Insulin Translocates PKC-ε and Phorbol esters induce and persistantly translocates PKC-β2 in BC3H-1 myocytes

M. L. Standaert; A. Avignon; Thomas Paul Arnold; S. I. Saba; D. R. Cooper; J. C. Watson; X. Zhou; L. Galloway; R. V. Farese

doi:10.1016/0898-6568(96)00043-5

Insulin Translocates PKC-ε and Phorbol esters induce and persistantly translocates PKC-β2 in BC3H-1 myocytes

M. L. Standaert
, A. Avignon
, Thomas Paul Arnold
, S. I. Saba
, D. R. Cooper
, J. C. Watson
, X. Zhou
, L. Galloway
, R. V. Farese

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

11 Scopus citations

Abstract

Initial studies suggested that insulin increases diacylglycerol and activates protein kinase C (PKC) in BC3H-1 myocytes. In these earlier studies, insulin was found to translocate PKC-β, but the presence of PKC-ϵ was not appreciated. More recently, the presence of PKC-ϵ was documented, but PKC-β was not detected, and it was questioned whether insulin activates PKC in BC3H-1 myocytes [Stumpo, D.J., Haupt, D.M. and Blackshear, P.J. (1994) J. Biol. Chem. 269 :21184–21190]. We questioned whether insulin translocates PKC-ϵ in BC3H-1 myocytes, and re-evaluated the question of whether myocytes truly contain a PKC-β isoform whose existence can be verified by its response to phorbol ester treatment. We found that PKC-ϵ was acutely translocated by insulin and phorbol esters from the cytosol to the membrane fraction in BC3H-1 myocytes; in addition, PKC-ϵ, like PKC-α, was depleted by chronic phorbol ester treatment. We also found that BC3H-I myocytes containing a 76,000 M r PKC-β isoform that is acutely translocated and subsequently depleted by phorbol esters. Moreover, chronic phorbol ester treatment induced an 84,000 Mr PKC- β 2 isoform that appeared to be persistently translocated and activated, as suggested by studies of myristoylated arginine-rich C kinase substrate (MARCKS) phosphorylation. We conclude that: (1) insulin acutely translocates PKC-ϵ, as well as PKC-β, in BC3H-1 myocytes; and (2) PKC-β is not truly downregulated by phorbol esters in BC3H-1 myocytes.

Original language	American English
Journal	Cellular Signalling
Volume	8
DOIs	https://doi.org/10.1016/0898-6568(96)00043-5
State	Published - Jan 1 1996

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Medicine and Health Sciences

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@article{d743d47aec5441ccb5c50f041d3d3168,

title = "Insulin Translocates PKC-ε and Phorbol esters induce and persistantly translocates PKC-β2 in BC3H-1 myocytes",

abstract = " Initial studies suggested that insulin increases diacylglycerol and activates protein kinase C (PKC) in BC3H-1 myocytes. In these earlier studies, insulin was found to translocate PKC-\β, but the presence of PKC-\ϵ was not appreciated. More recently, the presence of PKC-\ϵ was documented, but PKC-\β was not detected, and it was questioned whether insulin activates PKC in BC3H-1 myocytes [Stumpo, D.J., Haupt, D.M. and Blackshear, P.J. (1994) J. Biol. Chem. 269 :21184\–21190]. We questioned whether insulin translocates PKC-\ϵ in BC3H-1 myocytes, and re-evaluated the question of whether myocytes truly contain a PKC-\β isoform whose existence can be verified by its response to phorbol ester treatment. We found that PKC-\ϵ was acutely translocated by insulin and phorbol esters from the cytosol to the membrane fraction in BC3H-1 myocytes; in addition, PKC-\ϵ, like PKC-\α, was depleted by chronic phorbol ester treatment. We also found that BC3H-I myocytes containing a 76,000 M r PKC-\β isoform that is acutely translocated and subsequently depleted by phorbol esters. Moreover, chronic phorbol ester treatment induced an 84,000 Mr PKC- \β 2 isoform that appeared to be persistently translocated and activated, as suggested by studies of myristoylated arginine-rich C kinase substrate (MARCKS) phosphorylation. We conclude that: (1) insulin acutely translocates PKC-\ϵ, as well as PKC-\β, in BC3H-1 myocytes; and (2) PKC-\β is not truly downregulated by phorbol esters in BC3H-1 myocytes.",

author = "Standaert, \{M. L.\} and A. Avignon and Arnold, \{Thomas Paul\} and Saba, \{S. I.\} and Cooper, \{D. R.\} and Watson, \{J. C.\} and X. Zhou and L. Galloway and Farese, \{R. V.\}",

year = "1996",

month = jan,

day = "1",

doi = "10.1016/0898-6568(96)00043-5",

language = "American English",

volume = "8",

journal = "Cellular Signalling",

issn = "0898-6568",

publisher = "Elsevier Inc.",

}

TY - JOUR

T1 - Insulin Translocates PKC-ε and Phorbol esters induce and persistantly translocates PKC-β2 in BC3H-1 myocytes

AU - Standaert, M. L.

AU - Avignon, A.

AU - Arnold, Thomas Paul

AU - Saba, S. I.

AU - Cooper, D. R.

AU - Watson, J. C.

AU - Zhou, X.

AU - Galloway, L.

AU - Farese, R. V.

PY - 1996/1/1

Y1 - 1996/1/1

N2 - Initial studies suggested that insulin increases diacylglycerol and activates protein kinase C (PKC) in BC3H-1 myocytes. In these earlier studies, insulin was found to translocate PKC-β, but the presence of PKC-ϵ was not appreciated. More recently, the presence of PKC-ϵ was documented, but PKC-β was not detected, and it was questioned whether insulin activates PKC in BC3H-1 myocytes [Stumpo, D.J., Haupt, D.M. and Blackshear, P.J. (1994) J. Biol. Chem. 269 :21184–21190]. We questioned whether insulin translocates PKC-ϵ in BC3H-1 myocytes, and re-evaluated the question of whether myocytes truly contain a PKC-β isoform whose existence can be verified by its response to phorbol ester treatment. We found that PKC-ϵ was acutely translocated by insulin and phorbol esters from the cytosol to the membrane fraction in BC3H-1 myocytes; in addition, PKC-ϵ, like PKC-α, was depleted by chronic phorbol ester treatment. We also found that BC3H-I myocytes containing a 76,000 M r PKC-β isoform that is acutely translocated and subsequently depleted by phorbol esters. Moreover, chronic phorbol ester treatment induced an 84,000 Mr PKC- β 2 isoform that appeared to be persistently translocated and activated, as suggested by studies of myristoylated arginine-rich C kinase substrate (MARCKS) phosphorylation. We conclude that: (1) insulin acutely translocates PKC-ϵ, as well as PKC-β, in BC3H-1 myocytes; and (2) PKC-β is not truly downregulated by phorbol esters in BC3H-1 myocytes.

AB - Initial studies suggested that insulin increases diacylglycerol and activates protein kinase C (PKC) in BC3H-1 myocytes. In these earlier studies, insulin was found to translocate PKC-β, but the presence of PKC-ϵ was not appreciated. More recently, the presence of PKC-ϵ was documented, but PKC-β was not detected, and it was questioned whether insulin activates PKC in BC3H-1 myocytes [Stumpo, D.J., Haupt, D.M. and Blackshear, P.J. (1994) J. Biol. Chem. 269 :21184–21190]. We questioned whether insulin translocates PKC-ϵ in BC3H-1 myocytes, and re-evaluated the question of whether myocytes truly contain a PKC-β isoform whose existence can be verified by its response to phorbol ester treatment. We found that PKC-ϵ was acutely translocated by insulin and phorbol esters from the cytosol to the membrane fraction in BC3H-1 myocytes; in addition, PKC-ϵ, like PKC-α, was depleted by chronic phorbol ester treatment. We also found that BC3H-I myocytes containing a 76,000 M r PKC-β isoform that is acutely translocated and subsequently depleted by phorbol esters. Moreover, chronic phorbol ester treatment induced an 84,000 Mr PKC- β 2 isoform that appeared to be persistently translocated and activated, as suggested by studies of myristoylated arginine-rich C kinase substrate (MARCKS) phosphorylation. We conclude that: (1) insulin acutely translocates PKC-ϵ, as well as PKC-β, in BC3H-1 myocytes; and (2) PKC-β is not truly downregulated by phorbol esters in BC3H-1 myocytes.

UR - https://nsuworks.nova.edu/hpd_ot_faculty_articles/56

U2 - 10.1016/0898-6568(96)00043-5

DO - 10.1016/0898-6568(96)00043-5

M3 - Article

SN - 0898-6568

VL - 8

JO - Cellular Signalling

JF - Cellular Signalling

ER -

Insulin Translocates PKC-ε and Phorbol esters induce and persistantly translocates PKC-β2 in BC3H-1 myocytes

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