Association of protein kinase-C-alpha with cytoplasmic vesicles in melanoma cells.
In B16a melanoma cells, protein kinase-C-alpha (PKC alpha) is immunomorphologically associated with cytoplasmic vesicles in addition to the previously observed locations (plasma membrane, cytoskeleton, nucleus), as detected with monoclonal antibody (MAb) MC3a. Subcellular fractionation indicated that the authentic 80-KD protein as well as PKC activity can be detected in several particulate fractions except for L2, which contains dense lysosomes. The highest PKC activity is associated with the cytosol-ultralight vesicles and the L1 fraction (containing plasma membrane, endosomes, and the Golgi apparatus). Both of these fractions contained the fluid-phase endocytosis marker peroxidase, indicating that PKC alpha, in addition to other subcellular structures, is most probably associated with endosomal membranes in B16a melanoma cells.
Timar
J
J
First Institute of Pathology and Experimental Cancer Research, Semmelweis University of Medicine, Budapest, Hungary.
Liu
B
B
Bazaz
R
R
Honn
K V
KV
D000818:Animals; D003593:Cytoplasm / Q000201:enzymology; D007150:Immunohistochemistry; D007527:Isoenzymes / Q000378:metabolism*; D008545:Melanoma / Q000201:enzymology* / Q000473:pathology; D051379:Mice; D011493:Protein Kinase C / Q000378:metabolism*; D051571:Protein Kinase C-alpha; D013347:Subcellular Fractions; D014407:Tumor Cells, Cultured
D007527:Isoenzymes; C496630:Prkca protein, mouse; D011493:Protein Kinase C; D051571:Protein Kinase C-alpha