Protein kinase activity is associated with CD63 in melanoma cells

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Abstract

Background: The tetraspan protein CD63, originally described as a stage-specific melanoma antigen but also present in a number of normal cells, regulates melanoma cell growth in nude mice, motility in serum containing media, and adhesion to several extracellular matrix proteins. CD63 has been reported to associate with β1 and β2 integrins, but the mechanism of signal transduction by CD63 is not clear. This study examined whether CD63 is associated with protein kinase and can transmit signals in melanoma cells. Methods: Immunoprecipitation and radiolabeling were used to test for association of protein kinase activity with CD63. Adhesion of cells to monoclonal antibodies immobilized to microtiter plates was used to examine the ability of CD63 to transmit signals. Results: CD63 was capable of transmitting a signal in melanoma cells that required extracellular calcium. In the absence of extracellular calcium at the time of binding to the CD63 mAb, the cell was no longer responsive to stimulation by CD63. Immunoprecipitation studies demonstrated protein kinase activity associated with CD63, and phosphoamino acid analysis revealed that most of this protein kinase activity was due to serine kinase activity. Conclusion: The current study suggests that serine protein kinase activity associated with CD63 may play a role in signaling by CD63 in melanoma cells.

Original languageEnglish (US)
Article number42
JournalJournal of Translational Medicine
Volume3
DOIs
StatePublished - Nov 30 2005

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Protein Kinases
Melanoma
Protein-Serine-Threonine Kinases
Adhesion
Immunoprecipitation
Phosphoamino Acids
Melanoma-Specific Antigens
Calcium
Signal transduction
Extracellular Matrix Proteins
Cell growth
Integrins
Nude Mice
Cell Adhesion
Monoclonal Antibodies
Cells
Association reactions
Signal Transduction
Cell Count
Growth

Cite this

@article{80932341fde14bb2a91f51aab76882f9,
title = "Protein kinase activity is associated with CD63 in melanoma cells",
abstract = "Background: The tetraspan protein CD63, originally described as a stage-specific melanoma antigen but also present in a number of normal cells, regulates melanoma cell growth in nude mice, motility in serum containing media, and adhesion to several extracellular matrix proteins. CD63 has been reported to associate with β1 and β2 integrins, but the mechanism of signal transduction by CD63 is not clear. This study examined whether CD63 is associated with protein kinase and can transmit signals in melanoma cells. Methods: Immunoprecipitation and radiolabeling were used to test for association of protein kinase activity with CD63. Adhesion of cells to monoclonal antibodies immobilized to microtiter plates was used to examine the ability of CD63 to transmit signals. Results: CD63 was capable of transmitting a signal in melanoma cells that required extracellular calcium. In the absence of extracellular calcium at the time of binding to the CD63 mAb, the cell was no longer responsive to stimulation by CD63. Immunoprecipitation studies demonstrated protein kinase activity associated with CD63, and phosphoamino acid analysis revealed that most of this protein kinase activity was due to serine kinase activity. Conclusion: The current study suggests that serine protein kinase activity associated with CD63 may play a role in signaling by CD63 in melanoma cells.",
author = "Joji Iida and Skubitz, {Amy P.N.} and McCarthy, {James B.} and Skubitz, {Keith M.}",
year = "2005",
month = "11",
day = "30",
doi = "10.1186/1479-5876-3-42",
language = "English (US)",
volume = "3",
journal = "Journal of Translational Medicine",
issn = "1479-5876",
publisher = "BioMed Central",

}

TY - JOUR

T1 - Protein kinase activity is associated with CD63 in melanoma cells

AU - Iida, Joji

AU - Skubitz, Amy P.N.

AU - McCarthy, James B.

AU - Skubitz, Keith M.

PY - 2005/11/30

Y1 - 2005/11/30

N2 - Background: The tetraspan protein CD63, originally described as a stage-specific melanoma antigen but also present in a number of normal cells, regulates melanoma cell growth in nude mice, motility in serum containing media, and adhesion to several extracellular matrix proteins. CD63 has been reported to associate with β1 and β2 integrins, but the mechanism of signal transduction by CD63 is not clear. This study examined whether CD63 is associated with protein kinase and can transmit signals in melanoma cells. Methods: Immunoprecipitation and radiolabeling were used to test for association of protein kinase activity with CD63. Adhesion of cells to monoclonal antibodies immobilized to microtiter plates was used to examine the ability of CD63 to transmit signals. Results: CD63 was capable of transmitting a signal in melanoma cells that required extracellular calcium. In the absence of extracellular calcium at the time of binding to the CD63 mAb, the cell was no longer responsive to stimulation by CD63. Immunoprecipitation studies demonstrated protein kinase activity associated with CD63, and phosphoamino acid analysis revealed that most of this protein kinase activity was due to serine kinase activity. Conclusion: The current study suggests that serine protein kinase activity associated with CD63 may play a role in signaling by CD63 in melanoma cells.

AB - Background: The tetraspan protein CD63, originally described as a stage-specific melanoma antigen but also present in a number of normal cells, regulates melanoma cell growth in nude mice, motility in serum containing media, and adhesion to several extracellular matrix proteins. CD63 has been reported to associate with β1 and β2 integrins, but the mechanism of signal transduction by CD63 is not clear. This study examined whether CD63 is associated with protein kinase and can transmit signals in melanoma cells. Methods: Immunoprecipitation and radiolabeling were used to test for association of protein kinase activity with CD63. Adhesion of cells to monoclonal antibodies immobilized to microtiter plates was used to examine the ability of CD63 to transmit signals. Results: CD63 was capable of transmitting a signal in melanoma cells that required extracellular calcium. In the absence of extracellular calcium at the time of binding to the CD63 mAb, the cell was no longer responsive to stimulation by CD63. Immunoprecipitation studies demonstrated protein kinase activity associated with CD63, and phosphoamino acid analysis revealed that most of this protein kinase activity was due to serine kinase activity. Conclusion: The current study suggests that serine protein kinase activity associated with CD63 may play a role in signaling by CD63 in melanoma cells.

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