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KMID : 0043319980210040378
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Archives of Pharmacal Research
1998 Volume.21 No. 4 p.378 ~ p.384
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Farnesylcysteine Methyltransferase Activity and Ras Protein Expression in Human Stomach Tumor Tissue
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Han Eui-Sik
Noh Sung-Hoon
Han Beom-Seok
Oh Hye-Young
Ha Kwang-Won
Hong Sung-Youl
Hong Seok-Min
Han Jung-Whwan
Lee Hyang-Woo
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Abstract
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The processing pathway of G-proteins and Ras family proteins includes the isoprenylation of the cysteine residue, followed by proteolysis of three terminal residues and .alpha.-carboxyl methyl esterification of the cysteine residue. Farnesylcysteine methyltransferase (FCMT) activity is responsible for the methylation reaction which play a role in the membrane attachment of a variety of cellular proteins. Four kinds of Ras protein (c-Ha-ras, c-N-Ras, c-Ki-Ras, pan-Ras) expression were detected in adenocarcinoma of human tissue by immunohistochemical method, and hematoxylin and eosin staining. The level of Ras protein in human stomach tumor tissues was much higher than in normal and peritumoral regions of the same biopsy samples. The FCMT activities of each cellular fractions were high in mitochondrial fraction followed by microsomal fraction, whole homogenate and cytosolic fraction. The inhibitory effect on FCMT activity on stomach tumor tissue was determined after treatment with 0.25 of S-adenosyl--homocysteine. S-adenosyl--homocysteine inhibited FCMT activity from 11.2% to 30.5%. These results suggested that FCMT might be involved in Ras proteins activity.
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KEYWORD
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Human stomach tumor tissue, Ras, Farnesylcysteine methyltrasferase
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