purpurea alba, Sophora japonica, and Wistaria, floribunda. Carbohydr Res 86: 123-131, 1980. Pekelharing JM, Vissers P, Peters HA, Leijnse B: Lectin-enzyme immunoassay of transferrin sialovariants using immobilized antitrans-ferrin and enzyme-labeled galactose-binding lectin from Ricinus communis. Anal Biochem 165: 320-326, 1987. 1984; 61 1976; 20 1982; 79 1987; 164 1976; 25 1984; 81 1987; 165 1980; 86 1985; 9 1982; 30 1986; 37 1974; 249 1981; 209 1975; 250 1981; 48 1983; 71 1983; 91 1972; 69 1985; 45 1985; 43 1987; 39 1987; 59 1979; 179 1982; 47 1974; 22 1987; 60 1984; 2 1981; 114 1976; 50 1986; 46 1984; 12 1984; 738 1986; 27 1984 1977; 79 1985; 316 1982; 257 1985; 10 1983; 309 1985; 16 Yuan S (e_1_2_1_15_2) 1985; 45 Johnson VG (e_1_2_1_18_2) 1986; 46 Lan MS (e_1_2_1_16_2) 1985; 45 e_1_2_1_40_2 Delacroix DL (e_1_2_1_33_2) 1982; 47 Magnani JL (e_1_2_1_12_2) 1985; 43 Lotan R (e_1_2_1_29_2) 1975; 250 e_1_2_1_45_2 Baenziger J (e_1_2_1_2_2) 1974; 249 e_1_2_1_23_2 Baenziger J (e_1_2_1_3_2) 1974; 249 e_1_2_1_20_2 Mizoguchi A (e_1_2_1_35_2) 1982; 257 e_1_2_1_21_2 e_1_2_1_42_2 e_1_2_1_26_2 e_1_2_1_27_2 Greenstein AJ (e_1_2_1_41_2) 1979; 179 e_1_2_1_24_2 Homburger HA (e_1_2_1_22_2) 1984; 81 e_1_2_1_25_2 e_1_2_1_28_2 Briese V (e_1_2_1_43_2) 1984 e_1_2_1_6_2 e_1_2_1_30_2 e_1_2_1_7_2 e_1_2_1_4_2 e_1_2_1_5_2 e_1_2_1_11_2 e_1_2_1_34_2 e_1_2_1_32_2 e_1_2_1_10_2 e_1_2_1_31_2 e_1_2_1_38_2 e_1_2_1_37_2 e_1_2_1_13_2 e_1_2_1_36_2 e_1_2_1_14_2 e_1_2_1_19_2 e_1_2_1_8_2 e_1_2_1_17_2 Witz IP (e_1_2_1_44_2) 1976 e_1_2_1_9_2 e_1_2_1_39_2 |
| References_xml | – reference: Bast RC, Klug TL, St. John E, Jenison E, Niloff JM, Lazarus H, Berkowitz RS, Leavitt T, Griffiths CT, Parker L, Zurawski VR, Knapp RC: A radioimmunoassay using a monoclonal antibody to monitor the course of epithelial ovarian cancer. N Engl J Med 309: 883-887, 1983. – reference: Smets LA, Van Beek WP: Carbohydrates of the tumor cell surface. Biochim Biophys Acta 738: 237-249, 1984. – reference: Pierce-Cretel A, Pamblanco M, Strecker G, Montreuil J, Spik G: Heterogeneity of the glycans O-glycosidically linked to the hinge region of secretory immunoglobulins from human milk. Eur J Biochem 114: 169-178, 1981. – reference: Delacroix DL, Dive D, Rambaud JC, Vaerman JP: IgA subclasses in various secretions and in serum. Immunology 47: 383-385, 1982. – reference: Mizoguchi A, Mizuochi T, Kobata A: Structures of the carbohydrate moieties of secretory component purified from human milk. J Biol Chem 257: 9612-9621, 1982. – reference: Hsu S, Raine L: Versatility of biotin-labeled lectins and avidin-biotin-peroxidase complex for localization of carbohydrate in tissue sections. J Histochem Cytochem 30: 157-161, 1982. – reference: Hakamori S: Tumor-associated carbohydrate antigens. Annu Rev Immunol 2: 103-126, 1984. – reference: Homburger HA, Casey M, Jacob GL, Klee GG: Measurement of secretory IgA in serum by radioimmunoassay in patients with chronic nonalcoholic liver disease or carcinoma. Am J Clin Pathol 81: 569-574, 1984. – reference: Nakane PK, Kawaoi A: Peroxidase-labeled antibody: A new method Jf conjugation. J Histochem Cytochem 22: 1084-1091, 1974. – reference: Ulrich W, Horvat R, Krisch K: Lectin histochemistry of kidney tumors and its pathomorphological relevance. Histopathology 9: 1037-1050, 1985. – reference: Rittenhouse HG, Manderino GL, Hass GM: Mucin-type glycoproteins as tumor markers. 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| Snippet | Serum IgA1 contains O‐linked carbohydrate structures, whereas other immuno‐globulins contain only N‐linked structures. An assay was developed which detects... Serum IgA 1 contains O‐linked carbohydrate structures, whereas other immuno‐globulins contain only N‐linked structures. An assay was developed which detects... Serum IgA sub(1) contains O-linked carbohydrate structures, whereas other immunoglobulins contain only N-linked structures. An assay was developed which... |
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| SubjectTerms | CEA colon cancer IgA1 lectin-enzyme immunoassay O-glycosidic linkages peanut agglutinin |
| Title | IgA With altered carbohydrate structure as a tumor-associated marker in serum of cancer patients |
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