1989 Fiscal Year Final Research Report Summary
Transformational Alteration of Human pancreatic Gamma-Glutamyl-transpeptidase (gamma-GTP)
| Project/Area Number |
63570318
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Gastroenterology
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| Research Institution | Kanazawa University |
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Principal Investigator |
SAWABU Norio Kanazawa University, Cancer, Research Institute, Professor, がん研究所, 教授 (90019969)
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| Project Period (FY) |
1988 – 1989
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| Keywords | gamma-GTP / Pancreatic Cancer / Sugar chain / Hepatocellular Carcinoma / Monoclonal antibody / Transformational alteration |
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| Research Abstract |
To elucidate the specific changes of pancreatic gamma-glutamltranspeptidase (gamma-GTP) associated with malignant transformation, some properties of gama-GTP purified from pancreatic cancer were compared with those of gamma-GTPs from normal pancreas and other tissues. Four of five pancreatic cancer gamma-GTPs showed distinctly slower electrophoretic mobility than the normal enzymes. Isoelectric points of pancreatic cancer gamma-GTPs varied in each case, but all of them were higher than those of normal enzymes. This difference in isoelectric points of gamma-GTPs between cancerous tissue and normal tissue was reduced by neuraminidase treatment. Lectin affinity chromatography revealed two of five pancreatic cancer gamma-GTPs with a greater affinity to concanavalin A (Con A) than normal pancreas gamma-GTPs. Four of five pancreatic cancer gamma-GTPs had a greater affinity to Lens culinaris agglutinin (LCA) than normal pancreas gamma-GTPs. Normal pancreas had little affinity to phaseolus vul
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garis erythroagglutinating (E-PHA), but two of five pancreatic cancer gamma-GTPs had an apparent affinity to E-PHA and one of them had a slight affinity to E-PHA. These results indicate that the transformational changes of pancreatic cancer gamma-GTP are mainly induced in the sugar chains of the enzyme molecules resulting in a lower content of sialic acid and higher content of fucose and bisecting GlcNAc residue as compared with the normal pancreatic enzymes.
Furthermore, to develop the monoclonal antibody (MAb) that recognize the specific alteration of sugar chain of pancreatic cancer gamma-GTP, we prepared the MAb against gamma-GTP from pancreatia cancer using the hybridoma technique. All of the MAbs were reactive with gamma-GTPs from not only pancreatic cancers but also other tissues, and could not recognize sugar chain but peptide portion of gamma-GTP. This is considered to be due to the fact that the immunogenicity of sugar chain can be weaker in comparison with that of peptide portion. We are now preparing the specific MAb, considering a new device. Less
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Research Products
(14 results)
