Measurements of Calcium in Chromaffin Cell Organelles Using Targeted Aequorins.


Journal

Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969

Informations de publication

Date de publication:
2023
Historique:
entrez: 7 10 2022
pubmed: 8 10 2022
medline: 12 10 2022
Statut: ppublish

Résumé

The molecular mechanisms that mediate and regulate calcium (Ca

Identifiants

pubmed: 36205893
doi: 10.1007/978-1-0716-2671-9_11
doi:

Substances chimiques

Aequorin 50934-79-7
Calcium SY7Q814VUP

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

153-177

Informations de copyright

© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Références

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doi: 10.1074/jbc.270.46.27510
Zhao Y, Araki S, Wu J et al (2011) An expanded palette of genetically encoded Ca2+ indicators. Science 333:1888–1891
doi: 10.1126/science.1208592
Suzuki J, Kanemaru K, Iino M (2016) Genetically encoded fluorescent indicators for organellar calcium imaging. Biophys J 111:1119–1131
doi: 10.1016/j.bpj.2016.04.054
Simpson USA, Brini AWM, Pozzan M et al (1995) Transfected aequorin in the measurement of cytosolic Ca 2 + concentration ([Ca 2 +]c). J Biol Chem 270:9896–9903
doi: 10.1074/jbc.270.17.9896
García AG, García-De-Diego AM, Gandía L et al (2006) Calcium signaling and exocytosis in adrenal chromaffin cells. Physiol Rev 86:1093–1131
doi: 10.1152/physrev.00039.2005
Montero M, Alonso MT, Carnicero E et al (2000) Chromaffin-cell stimulation triggers fast millimolar mitochondrial Ca2+ transients that modulate secretion. Nat Cell Biol 2:57–61
doi: 10.1038/35000001
Rigual R, Montero M, Rico AJ et al (2002) Modulation of secretion by the endoplasmic reticulum in mouse chromaffin cells. Eur J Neurosci 16:1690–1696
doi: 10.1046/j.1460-9568.11-2.02244.x
Alonso MT, Barrero MJ, Carnicero E et al (1999) Functional measurements of Ca2+ in the endoplasmic reticulum using a herpes virus to deliver targeted aequorin. Cell Calcium 24:87–96
doi: 10.1016/S0143-4160(98)90076-8
Alonso MT, Barrero MJ, Michelena P et al (1999) Ca2+-induced Ca2+ release in chromaffin cells seen from inside the ER with targeted aequorin. J Cell Biol 144:241–254
doi: 10.1083/jcb.144.2.241
Santo-Domingo J, Fonteriz RI, Lobatón CD et al (2010) Ca2+ dynamics in the secretory vesicles of neurosecretory PC12 and INS1 cells. Cell Mol Neurobiol 30:1197–1199
Santo-Domingo J, Vay L, Camacho M et al (2008) Calcium dynamics in bovine adrenal medulla chromaffin cell secretory granules. Eur J Neurosci 28:1265–1274
doi: 10.1111/j.1460-9568.2008.06440.x
Inouye S, Noguchi M, Sakaki Y et al (1985) Cloning and sequence analysis of cDNA for the luminescent protein aequorin. Proc Natl Acad Sci USA 82:3154–3158
doi: 10.1073/pnas.82.10.3154
Cobbold PH, Lee JAC (1991) Aequorin measurements of cytoplasmic free calcium. In: Cellular calcium: a práctical approach. Oxford Press
Li X, Drakulich DA, Zhang P et al (2002) Transduction of bovine adrenal chromaffin cells using a recombinant adenovirus expressing GFP. J Neurosci Methods 122:91–96
doi: 10.1016/S0165-0270(02)00295-9
Moro M, López M, Gandía L et al (1990) Separation and culture of living adrenaline- and noradrenaline-containing cells from bovine adrenal medullae. Anal Biochem 185:234–238
doi: 10.1016/0003-2697(90)90287-J
Montero M, Brini M, Marsault R et al (1995) Monitoring dynamic changes in free Ca2+ concentration in the endoplasmic reticulum of intact cells. EMBO J 14:5467–5475
doi: 10.1002/j.1460-2075.1995.tb00233.x
De la Fuente S, Fonteriz RI, Montero M et al (2013) Ca2+ homeostasis in the endoplasmic reticulum measured with a new low-Ca2+−affinity targeted aequorin. Cell Calcium 54:37–45
doi: 10.1016/j.ceca.2013.04.001
De la Fuente S, Fonteriz RI, de La Cruz PJ et al (2012) Mitochondrial free [Ca2+] dynamics measured with a novel low-Ca2+ − affinity aequorin probe. Biochem J 445:371–376
doi: 10.1042/BJ20120423
Allen DG, Blinks JR, Prendergast FG (1977) Aequorin luminescence: relation of light emission to calcium concentration-a calcium-independent component. Science 195:996–998
doi: 10.1126/science.841325

Auteurs

Jaime Santo-Domingo (J)

Departamento de Bioquímica y Biología Molecular y Fisiología, Facultad de Medicina, Unidad de Excelencia Instituto de Biología y Genética Molecular (IBGM), Universidad de Valladolid and CSIC, Valladolid, Spain. jaime.santo-domingo@uva.es.

Pilar Álvarez-Illera (P)

Departamento de Bioquímica y Biología Molecular y Fisiología, Facultad de Medicina, Unidad de Excelencia Instituto de Biología y Genética Molecular (IBGM), Universidad de Valladolid and CSIC, Valladolid, Spain.

Pablo Montenegro (P)

Pharmacology Unit, Department of Physical Medicine and Pharmacology, Medical School, Universidad de La Laguna, Tenerife, Spain.

Rosalba I Fonteriz (RI)

Departamento de Bioquímica y Biología Molecular y Fisiología, Facultad de Medicina, Unidad de Excelencia Instituto de Biología y Genética Molecular (IBGM), Universidad de Valladolid and CSIC, Valladolid, Spain.

Mayte Montero (M)

Departamento de Bioquímica y Biología Molecular y Fisiología, Facultad de Medicina, Unidad de Excelencia Instituto de Biología y Genética Molecular (IBGM), Universidad de Valladolid and CSIC, Valladolid, Spain.

Javier Álvarez (J)

Departamento de Bioquímica y Biología Molecular y Fisiología, Facultad de Medicina, Unidad de Excelencia Instituto de Biología y Genética Molecular (IBGM), Universidad de Valladolid and CSIC, Valladolid, Spain.

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