Get Protein Kinase C in Cancer Signaling and Therapy PDF

By Alex Toker (auth.), Marcelo G. Kazanietz (eds.)

ISBN-10: 1607615428

ISBN-13: 9781607615422

Protein kinase C (PKC), a relatives of serine-threonine kinases, rocketed to the vanguard of the melanoma learn box within the early 1980’s with its identity as an effector of phorbol esters, average items with tumor-promoting job. Phorbol esters had lengthy been of curiosity to the melanoma examine box because of early experiences within the mouse dermis carcinogenesis version, which confirmed that lengthy topical software of phorbol esters promoted the formation of epidermis tumors on mice formerly taken care of with mutagenic brokers.

Research within the final years has validated key roles for PKC isozymes within the regulate of phone proliferation, migration, adhesion, and malignant transformation. furthermore, there's a huge physique of proof linking PKC to invasion and melanoma telephone metastasis. it's now good validated that the expression of PKC isozymes is altered in quite a few forms of cancers. extra importantly, small molecule inhibitors were constructed with major anti-cancer job. The relevance of PKC isozymes in melanoma signaling is hence remarkable.

Protein Kinase C in melanoma Signaling and remedy consists of twenty-three chapters written by way of prime specialists within the box. The booklet is split into 4 sections: legislation of PKC isozyme functionality: from genes to biochemistry, PKC isozymes within the keep watch over of mobile functionality, PKC isozymes in melanoma, and PKC isozymes as pursuits for melanoma remedy. every one component of Protein Kinase C in melanoma Signaling and remedy starts off with an advent by means of a longtime expert within the box of Protein kinase C, through chapters that elucidate the significance of PKC in present melanoma research.

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Additional info for Protein Kinase C in Cancer Signaling and Therapy

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Corbalan-Garcia, S. (2001). Identification of the Phosphatidylserine Binding Site in the C2 Domain that Is Important for PKCalpha Activation and in Vivo Cell Localization. Biochemistry, 40(46), 13898–13905. C. (2007). The C2 domains of classical/conventional PKCs are specific PtdIns(4,5)P(2)-sensing domains. Biochemical Society Transactions, 35(Pt 5), 1046–1048. C. (2007). A single residue in the C1 domain sensitizes novel protein kinase C isoforms to cellular diacylglycerol production. The Journal Biologica Chemistry, 282(2), 826–830.

Biochemistry, 37(35), 12020–12025. , Wong. , et al. (1994). Zinc Finger Domains and Phorbol Ester Pharmacophore: Analysis of binding to mutated form of protein kinase C z and the vav and c-raf proto-oncogene products. The Journal Biological Chemistry, 269, 11590–11594. C. C. (1995). Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. Current Biology, 5(12), 1394–1403. , et al (2003). Interaction codes within the family of mammalian Phox and Bem1p domain-containing proteins.

2008). The chaperones Hsp90 and Cdc37 mediate the maturation and stabilization of protein kinase C through a conserved PXXP motif in the C-terminal tail. The Journal of Biological Chemistry, 284(8), 4921–4835. C. (2008). The life and death of protein kinase C. Current Drug Targets, 9(8), 614–625. G. (2007). Protein kinase C and other diacylglycerol effectors in cancer. Nature Reviews. Cancer, 7(4), 281–294. , et al. (2006). Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1.

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Protein Kinase C in Cancer Signaling and Therapy by Alex Toker (auth.), Marcelo G. Kazanietz (eds.)

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