Differential protein phosphorylation in human gastric adenocarcinomas.
A qualitative analysis of endogenous protein phosphorylation in microsomal fractions from surgical specimens of human gastric cancer, benign gastric ulcers and normal gastric tissues is presented. Fractions were incubated in the presence of (gamma-32P)ATP to measure the transfer of (gamma-32P) to natural substrates mediated by endogenous protein kinases. Phosphoproteins were characterized through PAGE-SDS and detected by autoradiography. KOH at high temperature was used to select for tyrosine-phosphorylated polypeptides on dried gels. We report a notorious enhancement in overall protein phosphorylation in gastric cancer samples over benign ulcers and normal controls as well. Moreover, a highly basic-low molecular weight phosphoprotein is found through 2-D protein gel analysis and a 50 kDa protein is detected only in the presence of Mg2+ after KOH treatment. These two proteins might become putative molecular markers to detect this type of neoplasia.
Marshall
S
S
Laboratorio de Genética Molecular, Universidad Catolica de Valparaiso, Chile.
Munoz
G
G
Sierralta
G
G
Horvat
A
A
D000230:Adenocarcinoma / Q000378:metabolism*; D002118:Calcium / Q000494:pharmacology; D006801:Humans; D008274:Magnesium / Q000494:pharmacology; D008861:Microsomes / Q000378:metabolism; D010750:Phosphoproteins / Q000032:analysis; D010766:Phosphorylation / Q000187:drug effects; D011494:Protein Kinases / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D013274:Stomach Neoplasms / Q000378:metabolism*; D013347:Subcellular Fractions / Q000378:metabolism
D010750:Phosphoproteins; D011506:Proteins; D011494:Protein Kinases; D008274:Magnesium; D002118:Calcium