Identification of protein kinase C as an intermediate in NA, K-atpase beta-subunit mediated lamellipodia formation and suppression of cell motility in carcinoma cells

S. P. Barwe; S. A. Rajasekaran; A. K. Rajasekaran

doi:10.1170/T759

Identification of protein kinase C as an intermediate in NA, K-atpase beta-subunit mediated lamellipodia formation and suppression of cell motility in carcinoma cells

S. P. Barwe
, S. A. Rajasekaran
, A. K. Rajasekaran

University of California at Los Angeles

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

We have shown that repletion of Na,K-ATPase Beta1-subunit (Na,K-Beta) in Moloney Sarcoma virus transformed MDCK (MSV-Na,K-Beta) cells induced lamellipodia and suppressed motility in a PI3-Kinase dependent manner. In this study, we provide evidence that decreased cell motility is due to increased attachment of Na,K-Beta expressing cells to the substratum. Treatment of MSV-Beta-GFP cells with bisindolylmalemide, a general Protein Kinase C (PKC) inhibitor, abolished PI3-Kinase activation and its down stream effects of Rac1 activation, binding of Na,K-Beta to annexin II, and suppression of cell motility and attachment. Thus, these studies unraveled that a PKC is involved upstream of PI3-Kinase in the suppression of Na,K-Beta mediated cell motility in carcinoma cells.

Original language	English
Pages (from-to)	41-47
Number of pages	7
Journal	Cellular and Molecular Biology
Volume	52
Issue number	8
DOIs	https://doi.org/10.1170/T759
State	Published - 2006
Externally published	Yes

Keywords

Cell attachment
Cell motility
K-ATPase
Na
PI3-Kinase
PKC

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title = "Identification of protein kinase C as an intermediate in NA, K-atpase beta-subunit mediated lamellipodia formation and suppression of cell motility in carcinoma cells",

abstract = "We have shown that repletion of Na,K-ATPase Beta1-subunit (Na,K-Beta) in Moloney Sarcoma virus transformed MDCK (MSV-Na,K-Beta) cells induced lamellipodia and suppressed motility in a PI3-Kinase dependent manner. In this study, we provide evidence that decreased cell motility is due to increased attachment of Na,K-Beta expressing cells to the substratum. Treatment of MSV-Beta-GFP cells with bisindolylmalemide, a general Protein Kinase C (PKC) inhibitor, abolished PI3-Kinase activation and its down stream effects of Rac1 activation, binding of Na,K-Beta to annexin II, and suppression of cell motility and attachment. Thus, these studies unraveled that a PKC is involved upstream of PI3-Kinase in the suppression of Na,K-Beta mediated cell motility in carcinoma cells.",

keywords = "Cell attachment, Cell motility, K-ATPase, Na, PI3-Kinase, PKC",

author = "Barwe, \{S. P.\} and Rajasekaran, \{S. A.\} and Rajasekaran, \{A. K.\}",

year = "2006",

doi = "10.1170/T759",

language = "English",

volume = "52",

pages = "41--47",

journal = "Cellular and Molecular Biology",

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publisher = "Cellular and Molecular Biology Association",

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}

TY - JOUR

T1 - Identification of protein kinase C as an intermediate in NA, K-atpase beta-subunit mediated lamellipodia formation and suppression of cell motility in carcinoma cells

AU - Barwe, S. P.

AU - Rajasekaran, S. A.

AU - Rajasekaran, A. K.

PY - 2006

Y1 - 2006

N2 - We have shown that repletion of Na,K-ATPase Beta1-subunit (Na,K-Beta) in Moloney Sarcoma virus transformed MDCK (MSV-Na,K-Beta) cells induced lamellipodia and suppressed motility in a PI3-Kinase dependent manner. In this study, we provide evidence that decreased cell motility is due to increased attachment of Na,K-Beta expressing cells to the substratum. Treatment of MSV-Beta-GFP cells with bisindolylmalemide, a general Protein Kinase C (PKC) inhibitor, abolished PI3-Kinase activation and its down stream effects of Rac1 activation, binding of Na,K-Beta to annexin II, and suppression of cell motility and attachment. Thus, these studies unraveled that a PKC is involved upstream of PI3-Kinase in the suppression of Na,K-Beta mediated cell motility in carcinoma cells.

AB - We have shown that repletion of Na,K-ATPase Beta1-subunit (Na,K-Beta) in Moloney Sarcoma virus transformed MDCK (MSV-Na,K-Beta) cells induced lamellipodia and suppressed motility in a PI3-Kinase dependent manner. In this study, we provide evidence that decreased cell motility is due to increased attachment of Na,K-Beta expressing cells to the substratum. Treatment of MSV-Beta-GFP cells with bisindolylmalemide, a general Protein Kinase C (PKC) inhibitor, abolished PI3-Kinase activation and its down stream effects of Rac1 activation, binding of Na,K-Beta to annexin II, and suppression of cell motility and attachment. Thus, these studies unraveled that a PKC is involved upstream of PI3-Kinase in the suppression of Na,K-Beta mediated cell motility in carcinoma cells.

KW - Cell attachment

KW - Cell motility

KW - K-ATPase

KW - Na

KW - PI3-Kinase

KW - PKC

UR - https://www.scopus.com/pages/publications/34249105226

U2 - 10.1170/T759

DO - 10.1170/T759

M3 - Article

C2 - 17535735

AN - SCOPUS:34249105226

SN - 0145-5680

VL - 52

SP - 41

EP - 47

JO - Cellular and Molecular Biology

JF - Cellular and Molecular Biology

IS - 8

ER -

Identification of protein kinase C as an intermediate in NA, K-atpase beta-subunit mediated lamellipodia formation and suppression of cell motility in carcinoma cells

Abstract

Keywords

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