Selective secretion of protein kinase C isozymes by thrombin-stimulated human platelets

T. J. Hillen; A. R. Aroor; S. D. Shukla

doi:10.1006/bbrc.2000.4083

Selective secretion of protein kinase C isozymes by thrombin-stimulated human platelets

T. J. Hillen, A. R. Aroor, S. D. Shukla

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Abstract

The protein kinase C (PKC) was secreted from thrombin-stimulated human platelets in a time- and dose-dependent manner. The PKC specific inhibitors Ro31-8220 (0.05 μM) and GF 109203X (0.5 μM) totally inhibited the secreted kinase activity. Western blot analysis of the secretory components showed reactivity to PKCα, PKCβII, and PKCδ antibodies, but not to PKCβI, and p42/44 MAPK, although they were present in lysed platelets. The fractionation of platelets secreted components showed that PKC activity increased in both soluble and microparticle fractions after thrombin treatments. This is the first report demonstrating that activated human platelets selectively secrete protein kinase C isozymes. Protein kinase C secreted by platelets in this unique manner may have an extracellular role in the plasma, and may regulate cellular functions, including remodeling of vascular endothelial cells.

Original language	English
Pages (from-to)	259-264
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	280
Issue number	1
DOIs	https://doi.org/10.1006/bbrc.2000.4083
State	Published - 2001

Keywords

Platelet microparticles
Platelets
Protein kinase C
Protein kinase C isoenzymes
Secretion
Thrombin

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10.1006/bbrc.2000.4083

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title = "Selective secretion of protein kinase C isozymes by thrombin-stimulated human platelets",

abstract = "The protein kinase C (PKC) was secreted from thrombin-stimulated human platelets in a time- and dose-dependent manner. The PKC specific inhibitors Ro31-8220 (0.05 μM) and GF 109203X (0.5 μM) totally inhibited the secreted kinase activity. Western blot analysis of the secretory components showed reactivity to PKCα, PKCβII, and PKCδ antibodies, but not to PKCβI, and p42/44 MAPK, although they were present in lysed platelets. The fractionation of platelets secreted components showed that PKC activity increased in both soluble and microparticle fractions after thrombin treatments. This is the first report demonstrating that activated human platelets selectively secrete protein kinase C isozymes. Protein kinase C secreted by platelets in this unique manner may have an extracellular role in the plasma, and may regulate cellular functions, including remodeling of vascular endothelial cells.",

keywords = "Platelet microparticles, Platelets, Protein kinase C, Protein kinase C isoenzymes, Secretion, Thrombin",

author = "Hillen, {T. J.} and Aroor, {A. R.} and Shukla, {S. D.}",

note = "Funding Information: The authors are thankful to Mr. Yu-I Weng for experimental help and to Ms. Pam Burgess for word processing this manuscript. Travis Hillen was supported by a University of Missouri Columbia Molecular Biology Program Fellowship.",

year = "2001",

doi = "10.1006/bbrc.2000.4083",

language = "English",

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journal = "Biochemical and Biophysical Research Communications",

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T1 - Selective secretion of protein kinase C isozymes by thrombin-stimulated human platelets

AU - Hillen, T. J.

AU - Aroor, A. R.

AU - Shukla, S. D.

N1 - Funding Information: The authors are thankful to Mr. Yu-I Weng for experimental help and to Ms. Pam Burgess for word processing this manuscript. Travis Hillen was supported by a University of Missouri Columbia Molecular Biology Program Fellowship.

PY - 2001

Y1 - 2001

N2 - The protein kinase C (PKC) was secreted from thrombin-stimulated human platelets in a time- and dose-dependent manner. The PKC specific inhibitors Ro31-8220 (0.05 μM) and GF 109203X (0.5 μM) totally inhibited the secreted kinase activity. Western blot analysis of the secretory components showed reactivity to PKCα, PKCβII, and PKCδ antibodies, but not to PKCβI, and p42/44 MAPK, although they were present in lysed platelets. The fractionation of platelets secreted components showed that PKC activity increased in both soluble and microparticle fractions after thrombin treatments. This is the first report demonstrating that activated human platelets selectively secrete protein kinase C isozymes. Protein kinase C secreted by platelets in this unique manner may have an extracellular role in the plasma, and may regulate cellular functions, including remodeling of vascular endothelial cells.

AB - The protein kinase C (PKC) was secreted from thrombin-stimulated human platelets in a time- and dose-dependent manner. The PKC specific inhibitors Ro31-8220 (0.05 μM) and GF 109203X (0.5 μM) totally inhibited the secreted kinase activity. Western blot analysis of the secretory components showed reactivity to PKCα, PKCβII, and PKCδ antibodies, but not to PKCβI, and p42/44 MAPK, although they were present in lysed platelets. The fractionation of platelets secreted components showed that PKC activity increased in both soluble and microparticle fractions after thrombin treatments. This is the first report demonstrating that activated human platelets selectively secrete protein kinase C isozymes. Protein kinase C secreted by platelets in this unique manner may have an extracellular role in the plasma, and may regulate cellular functions, including remodeling of vascular endothelial cells.

KW - Platelet microparticles

KW - Platelets

KW - Protein kinase C

KW - Protein kinase C isoenzymes

KW - Secretion

KW - Thrombin

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DO - 10.1006/bbrc.2000.4083

M3 - Article

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AN - SCOPUS:0034817389

SN - 0006-291X

VL - 280

SP - 259

EP - 264

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

Selective secretion of protein kinase C isozymes by thrombin-stimulated human platelets

Abstract

Keywords

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