80. Induction of tumor suppression/cell senescence in human melanoma cells following transfection of protein kinase C βII gene

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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Corrections: 12(S)-Hydroxyeicosatetraenoic Acid and 13(S)- Hydroxyoctadecadienoic Acid Regulation of Protein Kinase C- in Melanoma Cells: Role of Receptor-Mediated Hydrolysis of Inositol Phospholipids

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.92.24.11322b ◽

1995 ◽

Vol 92 (24) ◽

pp. 11322b-11322 ◽

Cited By ~ 1

Author(s):

B. Liu

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Melanoma Cells ◽

Hydroxyeicosatetraenoic Acid ◽

Kinase C ◽

Inositol Phospholipids ◽

Hydroxyoctadecadienoic Acid ◽

Hydrolysis Of

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Expression of protein kinase C subspecies IX cultured human melanocytes and melanoma cells

Journal of Dermatological Science ◽

10.1016/0923-1811(92)90205-p ◽

1992 ◽

Vol 4 (2) ◽

pp. 132

Author(s):

M. Oka ◽

T. Horikawa ◽

M. Ueda ◽

Y. Funasaka ◽

K. Nishino ◽

...

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Melanoma Cells ◽

Kinase C ◽

Human Melanocytes

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Enhanced Expression of Protein Kinase C Subspecies in Melanogenic Compartments in B16 Melanoma Cells by UVB or MSH

Journal of Investigative Dermatology ◽

10.1111/1523-1747.ep12343168 ◽

1996 ◽

Vol 106 (2) ◽

pp. 377-378 ◽

Cited By ~ 22

Author(s):

Masahiro Oka ◽

Masamitsu Ichihashi ◽

Ashok K. Chakraborty

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Melanoma Cells ◽

B16 Melanoma ◽

B16 Melanoma Cells ◽

Kinase C ◽

Enhanced Expression

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WNT5A-Induced Activation of the Protein Kinase C Substrate MARCKS Is Required for Melanoma Cell Invasion

Cancers ◽

10.3390/cancers12020346 ◽

2020 ◽

Vol 12 (2) ◽

pp. 346 ◽

Cited By ~ 1

Author(s):

Purusottam Mohapatra ◽

Vikas Yadav ◽

Maren Toftdahl ◽

Tommy Andersson

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Melanoma Cell ◽

Cell Invasion ◽

Leading Edge ◽

Melanoma Cells ◽

Kinase Substrate ◽

Kinase C ◽

Metastatic Behavior ◽

Membrane Protrusions

WNT5A is a well-known mediator of melanoma cell invasion and metastasis via its ability to activate protein kinase C (PKC), which is monitored by phosphorylation of the endogenous PKC substrate myristoylated alanine-rich c-kinase substrate (MARCKS). However, a possible direct contribution of MARCKS in WNT5A-mediated melanoma cell invasion has not been investigated. Analyses of melanoma patient databases suggested that similar to WNT5A expression, MARCKS expression appears to be associated with increased metastasis. A relationship between the two is suggested by the findings that recombinant WNT5A (rWNT5A) induces both increased expression and phosphorylation of MARCKS, whereas WNT5A silencing does the opposite. Moreover, WNT5A-induced invasion of melanoma cells was blocked by siRNA targeting MARCKS, indicating a crucial role of MARCKS expression and/or its phosphorylation. Next, we employed a peptide inhibitor of MARCKS phosphorylation that did not affect MARCKS expression and found that it abolished WNT5A-induced melanoma cell invasion. Similarly, rWNT5A induced the accumulation of phosphorylated MARCKS in membrane protrusions at the leading edge of melanoma cells. Our results demonstrate that WNT5A-induced phosphorylation of MARCKS is not only an indicator of PKC activity but also a crucial regulator of the metastatic behavior of melanoma and therefore an attractive future antimetastatic target in melanoma patients.

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