Phytohemagglutinin-L (PHA-L) lectin surface binding of N-linked beta 1-6 carbohydrate and its relationship to activated mutant ras in human pancreatic cancer cell lines

Cancer Letters
R E SchwarzP B Paty

Abstract

Alterations of the N-linked carbohydrate core structure of cell surface glycoproteins (beta 1-6 branching) can be detected by phytohemagglutinin (PHA-L) lectin binding and has been linked to tumor progression and K-ras activation in colon cancer. The purpose of this study was to determine the prevalence of this carbohydrate alteration and its relationship to K-ras activation in pancreatic cancer. Nine human pancreatic cancer cell lines and 4 colon lines as controls were grown under standard tissue culture conditions. K-ras genome analysis was performed by polymerase chain reaction amplification and sequencing. The proportion of cellular p21-ras bound to GTP (ras-GTP level) was determined using immunoprecipitation of 32P-labeled cell lysates followed by thin layer chromatography and phosphoimaging analysis. Lectin blot analysis was performed on crude membrane preparations. Sensitivity to lectins was assessed with cell culture thymidine incorporation. Of 9 pancreatic cancer lines tested, 3 had wild type K-ras, 2 had heterozygous and 4 had homozygous mutations in codon 12 of K-ras. These genotypes correlated strongly with the level of ras-GTP measured. K-ras mutants had increased levels of ras-GTP compared to wild-type cell lines....Continue Reading

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Citations

Jul 5, 2012·Molecular & Cellular Proteomics : MCP·Putty-Reddy SudhirChung-Hsuan Chen
Feb 13, 2001·Biochemical and Biophysical Research Communications·M T Yip-SchneiderM S Marshall
Sep 1, 1999·British Journal of Cancer·R E SchwarzP B Paty
Sep 13, 2019·International Journal of Molecular Sciences·Enikő SzabóLászló Kovács
Jun 9, 2020·BioMed Research International·Milena Mazalovska, J Calvin Kouokam
May 26, 2004·Biochimica Et Biophysica Acta·Susan L Bellis

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