Monoclonal antibody against a cryptic carbohydrate antigen of murine and human lymphocytes. I. antigen expression in non-cryptic or unsubstituted form on certain murine lymphomas, on a spontaneous murine mammary carcinoma, and on several human adenocarcinomas
✍ Scribed by B. Michael Longenecker; A. F. Raisur Rahman; J. Barrington Leigh; Ross A. Purser; Arnold H. Greenberg; D. J. Willans; O. Keller; P. K. Petrik; T. Y. Thay; M. R. Suresh; A. A. Noujaim
- Publisher
- John Wiley and Sons
- Year
- 1984
- Tongue
- French
- Weight
- 777 KB
- Volume
- 33
- Category
- Article
- ISSN
- 0020-7136
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✦ Synopsis
Abstract
This paper describes an IgM monoclonal antibody (49H.8) which was produced following immunization of BALB/c mice with human neuraminidase‐treated erythrocytes (NE‐RBC). 49H.8 reacts with NE‐RBC, neuraminidase‐treated T lymphocytes (NE‐T) and NE B lymphocytes of both human and murine origin. Little or no reactivity with untreated T or B cells could be detected. Thus the 49H.8 antigen is ‚cryptic’︁ in most normal lymphocytes of both humans and mice. In contrast, the 49H.8 antigen was detected in non‐cryptic or unsubstituted form on many non‐treated murine lymphomas of both B‐ and T‐cell origin, on the spontaneous murine mammary carcinoma, TA3‐HA and on serveral human adenocarcinomas. The 49H.8 antigen appears to be related to the previously described 49H.24 antigen as shown by sugar inhibition experiments. 49H.24 reacts most strongly with the synthetic disaccharide (betaGal (1→3)alphaGalNAc) but not at all with betaGal (1→3)betaGalNac, 49H.24 does not react with any of the murine or human tumors tested. 49H.8 reacts with both the alpha and beta forms of the disaccharide but reacts most strongly with phenyl‐betagalactoside‐containing compounds. In contrast, phenylalpha‐galactoside‐containing compounds produced no reaction. The natural determinant detected by this antibody was not determined but various possibilities are considered. 49H.8 was used to detected antigen apparently shed from growing TA3‐Ha cells into the serum and ascites of tumor‐bearing mice. These observations suggest that the 49H.8 monoclonal antibody will be valuable as a specific reagent for a common tumor‐associated antigen shared by certain murine and human tumors, and as a means of assaying shed tumor antigen in circulation as in the TA3‐Ha mammary adenocarcinoma model.