| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Department of Biochemistry, Sasaki Institute, Tokyo 101 [T. O., K. Y]; Department of Biology, Faculty of Education, Gunma University, Gunma 371 [N. K.]; Department of Internal Medicine, Hyogo College of Medicine, Hyogo 663 [T. H., K. H., T. O.]; and Department of Internal Medicine, Okayama University School of Medicine, Okayama 700 [N. K.], Japan
2 To whom requests for reprints should be addressed.
Serum cholinesterase (ChE) (E.C. 3.1.1.8) is a glycoprotein which has 36 potential sites of asparagine-N-linked sugar chains. The structures of oligosaccharides released from ChE on hydrazinolysis were studied by serial lectin affinity column chromatography, exoglycosidase digestion, and methylation analysis. Seventy-three % of the sugar chains occurred as biantennary oligosaccharides and the remainder as C-2 and C-2,4/C-2,6 branched tri- and tetraantennary oligosaccharides. Several percentages of the Lewis X antigenic determinant and fucosylated mannose core were linked to them, and their sialic acid residues were linked to nonreducing terminal galactose residues at the C-3 and C-6 positions.
Aleuria aurantia lectin-reactive ChE with the Lewis X antigenic determinant increased in hepatocellular carcinomas and liver cirrhosis compared with chronic hepatitis; on the other hand, Aleuria aurantia lectin-reactive ChE did not change significantly after transcatheter arterial embolization and was not related to the serum levels of
-fetoprotein and carcinoembryonic antigen in patients with hepatocellular carcinomas. Accordingly, the analysis of Aleuria aurantia lectin-reactive ChE is clinically useful for differentiating liver cirrhosis from chronic hepatitis and to identify high risk groups for hepatocellular carcinomas, i.e., cirrhotic patients in Child's A grade.
1 This work was supported by a Grant-in-Aid for Cancer Research from the Ministry of Education, Science and Culture, and Special Funds from the Science and Technology Agency of the Japanese Government.
The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
Received 6/17/93. Accepted 10/29/93.
This article has been cited by other articles:
![]() |
K. Fukushima, Y. Ikehara, M. Kanai, N. Kochibe, M. Kuroki, and K. Yamashita A {beta}-N-Acetylglucosaminyl Phosphate Diester Residue Is Attached to the Glycosylphosphatidylinositol Anchor of Human Placental Alkaline Phosphatase: A TARGET OF THE CHANNEL-FORMING TOXIN AEROLYSIN J. Biol. Chem., September 19, 2003; 278(38): 36296 - 36303. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Saxena, Y. Ashani, L. Raveh, D. Stevenson, T. Patel, and B. P. Doctor Role of Oligosaccharides in the Pharmacokinetics of Tissue-Derived and Genetically Engineered Cholinesterases Mol. Pharmacol., January 1, 1998; 53(1): 112 - 122. [Abstract] [Full Text] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Cancer Research | Clinical Cancer Research |
| Cancer Epidemiology Biomarkers & Prevention | Molecular Cancer Therapeutics |
| Molecular Cancer Research | Cancer Prevention Research |
| Cancer Prevention Journals Portal | Cancer Reviews Online |
| Annual Meeting Education Book | Meeting Abstracts Online |