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Aberrant Elevation of Tyrosine‐specific Phosphorylation in Human Gastric Cancer Cells
Phosphotyrosine‐containing proteins in various human cancer cell lines were studied by immunoblotting with anti‐phosphotyrosine antibody. Of 29 cell lines derived from oral epidermoid cancer, esophageal cancer, gastric cancer, colon cancer, pancreatic cancer, hepatocellular carcinoma and malignant m...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Blackwell Publishing Ltd
1991
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5918361/ https://www.ncbi.nlm.nih.gov/pubmed/1778766 http://dx.doi.org/10.1111/j.1349-7006.1991.tb01816.x |
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author | Takeshima, Eisuke Hamaguchi, Michinari Watanabe, Tadashi Akiyama, Seiji Kataoka, Masato Ohnishi, Yukano Xiao, Hengyi Nagai, Yoshiyuki Hiroshi, Hiroshi |
author_facet | Takeshima, Eisuke Hamaguchi, Michinari Watanabe, Tadashi Akiyama, Seiji Kataoka, Masato Ohnishi, Yukano Xiao, Hengyi Nagai, Yoshiyuki Hiroshi, Hiroshi |
author_sort | Takeshima, Eisuke |
collection | PubMed |
description | Phosphotyrosine‐containing proteins in various human cancer cell lines were studied by immunoblotting with anti‐phosphotyrosine antibody. Of 29 cell lines derived from oral epidermoid cancer, esophageal cancer, gastric cancer, colon cancer, pancreatic cancer, hepatocellular carcinoma and malignant melanoma, 3 of the 6 gastric cancer cells showed aberrant elevation of tyrosine‐speciflc phosphorylation. On the other hand, both esophageal cancer cells and colon cancer cells, which were reported to have amplified epidermal growth factor receptor and activated p60(v‐src) kinase, respectively, showed no apparent elevation of tyrosine‐specific phosphorylation, and their profiles of phosphorylation were similar to that of normal human fibroblasts. Two gastric cancer cells, NUGC‐4 and MKN‐45, showed similar profiles of phosphorylation but their responses to growth factors differed from each other. Tyrosine phosphorylation in NUGC‐4 was strongly activated by treatment with epidermal growth factor and quickly reduced by the acid treatment which is effective in removing growth factors from cellular surface receptors. On the contrary, phosphorylation in MKN‐45 did not respond to either growth factor or acid treatment. These results suggest that NUGC‐4 and MKN‐45 have tyrosine kinases which are activated by different mechanisms but share similar substrates. |
format | Online Article Text |
id | pubmed-5918361 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1991 |
publisher | Blackwell Publishing Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-59183612018-05-11 Aberrant Elevation of Tyrosine‐specific Phosphorylation in Human Gastric Cancer Cells Takeshima, Eisuke Hamaguchi, Michinari Watanabe, Tadashi Akiyama, Seiji Kataoka, Masato Ohnishi, Yukano Xiao, Hengyi Nagai, Yoshiyuki Hiroshi, Hiroshi Jpn J Cancer Res Article Phosphotyrosine‐containing proteins in various human cancer cell lines were studied by immunoblotting with anti‐phosphotyrosine antibody. Of 29 cell lines derived from oral epidermoid cancer, esophageal cancer, gastric cancer, colon cancer, pancreatic cancer, hepatocellular carcinoma and malignant melanoma, 3 of the 6 gastric cancer cells showed aberrant elevation of tyrosine‐speciflc phosphorylation. On the other hand, both esophageal cancer cells and colon cancer cells, which were reported to have amplified epidermal growth factor receptor and activated p60(v‐src) kinase, respectively, showed no apparent elevation of tyrosine‐specific phosphorylation, and their profiles of phosphorylation were similar to that of normal human fibroblasts. Two gastric cancer cells, NUGC‐4 and MKN‐45, showed similar profiles of phosphorylation but their responses to growth factors differed from each other. Tyrosine phosphorylation in NUGC‐4 was strongly activated by treatment with epidermal growth factor and quickly reduced by the acid treatment which is effective in removing growth factors from cellular surface receptors. On the contrary, phosphorylation in MKN‐45 did not respond to either growth factor or acid treatment. These results suggest that NUGC‐4 and MKN‐45 have tyrosine kinases which are activated by different mechanisms but share similar substrates. Blackwell Publishing Ltd 1991-12 /pmc/articles/PMC5918361/ /pubmed/1778766 http://dx.doi.org/10.1111/j.1349-7006.1991.tb01816.x Text en |
spellingShingle | Article Takeshima, Eisuke Hamaguchi, Michinari Watanabe, Tadashi Akiyama, Seiji Kataoka, Masato Ohnishi, Yukano Xiao, Hengyi Nagai, Yoshiyuki Hiroshi, Hiroshi Aberrant Elevation of Tyrosine‐specific Phosphorylation in Human Gastric Cancer Cells |
title | Aberrant Elevation of Tyrosine‐specific Phosphorylation in Human Gastric Cancer Cells |
title_full | Aberrant Elevation of Tyrosine‐specific Phosphorylation in Human Gastric Cancer Cells |
title_fullStr | Aberrant Elevation of Tyrosine‐specific Phosphorylation in Human Gastric Cancer Cells |
title_full_unstemmed | Aberrant Elevation of Tyrosine‐specific Phosphorylation in Human Gastric Cancer Cells |
title_short | Aberrant Elevation of Tyrosine‐specific Phosphorylation in Human Gastric Cancer Cells |
title_sort | aberrant elevation of tyrosine‐specific phosphorylation in human gastric cancer cells |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5918361/ https://www.ncbi.nlm.nih.gov/pubmed/1778766 http://dx.doi.org/10.1111/j.1349-7006.1991.tb01816.x |
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