Poly (alpha 2,8-deaminoneuraminic acid) is expressed in lung on a single 150-kDa glycoprotein and is an oncodevelopmental antigen.
- 20 August 1996
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 93 (17) , 8995-8998
- https://doi.org/10.1073/pnas.93.17.8995
Abstract
Homopolymers of alpha 2,8-linked N-acetylneuraminic acid [poly(alpha 2,8-Neu5Ac)] of the neural cell adhesion molecule NCAM have been shown to be temporally expressed during lung development and represent a marker for small cell lung carcinoma. We report the presence of a further polysialic acid in lung that consists of oligo/polymers of alpha 2,8-linked deaminoneuraminic acid residues [poly (alpha 2,8-KDN)], as detected with a monoclonal antibody in conjunction with a specific sialidase. Although the various cell types forming the bronchi, alveolar septs, and blood vessels were positive for poly (alpha 2,8-KDN) by immunohistochemistry, this polysialic acid was found on a single 150-kDa glycoprotein by immunoblot analysis. The poly(alpha 2,8-KDN)-bearing glycoprotein was not related to an NCAM protein based on immunochemical criteria. The expression of the poly (alpha 2,8-KDN) was developmentally regulated as evidenced by its gradual disappearance in the rat lung parenchyma commencing 1 week after birth. In adult lung the blood vessel endothelia and the smooth muscle fibers of both blood vessels and bronchi were positive but not the bronchial and alveolar epithelium. The poly (alpha 2,8-KDN)-bearing 150-kDa glycoprotein became reexpressed in various histological types of lung carcinomas and cell lines derived from them and represents a new oncodevelopmental antigen in lung.Keywords
This publication has 36 references indexed in Scilit:
- Polysialic acid of the neural cell adhesion molecule (N-CAM) is widely expressed during organogenesis in mesodermal and endodermal derivativesDifferentiation, 1994
- Identification and Structural Determination of the KDN-Containing N-Linked Glycan Chains Consisting of Bi- and Triantennary Complex-Type Units of KDN-Glycoprotein Previously Isolated from Rainbow Trout Vitelline EnvelopesBiochemistry, 1994
- Calcium Ion Binding of Three Different Types of Oligo/Polysialic Acids As Studied by Equilibrium Dialysis and Circular Dichroic MethodsBiochemistry, 1994
- Inactivation of the N-CAM gene in mice results in size reduction of the olfactory bulb and deficits in spatial learningNature, 1994
- The neural cell adhesion molecule N-CAM enhances L1-dependent cell-cell interactions.The Journal of cell biology, 1990
- Isolation and characterization of deaminated neuraminic acid-rich glycoprotein (KDN-gp-OF) in the ovarian fluid of rainbow trout (Salmogairdneri)Biochemical and Biophysical Research Communications, 1989
- Expression of the embryonal neural cell adhesion molecule N‐CAM in lung carcinoma. Diagnostic usefulness of monoclonal antibody 735 for the distinction between small cell lung cancer and non‐small cell lung cancerThe Journal of Pathology, 1989
- KDN-glycoprotein: A novel deaminated neuraminic acid-rich glycoprotein isolated from vitelline envelope of rainbow trout eggsBiochemical and Biophysical Research Communications, 1988
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970