scholarly journals Inhibition of Human Gastric Carcinoma Cell Growth in Vitro and in Vivo by Cladosporol Isolated from the Paclitaxel-Producing Strain Alternaria alternata var. monosporus

2009 ◽  
Vol 32 (12) ◽  
pp. 2072-2074 ◽  
Author(s):  
Jiepeng Chen ◽  
Xuelian Qiu ◽  
Ronghua Wang ◽  
Lili Duan ◽  
Shouxian Chen ◽  
...  
Keyword(s):  
Cell Growth ◽  
Gastric Carcinoma ◽  
Alternaria Alternata ◽  
Carcinoma Cell ◽  
Gastric Carcinoma Cell ◽  
Human Gastric Carcinoma

Synergistic inhibition of human gastric carcinoma cell growth by 1-β-d-arabinofuranosylcytosine and hydroxyurea or 2′-deoxyguanosine in vitro

1992 ◽  
Vol 63 (3) ◽  
pp. 221-228 ◽  
Author(s):  
Masahiko Matsumoto ◽  
Takayuki Kawahara ◽  
Michio Tsuda ◽  
Tomoichi Ohkubo ◽  
Hiroshi Kamiguchi ◽  
...  
Keyword(s):  
Cell Growth ◽  
Gastric Carcinoma ◽  
Carcinoma Cell ◽  
Gastric Carcinoma Cell ◽  
Synergistic Inhibition ◽  
Human Gastric Carcinoma

Inhibition of human gastric carcinoma cell growth in vitro by a polysaccharide from Aster tataricus

2012 ◽  
Vol 51 (4) ◽  
pp. 509-513 ◽  
Author(s):  
Yunxin Zhang ◽  
Qiusheng Wang ◽  
Tie Wang ◽  
Haikui Zhang ◽  
Ying Tian ◽  
...  
Keyword(s):  
Cell Growth ◽  
Gastric Carcinoma ◽  
Carcinoma Cell ◽  
Gastric Carcinoma Cell ◽  
Human Gastric Carcinoma

p145, a protein with associated tyrosine kinase activity in a human gastric carcinoma cell line

1988 ◽  
Vol 8 (8) ◽  
pp. 3510-3517
Author(s):  
S Giordano ◽  
M F Di Renzo ◽  
R Ferracini ◽  
L Chiadò-Piat ◽  
P M Comoglio
Keyword(s):  
Gastric Carcinoma ◽  
Tyrosine Kinase ◽  
Cell Line ◽  
Kinase Activity ◽  
Carcinoma Cell ◽  
Tyrosine Kinase Activity ◽  
Gastric Carcinoma Cell ◽  
Gastric Carcinoma Cell Line

A protein with an Mr of 145,000 (p145) was detected by antibodies to phosphotyrosine by Western blot (immunoblot) analysis. This protein was phosphorylated on tyrosine in a gastric carcinoma cell line. In cells that were metabolically labeled with 32Pi, this protein was phosphorylated on tyrosine and serine. p145 is a cysteine-rich transmembrane glycoprotein. The extracellular domain could be labeled by 125I under nonpermeating conditions and was cleaved by mild trypsin treatment of intact cells. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis under nonreducing conditions revealed a shift of p145 mobility to an apparent Mr of 190,000. After immunoprecipitation with phosphotyrosine antibodies, p145 displayed a strong associated protein kinase activity in vitro, becoming phosphorylated on tyrosine. There was no immunological cross-reaction between p145 and known tyrosine kinases. Both in vivo and in vitro tyrosine phosphorylations were unaffected by the addition of known growth factors. However, p145 was rapidly dephosphorylated in vivo when cells were exposed to low pH, a condition that is known to dissociate ligands from their receptors. These data suggest that p145 is associated with a protein tyrosine kinase activity which, in the tumor cell line studied, is activated by an as yet unidentified factor.

scholarly journals p145, a protein with associated tyrosine kinase activity in a human gastric carcinoma cell line.

1988 ◽  
Vol 8 (8) ◽  
pp. 3510-3517 ◽  
Author(s):  
S Giordano ◽  
M F Di Renzo ◽  
R Ferracini ◽  
L Chiadò-Piat ◽  
P M Comoglio
Keyword(s):  
Gastric Carcinoma ◽  
Tyrosine Kinase ◽  
Cell Line ◽  
Kinase Activity ◽  
Carcinoma Cell ◽  
Tyrosine Kinase Activity ◽  
Gastric Carcinoma Cell ◽  
Gastric Carcinoma Cell Line

A protein with an Mr of 145,000 (p145) was detected by antibodies to phosphotyrosine by Western blot (immunoblot) analysis. This protein was phosphorylated on tyrosine in a gastric carcinoma cell line. In cells that were metabolically labeled with 32Pi, this protein was phosphorylated on tyrosine and serine. p145 is a cysteine-rich transmembrane glycoprotein. The extracellular domain could be labeled by 125I under nonpermeating conditions and was cleaved by mild trypsin treatment of intact cells. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis under nonreducing conditions revealed a shift of p145 mobility to an apparent Mr of 190,000. After immunoprecipitation with phosphotyrosine antibodies, p145 displayed a strong associated protein kinase activity in vitro, becoming phosphorylated on tyrosine. There was no immunological cross-reaction between p145 and known tyrosine kinases. Both in vivo and in vitro tyrosine phosphorylations were unaffected by the addition of known growth factors. However, p145 was rapidly dephosphorylated in vivo when cells were exposed to low pH, a condition that is known to dissociate ligands from their receptors. These data suggest that p145 is associated with a protein tyrosine kinase activity which, in the tumor cell line studied, is activated by an as yet unidentified factor.

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