Modulation of cofactor requirement for the activation of protein kinase C by heparin Possible effect at the regulatory domain

Said A. Goueli; John A. Hanten; Khalil Ahmed

doi:10.1016/0014-5793(91)80533-9

Modulation of cofactor requirement for the activation of protein kinase C by heparin Possible effect at the regulatory domain

Said A. Goueli, John A. Hanten, Khalil Ahmed

Laboratory Medicine and Pathology

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

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Abstract

Heparin was found to stimulate the phosphorylation of histone H1 but not protamine sulfate catalyzed by Ca²⁺/phospholipid-dependent protein kinase (protein kinase C or PKC). The effect of heparin on histone H1 phosphorylation appeared to be due to an increase in phosphatidylserine affinity for PKC activation in the presence of heparin. This effect of heparin was abolisched when trypsinized, cofactor-independent, PKC was employed to phosphorylate histone H1. These studies suggest that heparin acts at the regulatory domain of PKC, and emphasize the importance of the negative charge in influencing the accessibility of the substrate to PKC action.

Original language	English (US)
Pages (from-to)	445-448
Number of pages	4
Journal	FEBS Letters
Volume	282
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(91)80533-9
State	Published - May 6 1991

Bibliographical note

Funding Information:
Acknowledgements: We thank Mr Alan Davis for his assistance during the preparation of this naanuscript. These studies were supported in part by USPHS Research Grant CA-15062 awarded by the National Cancer Institute, DHHS, and by the Medical Researcla Fund of the US Department of Veterans Affairs.

Keywords

Heparin
Phosphorylation
Protein kinase C
Regulatory domain

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10.1016/0014-5793(91)80533-9

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abstract = "Heparin was found to stimulate the phosphorylation of histone H1 but not protamine sulfate catalyzed by Ca2+/phospholipid-dependent protein kinase (protein kinase C or PKC). The effect of heparin on histone H1 phosphorylation appeared to be due to an increase in phosphatidylserine affinity for PKC activation in the presence of heparin. This effect of heparin was abolisched when trypsinized, cofactor-independent, PKC was employed to phosphorylate histone H1. These studies suggest that heparin acts at the regulatory domain of PKC, and emphasize the importance of the negative charge in influencing the accessibility of the substrate to PKC action.",

keywords = "Heparin, Phosphorylation, Protein kinase C, Regulatory domain",

author = "Goueli, {Said A.} and Hanten, {John A.} and Khalil Ahmed",

note = "Funding Information: Acknowledgements: We thank Mr Alan Davis for his assistance during the preparation of this naanuscript. These studies were supported in part by USPHS Research Grant CA-15062 awarded by the National Cancer Institute, DHHS, and by the Medical Researcla Fund of the US Department of Veterans Affairs.",

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T1 - Modulation of cofactor requirement for the activation of protein kinase C by heparin Possible effect at the regulatory domain

AU - Goueli, Said A.

AU - Hanten, John A.

AU - Ahmed, Khalil

N1 - Funding Information: Acknowledgements: We thank Mr Alan Davis for his assistance during the preparation of this naanuscript. These studies were supported in part by USPHS Research Grant CA-15062 awarded by the National Cancer Institute, DHHS, and by the Medical Researcla Fund of the US Department of Veterans Affairs.

PY - 1991/5/6

Y1 - 1991/5/6

N2 - Heparin was found to stimulate the phosphorylation of histone H1 but not protamine sulfate catalyzed by Ca2+/phospholipid-dependent protein kinase (protein kinase C or PKC). The effect of heparin on histone H1 phosphorylation appeared to be due to an increase in phosphatidylserine affinity for PKC activation in the presence of heparin. This effect of heparin was abolisched when trypsinized, cofactor-independent, PKC was employed to phosphorylate histone H1. These studies suggest that heparin acts at the regulatory domain of PKC, and emphasize the importance of the negative charge in influencing the accessibility of the substrate to PKC action.

AB - Heparin was found to stimulate the phosphorylation of histone H1 but not protamine sulfate catalyzed by Ca2+/phospholipid-dependent protein kinase (protein kinase C or PKC). The effect of heparin on histone H1 phosphorylation appeared to be due to an increase in phosphatidylserine affinity for PKC activation in the presence of heparin. This effect of heparin was abolisched when trypsinized, cofactor-independent, PKC was employed to phosphorylate histone H1. These studies suggest that heparin acts at the regulatory domain of PKC, and emphasize the importance of the negative charge in influencing the accessibility of the substrate to PKC action.

KW - Heparin

KW - Phosphorylation

KW - Protein kinase C

KW - Regulatory domain

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Modulation of cofactor requirement for the activation of protein kinase C by heparin Possible effect at the regulatory domain

Abstract

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