Effects of Monovalent and Divalent Cations on Ca<sup>2+</sup> Fluxes Across Chromaffin Secretory Membrane Vesicles

Krieger-Brauer, Heidemarie I.; Gratzl, Manfred

doi:10.1111/j.1471-4159.1983.tb00821.x

Cited by 34 publications

(14 citation statements)

References 19 publications

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“…In addition to the examples of adenylate cyclase and acetylcholinesterase discussed above, the a-bungarotoxin-binding part of the acetylcholine receptor (29) and sodium-calcium exchange activity have also been observed in chromaffin secretory vesicles (13,22,30). The finding on the absence of Na+-K+-ATPase activity in the chromaffin vesicle fractions (Fig.…”

Section: Fractionmentioning

confidence: 68%

Distribution of chromaffin secretory vesicles, acetylcholinesterase, and lysosomal enzymes in sucrose and percoll gradients

Gratzl

1984

Analytical Biochemistry

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emde chromaffin secretory vesicles, obtained by differential centrifugation, were further purified on isotonic (PereolI) gradients. The chromaffin vesicIe fractions recovered from the gradients contain acetylcholinesterase as well as lysosomal enzymes. With the aid of a subsequent sucrose gradient lysosomal enzymes could be removed from chromaffin vesicIe fractions. but not acetylcholinesterase. This suggests that lysosomal enzymes do not pass through the chromaffin vesicIes during the biogenesis of lysosomes but acetylcholinesterase does.

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Section: Fractionmentioning

confidence: 68%

Distribution of chromaffin secretory vesicles, acetylcholinesterase, and lysosomal enzymes in sucrose and percoll gradients

Gratzl

1984

Analytical Biochemistry

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“…Regarding alternative Ca 2+ transport systems in the granules, the presence of either Ca 2+ -ATPases, Na + /Ca 2+ or H + /Ca 2+ exchange systems have been proposed in different preparations [14][15][16][17][18]. Inhibition of sarcoendoplasmic reticulum Ca 2+ -ATPase with 10 M benzohydroquinone produced little effects on [Ca 2+ ] SG (data not shown), suggesting that this type of Ca 2+ -ATPase was not involved.…”

Section: Dynamic Measurements Of [Ca 2+ ] In the Secretory Vesiclesmentioning

confidence: 93%

Calcium dynamics in catecholamine-containing secretory vesicles

et al. 2005

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“…In mammalian cells, Ca 2ϩ uptake is mediated by either sarco/ endoplasmic reticulum Ca 2ϩ -ATPases (SERCAs) or secretory pathway Ca 2ϩ -ATPases, located in the Golgi complex and secretory granules (17,18). In addition, acidic organelles have a large concentration gradient of protons that has been reported to be necessary to maintain Ca 2ϩ accumulated (19,20), probably by supporting a Ca 2ϩ /H ϩ exchange mechanism mediated by the cooperative activity of Na ϩ /H ϩ and Na ϩ /Ca 2ϩ exchangers (21)(22). The proton gradient in acidic organelles is maintained by a vacuolar proton-ATPase (V-ATPase) that drives acidification (23)(24).…”

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confidence: 99%

STIM1 and STIM2 Are Located in the Acidic Ca2+ Stores and Associates with Orai1 upon Depletion of the Acidic Stores in Human Platelets

Zbidi

Jardín

Woodard

et al. 2011

Journal of Biological Chemistry

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Mammalian cells accumulate Ca2؉ into agonist-sensitive acidic organelles, vesicles that possess a vacuolar protonATPase. Acidic Ca 2؉ stores include secretory granules and lysosome-related organelles. Current evidence clearly indicates that acidic Ca 2؉ stores participate in cell signaling and function, including the activation of store-operated Ca 2؉ entry in human platelets upon depletion of the acidic stores, although the mechanism underlying the activation of store-operated Ca 2؉ entry controlled by the acidic stores remains unclear. STIM1 has been presented as the endoplasmic reticulum Ca 2؉ sensor, but its role sensing intraluminal Ca 2؉ concentration in the acidic stores has not been investigated. Here we report that STIM1 and STIM2 are expressed in the lysosome-related organelles and dense granules in human platelets isolated by immunomagnetic sorting. Depletion of the acidic Ca 2؉ stores using the specific vacuolar proton-ATPase inhibitor, bafilomycin A1, enhanced the association between STIM1 and STIM2 as well as between these proteins and the plasma membrane channel Orai1. Depletion of the acidic Ca 2؉ stores also induces time-dependent co-immunoprecipitation of STIM1 with the TRPC proteins hTRPC1 and hTRPC6, as well as between Orai1 and both TRPC proteins. In addition, bafilomycin A1 enhanced the association between STIM2 and SERCA3. These findings demonstrate the location of STIM1 and STIM2 in the acidic Ca 2؉ stores and their association with Ca 2؉ channels and ATPases upon acidic stores discharge.Store-operated calcium entry (SOCE), 4 a Ca 2ϩ influx mechanism regulated by the filling state of the intracellular Ca 2ϩ stores, is a major mechanism for Ca 2ϩ influx in non-excitable cells (1). It has long been known that Ca 2ϩ is stored in the endoplasmic reticulum (ER), which is the best-studied agonistreleasable Ca 2ϩ store; however, a number of studies have revealed that Ca 2ϩ is also dynamically accumulated in a number of acidic organelles (2), including secretory granules, lysosomes and lysosome-related organelles, endosomes, and vesicles of the Golgi complex (2-6). ER Ca 2ϩ store depletion has been reported to be sensed by STIM1 (stromal interaction molecule-1) (7-9). Although STIM1 was originally identified as a surface membrane protein in stromal cells (10) 4 The abbreviations used are: SOCE, store-operated calcium entry; ER, endoplasmic reticulum; HBS, HEPES-buffered saline; hTRPC1 and hTRPC6, human canonical TRP1 and TRP6, respectively; IP 3 , inositol 1,4,5-trisphosphate; TBHQ, 2,5-di-(tert-butyl)-1,4-hydroquinone; TG, thapsigargin; SERCA, sarco/endoplasmic reticulum Ca 2ϩ -ATPase; V-ATPase, vacuolar proton-ATPase; NAADP, nicotinic acid adenine dinucleotide phosphate; DTS, dense tubular system; AM, acetoxymethyl ester; BAPTA-AM, 1,2-bis(2-aminophenoxy)ethane-N,N,NЈ,NЈ-tetraacetic acid tetrakis(acetoxymethyl ester); GPN, glycyl-1-phenylalanine 2-naphthylamide; PDI, protein-disulfide isomerase.

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Effects of Monovalent and Divalent Cations on Ca²⁺ Fluxes Across Chromaffin Secretory Membrane Vesicles

Abstract: Bovine chromaffin secretory vesicle ghosts loaded with Na+ were found to take up Ca2+ when incubated in K + media or in sucrose media containing micromolar concentrations of free Ca2+. Li+-or choline+-loaded ghosts did not take up Ca2+.

Cited by 34 publications

References 19 publications

Distribution of chromaffin secretory vesicles, acetylcholinesterase, and lysosomal enzymes in sucrose and percoll gradients

Distribution of chromaffin secretory vesicles, acetylcholinesterase, and lysosomal enzymes in sucrose and percoll gradients

Calcium dynamics in catecholamine-containing secretory vesicles

STIM1 and STIM2 Are Located in the Acidic Ca2+ Stores and Associates with Orai1 upon Depletion of the Acidic Stores in Human Platelets

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Effects of Monovalent and Divalent Cations on Ca2+ Fluxes Across Chromaffin Secretory Membrane Vesicles

Abstract: Bovine chromaffin secretory vesicle ghosts loaded with Na+ were found to take up Ca2+ when incubated in K + media or in sucrose media containing micromolar concentrations of free Ca2+. Li+-or choline+-loaded ghosts did not take up Ca2+.

Cited by 34 publications

References 19 publications

Distribution of chromaffin secretory vesicles, acetylcholinesterase, and lysosomal enzymes in sucrose and percoll gradients

Distribution of chromaffin secretory vesicles, acetylcholinesterase, and lysosomal enzymes in sucrose and percoll gradients

Calcium dynamics in catecholamine-containing secretory vesicles

STIM1 and STIM2 Are Located in the Acidic Ca2+ Stores and Associates with Orai1 upon Depletion of the Acidic Stores in Human Platelets

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Effects of Monovalent and Divalent Cations on Ca²⁺ Fluxes Across Chromaffin Secretory Membrane Vesicles