A Dulhunty

Summary

Affiliation: Australian National University
Country: Australia

Publications

  1. doi request reprint Proteins within the intracellular calcium store determine cardiac RyR channel activity and cardiac output
    Angela F Dulhunty
    Department of Translational Biosciences, John Curtin School of Medical Research, Australian National University, Canberra, Australian Capital Territory, Australia
    Clin Exp Pharmacol Physiol 39:477-84. 2012
  2. doi request reprint Regulation of the cardiac muscle ryanodine receptor by glutathione transferases
    Angela F Dulhunty
    John Curtin School of Medical Research, Australian National University, Canberra City, Australia
    Drug Metab Rev 43:236-52. 2011
  3. pmc The recombinant dihydropyridine receptor II-III loop and partly structured 'C' region peptides modify cardiac ryanodine receptor activity
    Angela F Dulhunty
    Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, PO Box 334, Canberra, ACT 2601, Australia
    Biochem J 385:803-13. 2005
  4. pmc Functional implications of modifying RyR-activating peptides for membrane permeability
    Angela F Dulhunty
    Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, PO Box 334, Canberra, ACT 2601, Australia
    Br J Pharmacol 144:743-54. 2005
  5. pmc A recently identified member of the glutathione transferase structural family modifies cardiac RyR2 substate activity, coupled gating and activation by Ca2+ and ATP
    Angela F Dulhunty
    Division of Molecular Bioscience, John Curtin School of Medical Research, P O Box 334, Canberra, ACT 2601, Australia
    Biochem J 390:333-43. 2005
  6. ncbi request reprint Multiple actions of imperatoxin A on ryanodine receptors: interactions with the II-III loop "A" fragment
    Angela F Dulhunty
    Division of Molecular Bioscience, John Curtin School of Medical Research and Research School of Chemistry, Canberra, Australian Capital Territory 2601, Australia
    J Biol Chem 279:11853-62. 2004
  7. pmc Peptide fragments of the dihydropyridine receptor can modulate cardiac ryanodine receptor channel activity and sarcoplasmic reticulum Ca2+ release
    Angela F Dulhunty
    John Curtin School of Medical Research, Australian National University, Canberra, ACT 2601, Australia
    Biochem J 379:161-72. 2004
  8. ncbi request reprint Excitation-contraction coupling from the 1950s into the new millennium
    A F Dulhunty
    Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, Australian Capital Territory, Australia
    Clin Exp Pharmacol Physiol 33:763-72. 2006
  9. ncbi request reprint Novel regulators of RyR Ca2+ release channels: insight into molecular changes in genetically-linked myopathies
    A F Dulhunty
    Division of Molecular Bioscience, JCSMR and RSC, ANU, Canberra, ACT, 2601, Australia
    J Muscle Res Cell Motil 27:351-65. 2006
  10. ncbi request reprint Interactions between dihydropyridine receptors and ryanodine receptors in striated muscle
    A F Dulhunty
    John Curtin School of Medical Research, Australian National University, P O Box 334 2601 Canberra, Australia
    Prog Biophys Mol Biol 79:45-75. 2002

Collaborators

Detail Information

Publications48

  1. doi request reprint Proteins within the intracellular calcium store determine cardiac RyR channel activity and cardiac output
    Angela F Dulhunty
    Department of Translational Biosciences, John Curtin School of Medical Research, Australian National University, Canberra, Australian Capital Territory, Australia
    Clin Exp Pharmacol Physiol 39:477-84. 2012
    ..Herein, we discuss known interactions between the RyR, triadin, junctin and CSQ with emphasis on the cardiac isoforms of the proteins. Where there is little known about the cardiac isoforms, we discuss evidence from skeletal isoforms...
  2. doi request reprint Regulation of the cardiac muscle ryanodine receptor by glutathione transferases
    Angela F Dulhunty
    John Curtin School of Medical Research, Australian National University, Canberra City, Australia
    Drug Metab Rev 43:236-52. 2011
    ..We conclude that the C-terminal part of GSTM2-2 may provide the basis of a therapeutic compound for use in cardiac disorders...
  3. pmc The recombinant dihydropyridine receptor II-III loop and partly structured 'C' region peptides modify cardiac ryanodine receptor activity
    Angela F Dulhunty
    Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, PO Box 334, Canberra, ACT 2601, Australia
    Biochem J 385:803-13. 2005
    ..The data provide novel evidence that the DHPR II-III loop and its C region interact with cardiac RyR2, and that the ability to interact is not isoform-specific...
  4. pmc Functional implications of modifying RyR-activating peptides for membrane permeability
    Angela F Dulhunty
    Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, PO Box 334, Canberra, ACT 2601, Australia
    Br J Pharmacol 144:743-54. 2005
    ..7. The results show that lipoamino acid conjugation of A region peptides increases their membrane permeability without impairing their structure or efficacy in activating skeletal and cardiac RyRs...
  5. pmc A recently identified member of the glutathione transferase structural family modifies cardiac RyR2 substate activity, coupled gating and activation by Ca2+ and ATP
    Angela F Dulhunty
    Division of Molecular Bioscience, John Curtin School of Medical Research, P O Box 334, Canberra, ACT 2601, Australia
    Biochem J 390:333-43. 2005
    ..CLIC-2 provides a unique probe for substate activity, coupled gating and ligand-induced activation of cardiac RyR channels...
  6. ncbi request reprint Multiple actions of imperatoxin A on ryanodine receptors: interactions with the II-III loop "A" fragment
    Angela F Dulhunty
    Division of Molecular Bioscience, John Curtin School of Medical Research and Research School of Chemistry, Canberra, Australian Capital Territory 2601, Australia
    J Biol Chem 279:11853-62. 2004
    ..The results suggest that Imperatoxin A has three independent actions on ryanodine receptor channels and competes with peptide A for at least one action...
  7. pmc Peptide fragments of the dihydropyridine receptor can modulate cardiac ryanodine receptor channel activity and sarcoplasmic reticulum Ca2+ release
    Angela F Dulhunty
    John Curtin School of Medical Research, Australian National University, Canberra, ACT 2601, Australia
    Biochem J 379:161-72. 2004
    ..This is the first report of specific functional interactions between dihydropyridine receptor A region peptides and cardiac RyR ion channels in lipid bilayers...
  8. ncbi request reprint Excitation-contraction coupling from the 1950s into the new millennium
    A F Dulhunty
    Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, Australian Capital Territory, Australia
    Clin Exp Pharmacol Physiol 33:763-72. 2006
    ..Nevertheless, a multitude of questions about the molecular interactions and structures of the proteins and their interaction sites remain to be answered and provide a challenge for the next 50 years...
  9. ncbi request reprint Novel regulators of RyR Ca2+ release channels: insight into molecular changes in genetically-linked myopathies
    A F Dulhunty
    Division of Molecular Bioscience, JCSMR and RSC, ANU, Canberra, ACT, 2601, Australia
    J Muscle Res Cell Motil 27:351-65. 2006
    ....
  10. ncbi request reprint Interactions between dihydropyridine receptors and ryanodine receptors in striated muscle
    A F Dulhunty
    John Curtin School of Medical Research, Australian National University, P O Box 334 2601 Canberra, Australia
    Prog Biophys Mol Biol 79:45-75. 2002
    ..However, complexities are emerging and evidence has now been obtained for a bi-directional physical coupling between the proteins in cardiac as well as skeletal muscle. The molecular nature of this coupling remains to be elucidated...
  11. ncbi request reprint The ryanodine receptor: a pivotal Ca2+ regulatory protein and potential therapeutic drug target
    Angela F Dulhunty
    John Curtin School of Medical Research, Australian National University, PO Box 334, ACT 2601, Australia
    Curr Drug Targets 12:709-23. 2011
    ....
  12. pmc Characteristics of irreversible ATP activation suggest that native skeletal ryanodine receptors can be phosphorylated via an endogenous CaMKII
    A F Dulhunty
    Muscle Research Group, John Curtin School of Medical Research, Canberra, ACT 2601, Australia
    Biophys J 81:3240-52. 2001
    ..The results suggest that CaMKII is anchored to skeletal muscle RyRs and that phosphorylation by this kinase alters the enhancement of channel activity by ATP and Ca(2+)...
  13. ncbi request reprint How many cysteine residues regulate ryanodine receptor channel activity?
    A Dulhunty
    Muscle Research Group, John Curtin School of Medical Research, Australian National University, ACT, Canberra
    Antioxid Redox Signal 2:27-34. 2000
    ..These cysteine residues may be selectively modified under physiological and pathological conditions to regulate Ca2+ release from the sarcoplasmic reticulum and contraction...
  14. ncbi request reprint Role of some unconserved residues in the "C" region of the skeletal DHPR II-III loop
    Angela F Dulhunty
    Division of Molecular Bioscience, JCSMR and Research School of Chemistry, ANU, Canberra, ACT 2601, Australia
    Front Biosci 10:1368-81. 2005
    ....
  15. pmc Junctin and triadin each activate skeletal ryanodine receptors but junctin alone mediates functional interactions with calsequestrin
    Lan Wei
    John Curtin School of Medical Research, Australian National University, PO Box 334, Canberra City, ACT 2601, Australia
    Int J Biochem Cell Biol 41:2214-24. 2009
    ..We suggest that triadin serves a different function which may dominate during excitation-contraction coupling...
  16. pmc The random-coil 'C' fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
    Claudia S Haarmann
    Muscle Research Group, John Curtin School of Medical Research, Australian National University, P O Box 334, Canberra, ACT 2601, Australia
    Biochem J 372:305-16. 2003
    ..These interactions could reflect either dynamic changes that occur during excitation-contraction coupling or interactions between the proteins at rest...
  17. pmc The conformation of calsequestrin determines its ability to regulate skeletal ryanodine receptors
    Lan Wei
    John Curtin School of Medical Research, Australian Capital Territory, Australia
    Biophys J 91:1288-301. 2006
    ....
  18. doi request reprint Redox potential and the response of cardiac ryanodine receptors to CLIC-2, a member of the glutathione S-transferase structural family
    Chris Jalilian
    Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, ACT, Australia
    Antioxid Redox Signal 10:1675-86. 2008
    ....
  19. doi request reprint Muscle-specific GSTM2-2 on the luminal side of the sarcoplasmic reticulum modifies RyR ion channel activity
    Lan Wei
    Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, PO Box 334, Canberra City, ACT 2601, Australia
    Int J Biochem Cell Biol 40:1616-28. 2008
    ..The results indicate that GSTM2-2 is a novel luminal regulator of the RyR channels in the heart...
  20. ncbi request reprint Altered mRNA splicing of the skeletal muscle ryanodine receptor and sarcoplasmic/endoplasmic reticulum Ca2+-ATPase in myotonic dystrophy type 1
    Takashi Kimura
    Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, PO Box 334, Canberra ACT 2601, Australia
    Hum Mol Genet 14:2189-200. 2005
    ..We suggest that aberrant splicing of RyR1 and SERCA1 mRNAs might contribute to impaired Ca2+ homeostasis in DM1 muscle...
  21. ncbi request reprint The Mu class glutathione transferase is abundant in striated muscle and is an isoform-specific regulator of ryanodine receptor calcium channels
    Yasser Abdellatif
    Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, P O Box 334, Canberra City, ACT 2601, Australia
    Cell Calcium 41:429-40. 2007
    ..The results suggest that the major GST isoform expressed in muscle regulates Ca2+ signalling in skeletal and cardiac muscle and conserves Ca2+ stores in the sarcoplasmic reticulum...
  22. doi request reprint The structure of the C-terminal helical bundle in glutathione transferase M2-2 determines its ability to inhibit the cardiac ryanodine receptor
    Ruwani Hewawasam
    Structural Biology Program, John Curtin School of Medical Research, Australian National University, PO Box 334, Canberra, ACT 2601, Australia
    Biochem Pharmacol 80:381-8. 2010
    ....
  23. doi request reprint Unique isoform-specific properties of calsequestrin in the heart and skeletal muscle
    Lan Wei
    John Curtin School of Medical Research, Australian Capital Territory, Australia
    Cell Calcium 45:474-84. 2009
    ....
  24. ncbi request reprint The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator
    A Dulhunty
    John Curtin School of Medical Research, Australian National University, P O Box 334, Canberra, Australian Capital Territory 2601, Australia
    J Biol Chem 276:3319-23. 2001
    ..We propose a novel role for GSTO1-1 in protecting cells containing RyR2 from apoptosis induced by Ca(2+) mobilization from intracellular stores...
  25. doi request reprint Dissection of the inhibition of cardiac ryanodine receptors by human glutathione transferase GSTM2-2
    Dan Liu
    John Curtin School of Medical Research, Australian National University, Canberra, Australia
    Biochem Pharmacol 77:1181-93. 2009
    ..GSTM2-2 helices 5-8 may provide the basis for RyR2-specific compounds for experimental and therapeutic use...
  26. ncbi request reprint Caffeine sensitivity of native RyR channels from normal and malignant hyperthermic pigs: effects of a DHPR II-III loop peptide
    Esther M Gallant
    Muscle Researh Group, John Curtin School of Medical Research, Canberra, ACT 2601, Australia
    Am J Physiol Cell Physiol 286:C821-30. 2004
    ..the sensitivity of RyRs to a skeletal II-III loop peptide was depressed, and 3). an interaction between the caffeine and peptide C(S) activation mechanisms seen in normal RyRs was lost...
  27. pmc The three-dimensional structural surface of two beta-sheet scorpion toxins mimics that of an alpha-helical dihydropyridine receptor segment
    Daniel Green
    Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, P O Box 334, Canberra, ACT, 2601, Australia
    Biochem J 370:517-27. 2003
    ..These results suggest that diverse structural scaffolds can present similar conformational surface properties to target common receptor sites...
  28. ncbi request reprint Effects of an alpha-helical ryanodine receptor C-terminal tail peptide on ryanodine receptor activity: modulation by Homer
    Pierre Pouliquin
    Division of Molecular Bioscience, JCSMR and RSC, ANU, Canberra, ACT 2601, Australia
    Int J Biochem Cell Biol 38:1700-15. 2006
    ..We found that Homer 1b not only interacts with the channels, but reduces the inhibitory action of the C-terminal tail peptide, perhaps by stabilizing inter-domain interactions and preventing their disruption...
  29. pmc Calsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channels
    Nicole A Beard
    Division of Biochemistry and Molecular Biology, John Curtin School of Medical Research, Australian National University, Canberra, ACT 0200, Australia
    Biophys J 82:310-20. 2002
    ..We suggest that calsequestrin reduces ryanodine receptor activity by binding to a coprotein, possibly to the luminal domain of triadin...
  30. pmc A variably spliced region in the type 1 ryanodine receptor may participate in an inter-domain interaction
    Takashi Kimura
    Division of Molecular Bioscience, JCSMR John Curtin School of Medical Research, Australian National University, P O Box 334, Canberra, ACT 2601, Australia
    Biochem J 401:317-24. 2007
    ....
  31. doi request reprint In vitro modulation of the cardiac ryanodine receptor activity by Homer1
    Pierre Pouliquin
    Division of Molecular Bioscience, The John Curtin School of Medical Research, The Australian National University, P O Box 334, Canberra, ACT 2601, Australia
    Pflugers Arch 458:723-32. 2009
    ..These actions of Homer were generally similar in RyR2 and RyR1. The strong functional interactions suggest that Homer1 is likely to be an endogenous modulator of RyR channels in the heart and neurons as well as in skeletal muscle...
  32. ncbi request reprint Phosphorylation of skeletal muscle calsequestrin enhances its Ca2+ binding capacity and promotes its association with junctin
    Nicole A Beard
    John Curtin School of Medical Research, Australian National University, PO Box 334, Canberra, Australian Capital Territory 2601, Australia
    Cell Calcium 44:363-73. 2008
    ..These novel data shows that phosphorylated calsequestrin is required for high capacity calcium buffering and suggest that ryanodine receptor inhibition by calsequestrin is mediated by junctin...
  33. ncbi request reprint Structural and functional characterization of interactions between the dihydropyridine receptor II-III loop and the ryanodine receptor
    Marco G Casarotto
    Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, Canberra, Australian Capital Territory, Australia
    Clin Exp Pharmacol Physiol 33:1114-7. 2006
    ..5. Fluorescence quenching experiments have been used to identify and measure the binding affinity of the II-III loop with fragments of the RyR...
  34. pmc Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation
    Nicole A Beard
    John Curtin School of Medical Research, Australian Capital Territory, Australia
    Biophys J 88:3444-54. 2005
    ....
  35. ncbi request reprint What we don't know about the structure of ryanodine receptor calcium release channels
    Angela F Dulhunty
    The Muscle Research Group, John Curtin School of Medical Research, Australian National University, Canberra, Australian Capital Territory, Australia
    Clin Exp Pharmacol Physiol 30:713-23. 2003
    ..4. A model of the RyR pore based on the Streptomyces lividans KcsA channel structure is presented. Protein/protein interactions between the RyR and other regulatory proteins, as well as within the RyR subunit, are discussed...
  36. ncbi request reprint CLIC-2 modulates cardiac ryanodine receptor Ca2+ release channels
    Philip G Board
    Division of Molecular Bioscience, John Curtin School of Medical Research, The Australian National University, P O Box 334, Canberra, ACT 2601, Australia
    Int J Biochem Cell Biol 36:1599-612. 2004
    ..The inhibition of RyR channels was reversed by removing CLIC-2 from the solution or by adding an anti-CLIC-2 antibody. The results suggest that one function of CLIC-2 might be to limit Ca2+ release from internal stores in cells...
  37. ncbi request reprint Activating the ryanodine receptor with dihydropyridine receptor II-III loop segments: size and charge do matter
    Marco G Casarotto
    Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, ACT
    Front Biosci 9:2860-72. 2004
    ..The results suggest that the ability of the A region of the skeletal II-III loop to interact with the RyR could depend on the tertiary conformation of the II-III loop, which is thought to change during EC coupling...
  38. doi request reprint Control of muscle ryanodine receptor calcium release channels by proteins in the sarcoplasmic reticulum lumen
    Nicole A Beard
    John Curtin School of Medical Research, Australian National University, ACT, Australia
    Clin Exp Pharmacol Physiol 36:340-5. 2009
    ....
  39. doi request reprint The voltage-gated calcium-channel beta subunit: more than just an accessory
    Yamuna Karunasekara
    The John Curtin School of Medical Research, Australian National University, GPO Box 334, Canberra, ACT, 2601, Australia
    Eur Biophys J 39:75-81. 2009
    ..Such findings could have important implications with respect to EC coupling...
  40. doi request reprint Molecular recognition of the disordered dihydropyridine receptor II-III loop by a conserved spry domain of the type 1 ryanodine receptor
    Han Shen Tae
    John Curtin School of Medical Research, Australian National University, Canberra, Australian Capital Territory, Australia
    Clin Exp Pharmacol Physiol 36:346-9. 2009
    ..5. The mutant E1108A located in the negatively charged loop of SPRY2 reduces the binding affinity to the DHPR II-III loop...
  41. ncbi request reprint Agonists and antagonists of the cardiac ryanodine receptor: potential therapeutic agents?
    Angela F Dulhunty
    Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, P O Box 334, ACT, 2601, Australia
    Pharmacol Ther 113:247-63. 2007
    ..The use of regulatory binding sites within the RyR complex or on its associated proteins as templates for drug design is discussed...
  42. doi request reprint Multiple actions of the anthracycline daunorubicin on cardiac ryanodine receptors
    Amy D Hanna
    John Curtin School of Medical Research, Australian Capital Territory, Australia
    Mol Pharmacol 80:538-49. 2011
    ..We suggest that binding of daunorubicin to RyR2 and CSQ2, and oxidation of RyR2, are all likely to contribute to anthracycline-induced cardiotoxicity during chemotherapy...
  43. ncbi request reprint Structure of the Janus protein human CLIC2
    Brett A Cromer
    Biota Structural Biology Laboratory, St Vincent s Institute, Fitzroy, Victoria 3065, Australia
    J Mol Biol 374:719-31. 2007
    ..This so-called foot-in-mouth interaction suggests that CLIC2 might recognize other proteins such as the ryanodine receptor through a similar interaction...
  44. pmc Malignant hyperthermia mutation sites in the Leu2442-Pro2477 (DP4) region of RyR1 (ryanodine receptor 1) are clustered in a structurally and functionally definable area
    Mark L Bannister
    Boston Biomedical Research Institute, Watertown, MA 02472, USA
    Biochem J 401:333-9. 2007
    ..The data in the present paper indicates that mutation of residues in this region disrupts the interdomain interactions that stabilize the closed state of the channel...
  45. ncbi request reprint The cysteine-rich secretory protein domain of Tpx-1 is related to ion channel toxins and regulates ryanodine receptor Ca2+ signaling
    Gerard M Gibbs
    Monash Institute of Medical Research, Monash University, Clayton, Melbourne, Victoria, Australia
    J Biol Chem 281:4156-63. 2006
    ..These data show that the Tpx-1 Crisp domain on its own can regulate ion channel activity and provide compelling evidence for a role for Tpx-1 in the regulation of Ca(2+) fluxes observed during sperm capacitation...
  46. ncbi request reprint 1H, 13C and 15N assignments for the II-III loop region of the skeletal dyhydropyridine receptor
    Yanfang Cui
    J Biomol NMR 32:89-90. 2005
  47. pmc Regulation of skeletal ryanodine receptors by dihydropyridine receptor II-III loop C-region peptides: relief of Mg2+ inhibition
    Claudia S Haarmann
    School of Biomedical Sciences, Faculty of Health, University of Newcastle, NSW 2308, Australia
    Biochem J 387:429-36. 2005
    ..The relief of Mg2+ inhibition was particularly important since RyR activation during excitation-contraction coupling depends on a similar decrease in Mg2+ inhibition...
  48. pmc Triadin binding to the C-terminal luminal loop of the ryanodine receptor is important for skeletal muscle excitation contraction coupling
    Sanjeewa A Goonasekera
    Department of Pharmacology and Physiology, University of Rochester, Rochester, NY 14642, USA
    J Gen Physiol 130:365-78. 2007
    ..These findings demonstrate that junctin and triadin bind to different sites on RyR1 and that triadin plays an important role in ensuring rapid Ca(2+) release during excitation-contraction coupling in skeletal muscle...