CG&D
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ikuta, T.
Right arrow Articles by Kuroki, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ikuta, T.
Right arrow Articles by Kuroki, T.

Cell Growth & Differentiation, Vol 5, Issue 9 943-947, Copyright © 1994 by American Association of Cancer Research


ARTICLES

Cholesterol sulfate, a novel activator for the eta isoform of protein kinase C

T Ikuta, K Chida, O Tajima, Y Matsuura, M Iwamori, Y Ueda, K Mizuno, S Ohno and T Kuroki
Department of Cancer Cell Research, University of Tokyo, Japan.

Activity of protein kinase C depends on the interaction with polar head-groups of two membrane lipids, i.e., phosphatidylserine and diacylglycerol. In the present study, we demonstrated a novel activation mechanism of the eta isoform of protein kinase C (nPKC eta), which is predominantly expressed in epithelial tissues in close association with epithelial differentiation. We found that the nPKC eta was activated by cholesterol sulfate, a metabolite of cholesterol formed during squamous differentiation. This activation was greater than that by phosphatidylserine plus phorbol ester; the Vmax for the activation by cholesterol sulfate was 3.6 times that by phosphatidylserine plus phorbol ester, while Kms were almost equal. In the presence of cholesterol sulfate, phorbol ester only weakly enhanced the activity of nPKC eta. Activation of nPKC eta by cholesterol sulfate was further demonstrated by autophosphorylation of the kinase molecule. However, the alpha and delta isoforms of protein kinase C were not activated by cholesterol sulfate. The present observation affords a new insight into a signal transduction pathway of squamous differentiation.


This article has been cited by other articles:


Home page
Mol. Biol. CellHome page
Y. Shirai, S. Morioka, M. Sakuma, K.-i. Yoshino, C. Otsuji, N. Sakai, K. Kashiwagi, K. Chida, R. Shirakawa, H. Horiuchi, et al.
Direct binding of RalA to PKC{eta} and its crucial role in morphological change during keratinocyte differentiation
Mol. Biol. Cell, April 15, 2011; 22(8): 1340 - 1352.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
P. M. Elias, M. L. Williams, W. M. Holleran, Y. J. Jiang, and M. Schmuth
Thematic review series: Skin Lipids. Pathogenesis of permeability barrier abnormalities in the ichthyoses: inherited disorders of lipid metabolism
J. Lipid Res., April 1, 2008; 49(4): 697 - 714.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
W. B. Rizzo, D. A. Craft, T. Somer, G. Carney, J. Trafrova, and M. Simon
Abnormal fatty alcohol metabolism in cultured keratinocytes from patients with Sjogren-Larsson syndrome
J. Lipid Res., February 1, 2008; 49(2): 410 - 419.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
C. A. Strott and Y. Higashi
Cholesterol sulfate in human physiology: what's it all about?
J. Lipid Res., July 1, 2003; 44(7): 1268 - 1278.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Lung Cell. Mol. Physiol.Home page
L. H. Abdullah, J. T. Bundy, C. Ehre, and C. W. Davis
Mucin secretion and PKC isoforms in SPOC1 goblet cells: differential activation by purinergic agonist and PMA
Am J Physiol Lung Cell Mol Physiol, July 1, 2003; 285(1): L149 - L160.
[Abstract] [Full Text] [PDF]


Home page
Cancer Res.Home page
K. Chida, T. Hara, T. Hirai, C. Konishi, K. Nakamura, K. Nakao, A. Aiba, M. Katsuki, and T. Kuroki
Disruption of Protein Kinase C{eta} Results in Impairment of Wound Healing and Enhancement of Tumor Formation in Mouse Skin Carcinogenesis
Cancer Res., May 15, 2003; 63(10): 2404 - 2408.
[Abstract] [Full Text] [PDF]


Home page
Cancer Res.Home page
A. Alt, M. Ohba, L. Li, M. Gartsbein, A. Belanger, Mitchell. F. Denning, T. Kuroki, S. H. Yuspa, and T. Tennenbaum
Protein Kinase C{{delta}}-mediated Phosphorylation of {{alpha}}6{beta}4 Is Associated with Reduced Integrin Localization to the Hemidesmosome and Decreased Keratinocyte Attachment
Cancer Res., June 1, 2001; 61(11): 4591 - 4598.
[Abstract] [Full Text] [PDF]


Home page
J Biol ChemHome page
Z. Nemes, M. Demeny, L. N. Marekov, L. Fesus, and P. M. Steinert
Cholesterol 3-Sulfate Interferes with Cornified Envelope Assembly by Diverting Transglutaminase 1 Activity from the Formation of Cross-links and Esters to the Hydrolysis of Glutamine
J. Biol. Chem., January 28, 2000; 275(4): 2636 - 2646.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
M. Ohba, K. Ishino, M. Kashiwagi, S. Kawabe, K. Chida, N.-H. Huh, and T. Kuroki
Induction of Differentiation in Normal Human Keratinocytes by Adenovirus-Mediated Introduction of the eta  and delta  Isoforms of Protein Kinase C
Mol. Cell. Biol., September 1, 1998; 18(9): 5199 - 5207.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation
Copyright © 1994 by the American Association of Cancer Research.