Protein kinase Cβ expression in melanoma cells and melanocytes: differential expression correlates with biological responses to 12-O-tetradecanoylphorbol 13-acetate

1993 ◽  
Vol 119 (4) ◽  
pp. 199-206 ◽  
Author(s):  
Marianne Broome Powell ◽  
Richard K. Rosenberg ◽  
Mark J. Graham ◽  
Mary L. Birch ◽  
Douglas T. Yamanishi ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Differential Expression ◽  
Melanoma Cells ◽  
Biological Responses

scholarly journals T-LAK Cell-originated Protein Kinase (TOPK) Phosphorylation of Prx1 at Ser-32 Prevents UVB-induced Apoptosis in RPMI7951 Melanoma Cells through the Regulation of Prx1 Peroxidase Activity

2010 ◽  
Vol 285 (38) ◽  
pp. 29138-29146 ◽  
Author(s):  
Tatyana A. Zykova ◽  
Feng Zhu ◽  
Tatyana I. Vakorina ◽  
Jishuai Zhang ◽  
Lee Ann Higgins ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Peroxidase Activity ◽  
Melanoma Cells ◽  
Lak Cell ◽  
Induced Apoptosis

scholarly journals cDNA sequence and differential expression of the mouse Ca2+ /calmodulin-dependent protein kinase IV gene

FEBS Letters ◽  
1991 ◽  
Vol 289 (1) ◽  
pp. 105-109 ◽  
Author(s):  
David A. Jones ◽  
John Glod ◽  
Donna Wilson-Shaw ◽  
William E. Hahn ◽  
James M. Sikela
Keyword(s):  
Protein Kinase ◽  
Differential Expression ◽  
Cdna Sequence ◽  
Dependent Protein Kinase ◽  
Dependent Protein

Receptor-mediated endocytosis of urokinase-type plasminogen activator is regulated by cAMP-dependent protein kinase

1997 ◽  
Vol 110 (12) ◽  
pp. 1395-1402 ◽  
Author(s):  
L. Goretzki ◽  
B.M. Mueller
Keyword(s):  
Protein Kinase ◽  
Plasminogen Activator ◽  
Kinase Inhibitors ◽  
Melanoma Cells ◽  
Protein Kinase Inhibitors ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Type Plasminogen Activator ◽  
Urokinase Type Plasminogen Activator ◽  
Dependent Protein

Internalization of the urokinase-type plasminogen activator (uPA) requires two receptors, the uPA receptor (uPAR) and the low density lipoprotein receptor-related protein (LRP)/alpha2-macroglobulin (alpha2M) receptor. Here, we address whether protein kinases are involved in the internalization of uPA by human melanoma cells. Initially, we found that the internalization of uPA was significantly inhibited by the serine/threonine protein kinase inhibitors staurosporine, K-252a and H-89, but not by the tyrosine kinase inhibitors, genistein and lavendustin A. Internalization of uPA was also inhibited by a pseudosubstrate peptide for cAMP-dependent protein kinase (PKA), but not by a pseudosubstrate peptide for protein kinase C. We confirmed a requirement for PKA-activity and implicated a specific isoform by using an antisense oligonucleotide against the regulatory subunit RI alpha of PKA which suppresses PKA-I activity. Exposure of cells to this oligonucleotide led to a specific, dose-dependent decrease in RI alpha protein and to a significant inhibition in the rate of uPA internalization. We further demonstrate that treatment of melanoma cells with either H-89 or PKA RI alpha antisense oligonucleotides also resulted in a decreased internalization of two other ligands of LRP, activated alpha2M and lactoferrin, indicating that PKA activity is associated with LRP. Finally, we demonstrate that PKA activity is also required for the internalization of transferrin, but not for the internalization of the epidermal growth factor or adenovirus 2, suggesting that in melanoma cells, PKA activity is not generally required for clathrin-mediated endocytosis, but is rather associated with specific internalization receptors.

scholarly journals Association of protein kinase-C-alpha with cytoplasmic vesicles in melanoma cells.

1996 ◽  
Vol 44 (2) ◽  
pp. 177-182 ◽  
Author(s):  
J Timar ◽  
B Liu ◽  
R Bazaz ◽  
K V Honn
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Fluid Phase ◽  
Subcellular Fractionation ◽  
Melanoma Cells ◽  
Kinase C ◽  
Cytoplasmic Vesicles ◽  
Protein Kinase C Alpha ◽  
Pkc Alpha

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.

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