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The Multi-Functional Calcium/Calmodulin Stimulated Protein Kinase (CaMK) Family: Emerging Targets for Anti-Cancer Therapeutic Intervention

The importance of Ca(2+) signalling in key events of cancer cell function and tumour progression, such as proliferation, migration, invasion and survival, has recently begun to be appreciated. Many cellular Ca(2+)-stimulated signalling cascades utilise the intermediate, calmodulin (CaM). The Ca(2+)/...

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Detalles Bibliográficos
Autores principales: Brzozowski, Joshua S., Skelding, Kathryn A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6469190/
https://www.ncbi.nlm.nih.gov/pubmed/30621060
http://dx.doi.org/10.3390/ph12010008
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author Brzozowski, Joshua S.
Skelding, Kathryn A.
author_facet Brzozowski, Joshua S.
Skelding, Kathryn A.
author_sort Brzozowski, Joshua S.
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description The importance of Ca(2+) signalling in key events of cancer cell function and tumour progression, such as proliferation, migration, invasion and survival, has recently begun to be appreciated. Many cellular Ca(2+)-stimulated signalling cascades utilise the intermediate, calmodulin (CaM). The Ca(2+)/CaM complex binds and activates a variety of enzymes, including members of the multifunctional Ca(2+)/calmodulin-stimulated protein kinase (CaMK) family. These enzymes control a broad range of cancer-related functions in a multitude of tumour types. Herein, we explore the cancer-related functions of these kinases and discuss their potential as targets for therapeutic intervention.
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spelling pubmed-64691902019-04-24 The Multi-Functional Calcium/Calmodulin Stimulated Protein Kinase (CaMK) Family: Emerging Targets for Anti-Cancer Therapeutic Intervention Brzozowski, Joshua S. Skelding, Kathryn A. Pharmaceuticals (Basel) Review The importance of Ca(2+) signalling in key events of cancer cell function and tumour progression, such as proliferation, migration, invasion and survival, has recently begun to be appreciated. Many cellular Ca(2+)-stimulated signalling cascades utilise the intermediate, calmodulin (CaM). The Ca(2+)/CaM complex binds and activates a variety of enzymes, including members of the multifunctional Ca(2+)/calmodulin-stimulated protein kinase (CaMK) family. These enzymes control a broad range of cancer-related functions in a multitude of tumour types. Herein, we explore the cancer-related functions of these kinases and discuss their potential as targets for therapeutic intervention. MDPI 2019-01-07 /pmc/articles/PMC6469190/ /pubmed/30621060 http://dx.doi.org/10.3390/ph12010008 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Brzozowski, Joshua S.
Skelding, Kathryn A.
The Multi-Functional Calcium/Calmodulin Stimulated Protein Kinase (CaMK) Family: Emerging Targets for Anti-Cancer Therapeutic Intervention
title The Multi-Functional Calcium/Calmodulin Stimulated Protein Kinase (CaMK) Family: Emerging Targets for Anti-Cancer Therapeutic Intervention
title_full The Multi-Functional Calcium/Calmodulin Stimulated Protein Kinase (CaMK) Family: Emerging Targets for Anti-Cancer Therapeutic Intervention
title_fullStr The Multi-Functional Calcium/Calmodulin Stimulated Protein Kinase (CaMK) Family: Emerging Targets for Anti-Cancer Therapeutic Intervention
title_full_unstemmed The Multi-Functional Calcium/Calmodulin Stimulated Protein Kinase (CaMK) Family: Emerging Targets for Anti-Cancer Therapeutic Intervention
title_short The Multi-Functional Calcium/Calmodulin Stimulated Protein Kinase (CaMK) Family: Emerging Targets for Anti-Cancer Therapeutic Intervention
title_sort multi-functional calcium/calmodulin stimulated protein kinase (camk) family: emerging targets for anti-cancer therapeutic intervention
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6469190/
https://www.ncbi.nlm.nih.gov/pubmed/30621060
http://dx.doi.org/10.3390/ph12010008
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