Transglutaminase catalyzed incorporation of putrescine into surface proteins of mouse neuroblastoma cells
Transglutaminase, purified from guinea pig liver, was used to catalyze the incorporation of[14C]putrescine into exposed surface proteins of intact mouse neuroblastoma cells. This method specifically labeled two surface proteins (Mr = 92 000 and 76 000) in the N-18 mouse neuroblastoma cells and three surface proteins (Mr = 92 000, 76 000, and 72 000) in the NB-15 mouse neuroblastoma cells. In addition, transglutaminase also catalyzed cross-linking reactions of exposed surface proteins. In both the N-18 and NB-15 cells, differentiation was accompanied by a 2-fold increase of specific radioactivity incorporated into trichloroacetic acid insoluble cellular material, suggesting that the differentiated mouse neuroblastoma cells may possess greater amount of accessible peptide-bound glutaminyl residues on their surface than their malignant counterparts. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorographic method revealed that while the [14C]putrescine-labeled protein patterns of undifferentiated and differentiated mouse neuroblastoma cells were similar, the intensity of labeling of individual bands was specifically modulated by cell differentiation.
KeywordsSurface Protein Mouse Neuroblastoma Cell Exposed Surface Protein Glycine Ethyl Ester Dibutyryl Adenosine
N6,O2′-Dibutyryl adenosine 3′:5′-cyclic monophosphate
sodium dodecyl sulfate-polyacrylamide gel electrophoresis
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