The chromogranin A
chromogranin A
heart
intracellular signalling
neuropilin-1
nitric oxide
Journal
Acta physiologica (Oxford, England)
ISSN: 1748-1716
Titre abrégé: Acta Physiol (Oxf)
Pays: England
ID NLM: 101262545
Informations de publication
Date de publication:
04 2021
04 2021
Historique:
revised:
13
10
2020
received:
08
06
2020
accepted:
14
10
2020
pubmed:
20
10
2020
medline:
19
8
2021
entrez:
19
10
2020
Statut:
ppublish
Résumé
Chromogranin A (CgA), a 439-residue long protein, is an important cardiovascular regulator and a precursor of various bioactive fragments. Under stressful/pathological conditions, CgA cleavage generates the CgA Haemodynamic assessment was performed on an ex vivo Langendorff rat heart model, while mechanistic studies were performed using perfused hearts, H9c2 cardiomyocytes and in silico. On the ex vivo heart, CgA These results suggest that CgA
Substances chimiques
Chromogranin A
0
Peptide Fragments
0
Neuropilin-1
144713-63-3
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e13570Commentaires et corrections
Type : CommentIn
Informations de copyright
© 2020 Scandinavian Physiological Society. Published by John Wiley & Sons Ltd.
Références
Troger J, Theurl M, Kirchmair R, et al. Granin-derived peptides. Prog Neurogibol. 2017;154:37-61.
Helle KB, Corti A, Metz-Boutigue MH, Tota B. The endocrine role for chromogranin A: a prohormone for peptides with regulatory properties. Cell Mol Life Sci. 2007;64:2863-2886.
Pasqua T, Corti A, Gentile S, et al. Full-length human chromogranin-A cardioactivity: myocardial, coronary, and stimulus-induced processing evidence in normotensive and hypertensive male rat hearts. Endocrinology. 2013;154(9):3353-3365.
Ceconi C, Ferrari R, Bachetti T, et al. Chromogranin A in heart failure; a novel neurohumoral factor and a predictor for mortality. Eur Heart J. 2002;23(12):967-974.
Tota B, Angelone T, Cerra MC. The surging role of Chromogranin A in cardiovascular homeostasis. Front Chem. 2014;14:2-64.
Modlin IM, Gustafsson BI, Moss SF, Pavel M, Tsolakis AV, Kidd M. Chromogranin A-biological function and clinical utility in neuro endocrine tumor disease. Ann Surg Oncol. 2010;17(9):2427-2443.
Campana D, Nori F, Piscitelli L, et al. Chromogranin A: is it a useful marker of neuroendocrine tumors? J Clin Oncol. 2007;25(15):1967-1973.
Baudin E, Bidart JM, Bachelot A, et al. Impact of chromogranin A measurement in the work-up of neuroendocrine tumors. Ann Oncol. 2001;12(Suppl 2):S79-S82.
Di Giacinto P, Rota F, Rizza L, et al. From laboratory to clinical aspects of patients with neuroendocrine tumors. Int J Endocrinol. 2018;2:8126087.
Mahata SK, Corti A. Chromogranin A and its fragments in cardiovascular, immunometabolic, and cancer regulation. Ann NY Acad Sci. 2019;1455(1):34-58.
Pasqua T, Angelone T, Spena A, Cerra MC. Biological roles of the eclectic chromogranin-A-derived peptide catestatin. Curr Med Chem. 2017;24(31):3356-3372.
Metz-Boutigue MH, Garcia-Sablone P, Hogue-Angeletti R, Aunis D. Intracellular and extracellular processing of chromogranin A. Determination of cleavage sites. Eur J Biochem. 1993;217(1):247-257.
Crippa L, Bianco M, Colombo B, et al. A new chromogranin A-dependent angiogenic switch activated by thrombin. Blood. 2013;121(2):392-402.
Pieroni M, Corti A, Tota B, et al. Myocardial production of chromogranin A in human heart: a new regulatory peptide of cardiac function. Eur Heart J. 2007;28(9):1117-1127.
Pasqua T, Tota B, Penna C, et al. pGlu-serpinin protects the normotensive and hypertensive heart from ischemic injury. J Endocrinol. 2015;227(3):167-178.
Filice E, Pasqua T, Quintieri AM, et al. Chromofungin, CgA47-66-derived peptide, produces basal cardiac effects and postconditioning cardioprotective action during ischemia/reperfusion injury. Peptides. 2015;71:40-48.
Angelone T, Quintieri AM, Pasqua T, et al. Phosphodiesterase type-2 and NO-dependent S-nitrosylation mediate the cardioinhibition of the antihypertensive catestatin. Am J Physiol Heart Circ Physiol. 2012;302(2):H431-H442.
Bianco M, Gasparri AM, Colombo B, et al. Chromogranin A Is preferentially cleaved into proangiogenic peptides in the bone marrow of multiple myeloma patients. Cancer Res. 2016;76(7):1781-1791.
Curnis F, Dallatomasina A, Bianco M, et al. Regulation of tumor growth by circulating full-length chromogranin A. Oncotarget. 2016;7:72716-72732.
Giri S, Jennings LK. The spectrum of thrombin in acute coronary syndromes. Thromb Res. 2015;135(5):782-787.
Dallatomasina A, Gasparri AM, Colombo B, et al. Spatiotemporal regulation of tumor angiogenesis by circulating chromogranin A cleavage and neuropilin-1 engagement. Cancer Res. 2019;79(8):1925-1937.
Wang Y, Cao Y, Yamada S, et al. Cardiomyopathy and worsened ischemic heart failure in SM22-α cre-mediated neuropilin-1 null mice: dysregulation of PGC1α and mitochondrial homeostasis. Arterioscler Thromb Vasc Biol. 2015;35(6):1401-1412.
Kawasaki T, Kitsukawa T, Bekku Y, et al. A requirement for neuropilin-1 in embryonic vessel formation. Development. 1999;126(21):4895-4902.
Angelone T, Quintieri AM, Brar BK, et al. The antihypertensive chromogranin A peptide catestatin acts as a novel endocrine/paracrine modulator of cardiac inotropism and lusitropism. Endocrinology. 2008;149(10):4780-4793.
Nissen JC, Selwood DL, Tsirka SE. Tuftsin signals through its receptor neuropilin-1 via the transforming growth factor beta pathway. J Neurochem. 2013;127(3):394-402.
Jarvis A, Allerston CK, Jia H, et al. Small molecule inhibitors of the neuropilin-1 vascular endothelial growth factor A (VEGF-A) interaction. J Med Chem. 2010;53(5):2215-2226.
Vander Kooi CW, Jusino MA, Perman B, Neau DB, Bellamy HD, Leahy DJ. Structural basis for ligand and heparin binding to neuropilin B domains. Proc Natl Acad Sci USA. 2007;104(15):6152-6157.
Preece NE, Nguyen M, Mahata M, et al. Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A. Regul Pept. 2004;118(1-2):75-87.
Santofimia-Castaño P, Rizzuti B, Abián O, Velázquez-Campoy A, Iovanna JL, Neira JL. Amphipathic helical peptides hamper protein-protein interactions of the intrinsically disordered chromatin nuclear protein 1 (NUPR1). Biochim Biophys Acta Gen Subj. 2018;1862(6):1283-1295.
Pantoja-Uceda D, Neira JL, Contreras LM, Manton CA, Welch DR, Rizzuti B. The isolated C-terminal nuclear localization sequence of the breast cancer metastasis suppressor 1 is disordered. Arch Biochem Biophys. 2019;664:95-101.
Lappano R, Mallet C, Rizzuti B, et al. The peptide ERα17p is a GPER inverse agonist that exerts antiproliferative effects in breast cancer cells. Cells. 2019;8(6):590.
Sun J, Murphy E. Protein S-nitrosylation and cardioprotection. Circ Res. 2010;106(2):285-296.
Vaingankar SM, Li Y, Biswas N, et al. Effects of chromogranin A deficiency and excess in vivo: biphasic blood pressure and catecholamine responses. J Hypertens. 2010;28(4):817-825.
Mahapatra NR, O'Connor DT, Vaingankar SM, et al. Hypertension from targeted ablation of chromogranin A can be rescued by the human ortholog. J Clin Invest. 2005;115(7):1942-1952.
Takiyyuddin MA, Parmer RJ, Kailasam MT, et al. Chromogranin A in human hypertension. Influence of heredity. Hypertension. 1995;26:213-220.
O'Connor DT, Kailasam MT, Kennedy BP, Ziegler MG, Yanaihara N, Parmer RJ. Early decline in the catecholamine release-inhibitory peptide catestatin in humans at genetic risk of hypertension. J Hypertens. 2002;20(7):1335-1345.
Mahata SK, Kiranmayi M, Mahapatra NR. Catestatin: a master regulator of cardiovascular functions. Curr Med Chem. 2018;25(11):1352-1374.
Goldhaber JI, Hamilton MA. Role of inotropic agents in the treatment of heart failure. Circulation. 2010;121(14):1655-1660.
Kennedy RH, Owings R, Shekhawat N, Joseph J. Acute negative inotropic effects of homocysteine are mediated via the endothelium. Am J Physiol Heart Circ Physiol. 2004;287(2):H812-H817.
Brutsaert DL. Cardiac endothelial-myocardial signaling: its role in cardiac growth, contractile performance, and rhythmicity. Physiol Rev. 2003;83(1):59-115.
Brunner F, Brás-Silva C, Cerdeira AS, Leite-Moreira AF. Cardiovascular endothelins: essential regulators of cardiovascular homeostasis. Pharmacol Ther. 2006;111(2):508-531.
Takashima S, Kitakaze M, Asakura M, et al. Targeting of both mouse neuropilin-1 and neuropilin-2 genes severely impairs developmental yolk sac and embryonic angiogenesis. Proc Natl Acad Sci USA. 2002;99(6):3657-3662.
Staton CA, Kumar I, Reed MW, Brown NJ. Neuropilins in physiological and pathological angiogenesis. J Pathol. 2007;212(3):237-248.
Teesalu T, Sugahara KN, Kotamraju VR, Ruoslahti E. C-end rule peptides mediate neuropilin-1-dependent cell, vascular, and tissue penetration. Proc Natl Acad Sci USA. 2009;106(38):16157-16162.
Teesalu T, Sugahara KN, Ruoslahti E. Tumor-penetrating peptides. Front Oncol. 2013;27:3-216.
Haspel N, Zanuy D, Nussinov R, Teesalu T, Ruoslahti E, Aleman C. Binding of a C-end rule peptide to neuropilin-1 receptor: a molecular modeling approach. Biochemistry. 2011;50(10):1755-1762.
Omar SA, Webb AJ, Lundberg JO, Weitzberg E. Therapeutic effects of inorganic nitrate and nitrite in cardiovascular and metabolic diseases. J Intern Med. 2016;279(4):315-336.
Abi-Gerges N, Fischmeister R, Mery PF. G protein-mediated inhibitory effect of nitric oxide on L-type Ca2+ current in rat ventricular myocytes. J Physiol. 2001;531(Pt 1):117-130.
Stojanovic MO, Ziolo MT, Wahler GM, Wolska BM. Anti-adrenergic effects of nitric oxide donor SIN-1 in rat cardiac myocytes. Am J Physiol Cell Physiol. 2001;281(1):C342-C349.
Leite-Moreira AF. Current perspectives in diastolic dysfunction and diastolic heart failure. Heart. 2006;92(5):712-718.
Kawamura H, Li X, Goishi K, et al. Neuropilin-1 in regulation of VEGF-induced activation of p38MAPK and endothelial cell organization. Blood. 2008;112(9):3638-3649.
Plein A, Fantin A, Ruhrberg C. Neuropilin regulation of angiogenesis, arteriogenesis, and vascular permeability. Microcirculation. 2014;21(4):315-323.
Farah C, Michel LYM, Balligand JL. Nitric oxide signalling in cardiovascular health and disease. Nat Rev Cardiol. 2018;15(5):292-316.
Murphy E, Kohr M, Menazza S, et al. Signaling by S-nitrosylation in the heart. J Mol Cell Cardiol. 2014;73:18-25.
Angelone T, Quintieri AM, Pasqua T, et al. The NO stimulator, Catestatin, improves the Frank-Starling response in normotensive and hypertensive rat hearts. Nitric Oxide. 2015;50:10-19.
Penna C, Angotti C, Pagliaro P. Protein S-nitrosylation in preconditioning and postconditioning. Exp Biol Med. 2014;239(6):647-662.
Whalen EJ, Foster MW, Matsumoto A, et al. Regulation of beta-adrenergic receptor signaling by S-Nitrosylation of G-protein-coupled receptor kinase 2. Cell. 2007;129(3):511-522.
Martínez-Ruiz A, Villanueva L, González de Orduña C, et al. S-Nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc Natl Acad Sci USA. 2005;102(24):8525-8530.
Choi BM, Pae HO, Jang SI, Kim YM, Chung HT. Nitric oxide as a proapoptotic as well as anti-apoptotic modulator. J Biochem Mol Biol. 2002;35(1):116-126.
Gonzalez DR, Treuer A, Sun QA, Stamler JS, Hare JM. S-Nitrosylation of cardiac ion channels. J Cardiovasc Pharmacol. 2009;54(3):188-195.
Wang L, Mukhopadhyay D, Xu X. C terminus of RGS-GAIP-interacting protein conveys neuropilin-1-mediated signaling during angiogenesis. FASEB J. 2006;20(9):1513-1515.
De Vries L, Elenko E, Hubler L, Jones TL, Farquhar MG. GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits. Proc Natl Acad Sci USA. 1996;93(26):15203-15208.
Lähteenvuo JE, Lähteenvuo MT, Kivelä A, et al. Vascular endothelial growth factor-B induces myocardium-specific angiogenesis and arteriogenesis via vascular endothelial growth factor receptor-1- and neuropilin receptor-1-dependent mechanisms. Circulation. 2009;119(6):845-856.
Hu LA, Chen W, Martin NP, Whalen EJ, Premont RT, Lefkowitz RJ. GIPC interacts with the beta1-adrenergic receptor and regulates beta1-adrenergic receptor-mediated ERK activation. J Biol Chem. 2003;278(28):26295-26301.
Jeanneteau F, Diaz J, Sokoloff P, Griffon N. Interactions of GIPC with dopamine D2, D3 but not D4 receptors define a novel mode of regulation of G protein-coupled receptors. Mol Biol Cell. 2004;15(2):696-705.
Mahata SK, O'Connor DT, Mahata M, et al. Novel autocrine feedback control of catecholamine release. A discrete Chromogranin A fragment is a non competitive nicotinic cholinergic antagonist. J Clin Invest. 1997;100(6):1623-1633.
Soker S, Takashima S, Miao HQ, Neufeld G, Klagsbrun M. Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor. Cell. 1998;92(6):735-745.
Seddon M, Shah AM, Casadei B. Cardiomyocytes as effectors of nitric oxide signalling. Cardiovasc Res. 2007;75(2):315-326.
Niu G, Chen X. Vascular endothelial growth factor as an anti-angiogenic target for cancer therapy. Curr Drug Targets. 2010;11(8):1000-1017.
Kazazi-Hyseni F, Beijnen JH, Schellens JH. Bevacizumab. Oncologist. 2010;15(8):819-825.
Zentilin L, Puligadda U, Lionetti V, et al. Cardiomyocyte VEGFR-1 activation by VEGF-B induces compensatory hypertrophy and preserves cardiac function after myocardial infarction. FASEB J. 2010;24(5):1467-1478.
Lymperopoulos A, Rengo G, Koch WJ. The adrenergic nervous system in heart failure: pathophysiology and therapy. Circ Res. 2013;113(6):739-753.
Sergeeva IA, Christoffels VM. Regulation of expression of atrial and brain natriuretic peptide, biomarkers for heart development and disease. Biochim Biophys Acta. 2013;1832(12):2403-2413.
Rocca C, Scavello F, Granieri MC, et al. Phoenixin-14: detection and novel physiological implications in cardiac modulation and cardioprotection. Cell Mol Life Sci. 2018;75(4):743-756.
Quintieri AM, Filice E, Amelio D, et al. The innovative "Bio-Oil Spread" prevents metabolic disorders and mediates preconditioning-like cardioprotection in rats. Nutr Metab Cardiovasc Dis. 2016;26(7):603-613.
Rocca C, Boukhzar L, Granieri MC, et al. A selenoprotein T-derived peptide protects the heart against ischaemia/reperfusion injury through inhibition of apoptosis and oxidative stress. Acta Physiol. 2018;223(4):e13067.
Rocca C, Scavello F, Colombo B, et al. Physiological levels of chromogranin A prevent doxorubicin-induced cardiotoxicity without impairing its anticancer activity. FASEB J. 2019;33(6):7734-7747.
Hassanabad ZF, Furman BL, Parratt JR, Aughey E. Coronary endothelial dysfunction increases the severity of ischaemia-induced ventricular arrhythmias in rat isolated perfused hearts. Basic Res Cardiol. 1998;93(4):241-249.
Casacchia T, Scavello F, Rocca C, et al. Leopoldia comosa prevents metabolic disorders in rats with high-fat diet-induced obesity. Eur J Nutr. 2019;58(3):965-979.
Rocca C, Femminò S, Aquila G, et al. Notch1 Mediates Preconditioning Protection Induced by GPER in Normotensive and Hypertensive Female Rat Hearts. Front Physiol. 2018;15:9-521.
Chen YU, Ivo A. Hampton TG, et al. Vascular endothelial growth factor promotes cardiomyocyte differentiation of embryonic stem cells. Am J Physiol Heart Circ Physiol. 2006;291(4):H1653-H1658.
Wu G, Mannam AP, Jiaping WU, et al. Hypoxia induces myocyte-dependent COX-2 regulation in endothelial cells: role of VEGF. Am J Physiol Heart Circ Physiol. 2003;285:H2420-H2429.
Emlet DR, Brown KA, Kociban DL, et al. Response to trastuzumab, erlotinib, and bevacizumab, alone and in combination, is correlated with the level of human epidermal growth factor receptor-2 expression in human breast cancer cell lines. Mol Cancer Ther. 2007;6(10):2664-2674.
Tse MMY, Aboutabl ME, Althurwi HN, Elshenawy OH, Abdelhamid G, El-Kadi AOS. Cytochrome P450 epoxygenase metabolite, 14,15-EET, protects against isoproterenol-induced cellular hypertrophy in H9c2 rat cell line. Vascul Pharmacol. 2013;58(5-6):363-373.
Humphrey W, Dalke A, Schulten K. VMD: visual molecular dynamics. J Mol Graphics. 1996;14(1):33-38.
Trott O, Olson AJ. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem. 2010;31(2):455-461.
Grande F, Rizzuti B, Occhiuzzi MA, et al. Identification by molecular docking of homoisoflavones from Leopoldia comosa as ligands of estrogen receptors. Molecules. 2018;23:E894.
Abraham MJ, Murtola T, Schulz R, et al. GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers. SoftwareX. 2015;1-2:19-25.
Lindorff-Larsen K, Piana S, Palmo K, et al. Improved side-chain torsion potentials for the Amber ff99SB protein force field. Proteins. 2010;78(8):1950-1958.
Evoli S, Guzzi R, Rizzuti B. Molecular simulations of ß-lactoglobulin complexed with fatty acids reveal the structural basis of ligand affinity to internal and possible external binding sites. Proteins Struct Funct Bioinformat. 2014;82:2609-2619.
Neira JL, Rizzuti B, Iovanna JL. Determinants of the pKa values of ionizable residues in an intrinsically disordered protein. Arch Biochem Biophys. 2016;598:18-27.