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  1. Article ; Online: Antiproliferative factor (APF) binds specifically to sites within the cytoskeleton-associated protein 4 (CKAP4) extracellular domain.

    Chavda, Burzin / Ling, Jun / Majernick, Thomas / Planey, Sonia Lobo

    BMC biochemistry

    2017  Volume 18, Issue 1, Page(s) 13

    Abstract: Background: Antiproliferative factor (APF) is a sialoglycopeptide elevated in the urine of patients with interstitial cystitis-a chronic, painful bladder disease. APF inhibits the proliferation of normal bladder epithelial cells and cancer cells in ... ...

    Abstract Background: Antiproliferative factor (APF) is a sialoglycopeptide elevated in the urine of patients with interstitial cystitis-a chronic, painful bladder disease. APF inhibits the proliferation of normal bladder epithelial cells and cancer cells in vitro, presumably by binding to its cellular receptor, cytoskeleton associated-protein 4 (CKAP4); however, the biophysical interaction of APF with CKAP4 has not been characterized previously. In this study, we used surface plasmon resonance (SPR) to explore the binding kinetics of the interaction of APF and as-APF (a desialylated APF analogue with full activity) to CKAP4.
    Results: We immobilized non-glycosylated APF (TVPAAVVVA) to the Fc1 channel as the control and as-APF to Fc2 channel as the ligand in order to measure the binding of CKAP4 recombinant proteins encompassing only the extracellular domain (Aa 127-602) or the extracellular domain plus the transmembrane domain (Aa 106-602). Positive binding was detected to both CKAP4
    Conclusions: We determined that the CKAP4
    MeSH term(s) Amino Acid Sequence ; Binding Sites ; Cell Line, Tumor ; Extracellular Space/metabolism ; Glycoproteins/chemistry ; Glycoproteins/metabolism ; Humans ; Kinetics ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Models, Molecular ; Protein Binding ; Protein Domains ; Sequence Deletion ; Substrate Specificity ; Surface Plasmon Resonance
    Chemical Substances CKAP4 protein, human ; Glycoproteins ; Membrane Proteins ; antiproliferative factor APF, human
    Language English
    Publishing date 2017-09-11
    Publishing country England
    Document type Journal Article
    ZDB-ID 2041216-2
    ISSN 1471-2091 ; 1471-2091
    ISSN (online) 1471-2091
    ISSN 1471-2091
    DOI 10.1186/s12858-017-0088-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Targeting protein palmitoylation: selective inhibitors and implications in disease.

    Chavda, Burzin / Arnott, John A / Planey, Sonia Lobo

    Expert opinion on drug discovery

    2014  Volume 9, Issue 9, Page(s) 1005–1019

    Abstract: Introduction: Palmitoylation describes the enzymatic attachment of the 16-carbon fatty acid, palmitate, to specific cysteines of proteins via a labile thioester bond. This post-translational modification increases the lipophilicity of the modified ... ...

    Abstract Introduction: Palmitoylation describes the enzymatic attachment of the 16-carbon fatty acid, palmitate, to specific cysteines of proteins via a labile thioester bond. This post-translational modification increases the lipophilicity of the modified protein, thus regulating its subcellular distribution and function. The transfer of palmitate to a substrate is mediated by palmitoyl acyltransferases (PATs), while depalmitoylation is catalyzed by acyl protein thioesterases (APTs). Nearly one-third of the 23 genes that encode PATs are linked to human diseases, representing important targets for drug development.
    Areas covered: In this review, the authors summarize the recent technical advances in the field of palmitoylation and how they will affect our ability to understand palmitoylation and its relevance to human disease. They also review the current literature describing existing palmitoylation inhibitors. The aim of this article is to increase the awareness of the importance of palmitoylation in disease by reviewing the recent progress made in identifying pharmacological modulators of PATs/APTs. It also aims to provide suggestions for general considerations in the development of selective and potent PAT inhibitors.
    Expert opinion: Developing therapeutically useful pharmacological modulators of palmitoylation will require that they be developed within the context of well-characterized PAT/APT-related signaling systems. The successful development of potent, specific drugs in similarly complex systems suggests that development of useful drugs targeting PATs is feasible.
    MeSH term(s) Acyltransferases/antagonists & inhibitors ; Acyltransferases/genetics ; Acyltransferases/metabolism ; Animals ; Drug Design ; Enzyme Inhibitors/pharmacology ; Humans ; Lipoylation/drug effects ; Molecular Targeted Therapy ; Protein Processing, Post-Translational ; Signal Transduction/drug effects ; Substrate Specificity
    Chemical Substances Enzyme Inhibitors ; Acyltransferases (EC 2.3.-)
    Language English
    Publishing date 2014-09
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 2259618-5
    ISSN 1746-045X ; 1746-0441
    ISSN (online) 1746-045X
    ISSN 1746-0441
    DOI 10.1517/17460441.2014.933802
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6388: Show issues Location:
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  3. Article ; Online: Role of vacuolar membrane proton pumps in the acidification of protein storage vacuoles following germination.

    Wilson, Karl A / Chavda, Burzin J / Pierre-Louis, Gandhy / Quinn, Adam / Tan-Wilson, Anna

    Plant physiology and biochemistry : PPB

    2016  Volume 104, Page(s) 242–249

    Abstract: During soybean (Glycine max (L.) Merrill) seed development, protease C1, the proteolytic enzyme that initiates breakdown of the storage globulins β-conglycinin and glycinin at acidic pH, is present in the protein storage vacuoles (PSVs), the same ... ...

    Abstract During soybean (Glycine max (L.) Merrill) seed development, protease C1, the proteolytic enzyme that initiates breakdown of the storage globulins β-conglycinin and glycinin at acidic pH, is present in the protein storage vacuoles (PSVs), the same subcellular compartments in seed cotyledons where its protein substrates accumulate. Actual proteolysis begins to be evident 24 h after seed imbibition, when the PSVs become acidic, as indicated by acridine orange accumulation visualized by confocal microscopy. Imidodiphosphate (IDP), a non-hydrolyzable substrate analog of proton-translocating pyrophosphatases, strongly inhibited acidification of the PSVs in the cotyledons. Consistent with this finding, IDP treatment inhibited mobilization of β-conglycinin and glycinin, the inhibition being greater at 3 days compared to 6 days after seed imbibition. The embryonic axis does not appear to play a role in the initial PSV acidification in the cotyledon, as axis detachment did not prevent acridine orange accumulation three days after imbibition. SDS-PAGE and immunoblot analyses of cotyledon protein extracts were consistent with limited digestion of the 7S and 11S globulins by protease C1 starting at the same time and proceeding at the same rate in detached cotyledons compared to cotyledons of intact seedlings. Embryonic axis removal did slow down further breakdown of the storage globulins by reactions known to be catalyzed by protease C2, a cysteine protease that normally appears later in seedling growth to continue the storage protein breakdown initiated by protease C1.
    MeSH term(s) Acids/metabolism ; Antigens, Plant/metabolism ; Cotyledon/drug effects ; Cotyledon/metabolism ; Enzyme Inhibitors/pharmacology ; Germination/drug effects ; Globulins/metabolism ; Intracellular Membranes/drug effects ; Intracellular Membranes/metabolism ; Phosphates/pharmacology ; Plant Proteins/metabolism ; Proteolysis/drug effects ; Proton Pump Inhibitors/pharmacology ; Proton Pumps/metabolism ; Proton-Translocating ATPases/metabolism ; Seed Storage Proteins/metabolism ; Seedlings/drug effects ; Seedlings/metabolism ; Soybean Proteins/metabolism ; Glycine max/drug effects ; Glycine max/metabolism ; Vacuoles/drug effects ; Vacuoles/metabolism
    Chemical Substances Acids ; Antigens, Plant ; Enzyme Inhibitors ; Globulins ; Phosphates ; Plant Proteins ; Proton Pump Inhibitors ; Proton Pumps ; Seed Storage Proteins ; Soybean Proteins ; beta-conglycinin protein, Glycine max ; Proton-Translocating ATPases (EC 3.6.3.14)
    Language English
    Publishing date 2016-03-26
    Publishing country France
    Document type Journal Article
    ZDB-ID 742978-2
    ISSN 1873-2690 ; 0981-9428
    ISSN (online) 1873-2690
    ISSN 0981-9428
    DOI 10.1016/j.plaphy.2016.03.031
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Bonn / Germany

    Z 2696: Show issues
    Z 2005/727: Show issues

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  4. Article: Role of vacuolar membrane proton pumps in the acidification of protein storage vacuoles following germination

    Wilson, Karl A / Adam Quinn / Anna Tan-Wilson / Burzin J. Chavda / Gandhy Pierre-Louis

    Plant physiology and biochemistry. 2016 July, v. 104

    2016  

    Abstract: During soybean (Glycine max (L.) Merrill) seed development, protease C1, the proteolytic enzyme that initiates breakdown of the storage globulins β-conglycinin and glycinin at acidic pH, is present in the protein storage vacuoles (PSVs), the same ... ...

    Abstract During soybean (Glycine max (L.) Merrill) seed development, protease C1, the proteolytic enzyme that initiates breakdown of the storage globulins β-conglycinin and glycinin at acidic pH, is present in the protein storage vacuoles (PSVs), the same subcellular compartments in seed cotyledons where its protein substrates accumulate. Actual proteolysis begins to be evident 24 h after seed imbibition, when the PSVs become acidic, as indicated by acridine orange accumulation visualized by confocal microscopy. Imidodiphosphate (IDP), a non-hydrolyzable substrate analog of proton-translocating pyrophosphatases, strongly inhibited acidification of the PSVs in the cotyledons. Consistent with this finding, IDP treatment inhibited mobilization of β-conglycinin and glycinin, the inhibition being greater at 3 days compared to 6 days after seed imbibition. The embryonic axis does not appear to play a role in the initial PSV acidification in the cotyledon, as axis detachment did not prevent acridine orange accumulation three days after imbibition. SDS-PAGE and immunoblot analyses of cotyledon protein extracts were consistent with limited digestion of the 7S and 11S globulins by protease C1 starting at the same time and proceeding at the same rate in detached cotyledons compared to cotyledons of intact seedlings. Embryonic axis removal did slow down further breakdown of the storage globulins by reactions known to be catalyzed by protease C2, a cysteine protease that normally appears later in seedling growth to continue the storage protein breakdown initiated by protease C1.
    Keywords acidification ; acridine orange ; beta-conglycinin ; confocal microscopy ; cotyledons ; cysteine proteinases ; digestion ; germination ; globulins ; Glycine max ; glycinin ; imbibition ; pH ; polyacrylamide gel electrophoresis ; proteolysis ; proton pump ; pyrophosphatases ; seed development ; seedling growth ; seedlings ; soybeans ; vacuoles
    Language English
    Dates of publication 2016-07
    Size p. 242-249.
    Publishing place Elsevier Masson SAS
    Document type Article
    ZDB-ID 742978-2
    ISSN 1873-2690 ; 0981-9428
    ISSN (online) 1873-2690
    ISSN 0981-9428
    DOI 10.1016/j.plaphy.2016.03.031
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 2696: Show issues
    Z 2005/727: Show issues

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    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

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