A new enzyme-linked lectin/mucin antibody sandwich assay (CAM 17.1/ WGA) assessed in combination with CA 19-9 and peanut lectin binding assay for the diagnosis of pancreatic cancer

Abstract

Background. Mucus glycoproteins are often present in the sera of patients with pancreatic cancer, and their detection and quantification can be used in serologic diagnosis. Methods. A novel enzyme‐linked “sandwich” assay (CAM 17.1/WGA) has been developed in which a lectin, wheat germ agglutinin (WGA), is bound to the solid phase to capture serum glycoproteins, and after addition of test sera, a monoclonal antimucin antibody (CAM 17.1) and peroxidase‐tagged second antibody are used as a detection system. Results. The test has been applied to sera from 79 patients with pancreatic cancer and 120 controls. The CAM 17.1/WGA assay alone had a sensitivity of 78% and specificity of 76% in the diagnosis of pancreatic cancer. Combination of the CAM 17.1/WGA test with a previously described peanut lectin binding assay (PNA/ELLA) provided a sensitivity of 92% and specificity of 70%, whereas combination of the CAM 17.1/WGA assay with the CA 19‐9 radioimmunoassay had a sensitivity of 85% and specificity of 76%. Combination of all three tests had a sensitivity of 94% and specificity of 66%. In nonjaundiced patients, the combination of CAM 17.1/WGA and PNA/ELLA had a sensitivity of 93% and specificity of 79% in the diagnosis of pancreatic cancer. Conclusions. This new test adds significantly to the armamentarium of serologic tests for pancreatic cancer. These tests are particularly effective when used in combination to detect different mucin‐borne carbohydrate antigens. They deserve more widespread use, particularly in examining nonjaundiced patients with unexplained abdominal pain or weight loss.

Anti-T antibodies and peanut-agglutinin-binding glycoproteins in sera of patients with gastric cancer

“…It has been used as a capture system for the detection of mucinous glycoproteins (Parker et al 1992;Langkilde et al 1992). Because of the diversity of carbohydrate structure carried by the tumor-related mucins (Hounsell et al 1985), it might be appropriate to use a combination of tests rather than relying on detection of a single epitope.…”

“…Our method could detect at least 30 ng/ml natural PNA-binding glycoprotein (asialoglycophorin), and this result is comparable to a radioimmunoassay using PNA (King and Holburn 1979). Although monoclonal antibodies are highly speci®c for detecting the T-antigen in serum (Samuel et al 1990;Kawa et al 1991;Parker et al 1992), the sandwich enzyme-linked lectin assay we used in this study has some advantages over the radioimmunoassays using monoclonal antibodies. Lectins are readily available, inexpensive and speci®c, and the use of a radioisotope can be avoided.…”

Morphological and molecular characterization of human gastric mucous cells in long-term primary culture

“…Lectins enable characterization of the terminal glycosylation of glycoproteins through agglutination to specific terminal carbohydrates [29,36]. In the present paper we have shown by lectin-ELISA that the secreted glycoproteins of primary cultured human gastric mucous cells bind to specific lectins that are characteristic for gastric mucins.…”

Detection of Infectious Bronchitis Virus and Specific Anti- Viral Antibodies Using a Concanavalin A–Sandwich–ELISA

“…They are stable and can provide an extraordinarily sensitive detection system of glycosylation and carbohydrate sites (14). The lectin-ELISA has been used for the diagnosis of pancreatic cancer, human immunodeficience virus (HIV) and feline immunodeficiency virus (FIV), revealing to be highly sensitive and feasible (9,23,26,30). Despite their specificity and efficacy as glycoprotein binders, lectins have not been used on enzyme immunoassays for the diagnosis of coronaviruses, including IBV, or even other avian viral pathogens.…”