Last edited by Voshakar
Thursday, May 14, 2020 | History

3 edition of Glutathione S-transferases and drug resistance found in the catalog.

Glutathione S-transferases and drug resistance

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Published by Taylor & Francis in London, New York .
Written in English

    Subjects:
  • Glutathione transferase -- Congresses.,
  • Drug resistance -- Congresses.,
  • Drugs -- Metabolic detoxification -- Congresses.,
  • Drug Resistance -- immunology -- congresses.,
  • Glutathione Transferases -- congresses.

  • Edition Notes

    Statementedited by J.D. Hayes, C.B. Pickett, and T.J. Mantle.
    ContributionsHayes, J. D., Pickett, C. B., Mantle, T. J., University of Edinburgh. Dept. of Clinical Chemistry., International GST Conference (3rd : 1989 : Royal College of Physicians of Edinburgh)
    Classifications
    LC ClassificationsQP606.G59 G58 1990
    The Physical Object
    Paginationxv, 459 p. :
    Number of Pages459
    ID Numbers
    Open LibraryOL1858233M
    ISBN 100850667895
    LC Control Number90010743

    Glutathione transferase (formerly GST) catalyzes the inactivation of various electrophile-producing anticancer agents via conjugation to the tripeptide glutathione. Moreover, several data link the overexpression of some GSTs, in particular GSTP, to both natural and acquired resistance to various structurally unrelated anticancer drugs. Tumor overexpression of these proteins has Cited by: Novel drugs that affect glutathione metabolism; the regulation of genes encoding drug-metabolizing enzymes in normal and preneoplastic tissues; and the relevance of glutathione S-transferases to anticancer drug resistance are also considered. The book further tackles the cellular resistance to cyclophosphamide; the preclinical and clinical.

    General mechanisms of resistance are discussed, including the drug resistance related proteins p­ glycoprotein, MRP (multi-drug resistance protein) and LRP (lung resistance protein), and the role of glutathione and glutathione-S-transferases. Moreover, more drug type-specific mechanisms of resistance are a topic, such as for glucocorticoids. Key words: Diamondback moth, glutathione S-transferase, insecticide resistance Introduction Glutathione S-transferases (GSTs, EC) are a family of enzymes that catalyze the nucleophilic attack of the sulfur atom of glutathione on the electrophilie center of many chemical compounds (Mannervik and Danielson, ). The GSTs, in addition to.

    Glutathione S-transferases (GSTs) are an important family of the detoxifying enzymes catalyzing the conjugation of glutathione to a wide variety of hydrophobic electrophilic substances [1]. GSTs have various isoenzymes which have been studied extensively in rats [2].Cited by: 3. Glutathione S-transferases form homodimers, but in eukaryotes can also form heterodimers of the A1 and A2 or YC1 and YC2 subunits. The homodimeric enzymes display a conserved structural fold. Each monomer is composed of a distinct N-terminal sub-domain, which adopts the thioredoxin fold, and a C-terminal all-helical ro: IPR


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Glutathione S-transferases and drug resistance Download PDF EPUB FB2

Development of drug resistance is a key element in the failure of chemotherapy treatment. Exposure to anticancer agents may lead to the induction and expression of gene products that protect the by:   1.

Oncogene. Oct 20;22(47) The role of glutathione-S-transferase in anti-cancer drug resistance. Townsend DM(1), Tew KD. Author information: (1)Department of Pharmacology, Fox Chase Cancer Center, Burholme Avenue, Philadelphia, PAUSA.

Glutathione-S-transferases (GSTs) are a family of Phase II detoxification enzymes that Cited by: Glutathione and glutathione S-transferases (GST) are the focus of much attention in characterizing drug resistant cells. However, ambiguous and sometimes conflicting data have complicated the field.

Part 1 Enzymology of the glutathione S-transferases, the glutathione S-transferases and their contribution to drug resistance in nature,t and ; rapid purification of glutathione S-tranferases by gradient affinity elution of the glutathione-agarose and the S-hexylglutathione-agarose chromatography matrics,   William B.

Coleman PhD, in Molecular Pathology (Second Edition), GSTP1. Glutathione S-transferases are enzymes responsible for the detoxification of reactive chemical species through conjugation to reduced glutathione.

The GSTP1 gene, encoding the pi class glutathione S-transferase, was the first hypermethylated gene to be characterized in prostate. The major roles of glutathione (GSH) and glutathione S-transferases (GSTs) in the detoxification of xenobiotics predicts their important role in drug resistance.

As such, both GSH and GSTs have been manipulated as targets in the design of novel chemotherapeutic by: 2. Author: Kenneth D. Tew,Cecil B. Pickett,Timothy J.

Mantle,Bengt Mannervik; Publisher: CRC Press ISBN: Category: Medical Page: View: DOWNLOAD NOW» Structure and Function of Glutathione S-Transferases provides some of the latest information available on a variety of structural and functional components of glutathione S-transferases, a.

Glutathione S-transferases (GSTs), previously known as ligandins, comprise a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification.

The GST family consists of three superfamilies: the cytosolic, mitochondrial, and BRENDA: BRENDA entry. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance Study on PubMed.

GST's on Wikipedia. On Amazon (a thorough book on GST's): Glutathione S-Transferases: Structure, Function and Clinical Implications. 6 Glutathione and Herbicide Resistance in Plants Anderson JV, Davis DG () Abiotic stress alters transcript prof iles and activity of glutathione S.

Structure and Function of Glutathione S-Transferases provides some of the latest information available on a variety of structural and functional components of glutathione S-transferases, a family of isozymes involved in many endogenous and exogenous functions in cells.

and the role that these enzymes play in governing drug resistance at the Cited by: Dulik, D.M. and Fenselau, C.

Conversion of melphalan to 4— (glutathionyl) phenylalanine a novel mechanism for conjugation by glutathione—s—transferases. Drug Metab. Dis. – Google ScholarCited by: 1. Crit Rev Biochem Mol Biol.

;30(6) The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotectioCited by: V Mechanisms of anticancer drug resistance A.L. Harris v~ Glutathione S-transferases in resistance to chemotherapeutic drugs C.R.

Wolf, C.J. Wareing, S.M. Black and J.D. Hayes K Glutathione S-transferases and resistance to alkylating agents K.D. Tew, J.C. Schisselbauer, M.L Clapper and S. Kuzmich Glutathione S-transferase pi and.

9 Glutathione S-Transferases and Anticancer I. Introduction II. The Resistant Phenotype in Walker Rat Breast Carcinoma Cells III. Drug Resistance and an Altered Glutathione STransferase Phenotype in Cell Culture IV.

Subcellular Compartmentalization of Glutathione S-Transferases V. Glutathione S-Transferases in Human Biopsies VI. DiscussionBook Edition: 1. La-aied Prapanthadara, Janet Hemingway and Albert J.

Ketterman, DDT-resistance in Anopheles gambiae (Diptera: Culicidae) from Zanzibar, Tanzania, based on increased DDT-dehydrochlorinase activity of glutathione S-transferases, Bulletin of Entomological Research, 85, 02, (), ().Cited by: Glutathione-S-transferases (GSTs) are a family of Phase II detoxification enzymes that catalyse the conjugation of glutathione (GSH) to a wide variety of endogenous and exogenous electrophilic compounds.

GSTs are divided into two distinct super-family members: the membrane-bound microsomal and cytosolic family members. General mechanisms of resistance are discussed, including the drug resistance related proteins p glycoprotein, MRP (multi-drug resistance protein) and LRP (lung resistance protein), and the role of glutathione and glutathione-S-transferases.

Moreover, more drug type-specific mechanisms of resistance are a topic, such as for glucocorticoids and. Glutathione S-Transferases: Structure, Function and Clinical Implications: Medicine & Health Science Books @ hor: Gerard J. Mulder. Metabolism of a number of carcinogens and drugs is covered in detail, and the role that these enzymes play in governing drug resistance at the preclinical and clinical levels is discussed.

The book will be excellent for biochemists, pharmacologists, oncologists, experimental therapeutic specialists, and others interested in glutathione S.

Structure and Function of Glutathione S-Transferases provides some of the latest information available on a variety of structural and functional components of glutathione S-transferases, a family of isozymes involved in many endogenous and exogenous functions in cells.

and the role that these enzymes play in governing drug resistance at the.The Glutathione S-Transferase (GST) AssayKit utilizes 1-Chloro-2,4-dinitrobenzene (CDNB) which is suitable for the broadest range of GST isozymes.

Upon conjugation of the thiol group of glutathione to the CDNB substrate, there is an increase in the absorbance at nm. The Glutathione S-Transferase (GST) Assay Kit isFile Size: KB.Glutathione S-transferases (GSTs) play crucial roles in the detoxification process and the development of drug-resistance and are proved to be important markers for various tumors.

Different from the previous probes, we developed a fluorescent probe enabling the detection of intracellular GSTs in a low GSH level environment by pre-treatment of.