Last edited by Kagasho
Tuesday, July 21, 2020 | History

5 edition of Protein kinase C found in the catalog.

Protein kinase C

current concepts and future perspectives

  • 211 Want to read
  • 11 Currently reading

Published by Ellis Horwood in New York .
Written in English

    Subjects:
  • Protein kinases

  • Edition Notes

    Includes bibliographical references and index.

    Statementeditors, David S. Lester and Richard M. Epand.
    SeriesEllis Horwood series in biochemistry and biotechnology
    ContributionsLester, David S. 1953-, Epand, Richard M., 1937-
    Classifications
    LC ClassificationsQP606.P76 P75 1992, QP606.P76 P75 1992
    The Physical Object
    Paginationxii, 365 p.
    Number of Pages365
    ID Numbers
    Open LibraryOL18009231M
    ISBN 100137201869
    LC Control Number92033971

    The G protein dissociates and one subunit interacts with and activates an enzyme - adenylate cyclase- which converts ATP into a second messenger - cyclic AMP (cAMP) - in the cell. cAMP activates protein kinase A (PKA) which phosphorylates proteins at specific Ser or Thr side chains. Protein kinase C impacts on nearly every aspect of signal transduction, placing it at the forefront of research in how cells transduce information. In Protein Kinase C Protocols, leading investigators from academia and industry present a comprehensive collection of classical and emerging laboratory techniques for the study of this influential protein, all optimized for successful and.

    Protein Kinase CK2 is logically divided into three sections. The first section reviews key molecular and structural aspects of the enzyme. The second section looks at functional aspects of CK2 and the diverse roles it plays in cellular development, function, and health. The final section focuses on CK2 and cancer, looking at the impacts of the Cited by:   Although the Arabidopsis thaliana genome contains genes encoding 20 mitogen-activated protein kinases (MAPKs) and 10 MAPK kinases (MAPKKs), most of them are still functionally uncharacterized. In this work, we analyzed the function of the group B MAPK kinase, MKK3. Transgenic ProMKK3:GUS lines showed basal expression in vascular tissues that was strongly induced by Cited by:

      During drought, the plant hormone abscisic acid (ABA) triggers stomatal closure, thus reducing water loss. Using infrared thermography, we isolated two allelic Arabidopsis mutants (ost and ost) impaired in the ability to limit their transpiration upon drought. These recessive ost1 mutations disrupted ABA induction of stomatal closure as well as ABA inhibition of light-induced . Product Information. Protein kinase C (PKC), a family of serine-threonine kinases, rocketed to the forefront of the cancer research field in the early 's with its identification as an effector of phorbol esters, natural products with tumor promoting activity.


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Protein kinase C Download PDF EPUB FB2

Protein Kinase C (PKC) is a family of serine–threonine kinases found in most cell types whose activity has a strong influence on a wide variety of signal transduction events.

Alexandra C. Newton, in Handbook of Cell Signaling (Second Edition), Protein kinase C. The chapter focuses on the protein kinase C (PKC) that was originally identified as a Ca 2+ - and phospholipid-dependent protein kinase, and subsequently shown to be activated by diacylglycerols and phorbol esters.

This category is termed as conventional PKC (cPKC) to distinguish it. In Protein Kinase C Protocols, leading investigators from academia and industry present a comprehensive collection of classical and emerging laboratory techniques for the study of this influential protein, all optimized for successful and reproducible results.

Described in step-by-step detail, these methods can be easily used to explore the Format: Hardcover. PKC causes phosphorylation of membrane-bound regulatory proteins in VSM. MARCKS (myristoylated, alanine-rich C kinase substrate), a major PKC substrate, is bound to F-actin and may function as a cross-bridge between cytoskeletal actin and the plasma membrane [].Also, PKC causes phosphorylation of the inhibitory GTP-binding protein G i, facilitating the dissociation of the α i subunit from Cited by: 1.

Protein kinase B (PKB), also known as Akt, is a serine/threonine-specific protein kinase that plays a key role in multiple cellular processes such as glucose metabolism, apoptosis, cell proliferation, transcription and cell migration.

1 Family members - Isoforms. Binding phospholipids. HGNC: rows  We used ePK and aPK HMMs, and Blast/psi-Blast with divergent kinase sequences, to. Open Library is an open, editable library catalog, building towards a web page for every book ever published.

Protein kinase C by Lodewijk V. Dekker,Springer edition, paperback Protein Kinase C ( edition) | Open Library. It gets added by a protein kinase. So protein kinase uses ATP, transfers that gamma phosphate to a protein. So now you have many proteins, more than half the proteins in our bodies exist either as a dephosphorylated molecule or as a phosphorylated molecule.

ISBN: OCLC Number: Description: x, pages: illustrations ; 24 cm: Contents: Protein kinase C: history and perspective / Peter J. Parker --Molecular and catalytic properties of protein kinase C / Charles W. Mahoney and Kuo-Ping Huang --Molecular mechanism of protein kinase C regulation by lipids / Andrew F.G.

Quest and Robert M. Bell --Protein kinase C. Get this from a library. Protein kinase C. [Lodewijk V Dekker;] -- Devoted entirely to Protein Kinase C, this book forms a major point of reference for those active in the field. In addition it will appeal to those with a general interest in biochemistry, cell.

Diacylglycerol binds to and activates protein kinase C (PKC). The IP3 binds to ligand-gated receptor/Ca++ channels on internal membranes, leading to an influx of calcium ions into the cytoplasm.

Calcium ions bind to a calcium modulatory protein, calmodulin, which binds to and activates the calmodulin-dependent kinase (CAM-PK). Since the discovery that protein kinase C (PKC) transduces the ab- dance of signals that result in phospholipid hydrolysis, this enzyme has been at the forefront of research in signal transduction.

Protein Kinase C Protocols covers fundamental methods for studying the structure, function. Gschwendt, M., Kielbassa, K., Kittstein, W., and Marks, F.

() Tyrosine phosphorylation and stimulation of protein kinase C delta from porcine spleen by src in vitro. Dependence on the activated state of protein kinase C delta.

FEBS Lett. 85– PubMed CrossRef Google ScholarCited by: 7. An association between protein kinase C (PKC) signaling and T cell proliferation has been recognized for almost three decades.

Over 30 years ago, it was determined that a combination of phorbol esters and elevated intracellular calcium potently induces proliferation of cells of the T cell lineage (e.g., Whitfield et al., ; Lyall et al., ; Sutherland et al., ).Cited by: In Protein Kinase C Protocols, leading investigators from academia and industry present a comprehensive collection of classical and emerging laboratory techniques for the study of this influential protein, all optimized for successful and reproducible results.

kinase was the first protein kinase to be characterized biochemically and the mechanism of its regula-tion led to the discovery of cAMP-dependent protein kinase (protein kinase A, or PKA), which catalyzes the phosphorylation and activation of phosphorylase kinase.

This was the first protein kinase cascade or signaling module to be elucidated. Structure. Members of the protein kinase C family are a single polypeptide, comprised of an N-terminal regulatory region (approximately kDa) and a C-terminal catalytic region (approximately 45 kDa) ().Cloning of the first isozymes in the mids revealed four conserved domains: C1-C4().Each is a functional module, and many unrelated proteins have one or the other().

A protein kinase is a kinase enzyme that modifies other proteins by chemically adding phosphate groups to them (phosphorylation).Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other human genome contains about protein kinase genes and they constitute about 2% of all human genes.

Protein Kinase C in Cancer Signaling and Therapy is composed of twenty-three chapters written by leading experts in the field. The book is divided into four sections: Regulation of PKC isozyme function: from genes to biochemistry, PKC isozymes in the control of cell function, PKC isozymes in cancer, and PKC isozymes as targets for cancer therapy.

Ongoing research emphasizes 1) protein kinase C and MAP kinase signaling pathways induced by fatty acids in tumor cells in vitro, 2) mechanisms of tumor cell adhesion, migration, and invasion in vitro, 3) alterations in cytoskeletal structures in metastatic tumor cells, and 4) the role of protein glycosylation in tumor cell behavior.

Proteins are the work horses of the cell. As regulators of protein function, protein kinases are involved in the control of cellular functions via intricate signalling pathways, allowing for fine tuning of physiological functions. This book is a collaborative effort, with contribution from experts in their respective fields, reflecting the spirit of collaboration - across disciplines and.Protein Kinase C is a pivotal component of the mechanism that allows a cell to respond to its changing environment.

In this book, the most significant advances in recent basic research on Protein Kinase C are explained by active researchers in the field. The first seven chapters provide a comprehensive account of the fundamental structural and biochemical properties of Protein Kinase C.protein kinase C: any of a number of cytoplasmic calcium-activated kinases involved in numerous processes, including hormonal binding, platelet activation, and tumor promotion.