Inositol Trisphosphate and Cyclic ADP-Ribose–Mediated Release of Ca2+ from Single Isolated Pancreatic Zymogen Granules

Gerasimenko, Oleg Vsevolodovich; Gerasimenko, Julia Vladimirovna; Belan, Pavel; Petersen, O. H.

doi:10.1016/s0092-8674(00)81292-1

Cited by 237 publications

(237 citation statements)

References 37 publications

(2 reference statements)

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“…Of these possibilities, option (i) may be the most reasonable, given the known limited diffusional characteristics of Ca# + [25] and the ability to detect persistent gradients of Ca# + using aequorin targeted to the inner surface of the plasma membrane with a SNAP25-aequorin fusion protein [2]. Consistent with this view, data in acinar cells pointing to the presence of IP $ and cyclic ADP-ribose receptors on dense-core granules [4] have recently been questioned in studies using highly purified granule preparations [26]. Similarly, immunocytochemical evidence that implicated the presence of IP $ receptors on the dense-core granule membrane of insulin-secreting RINm5F cells [27] has been seriously criticized [28].…”

Section: Role Of Granule Ca 2 + Mobilization In Secretionmentioning

confidence: 82%

“…For example, in acinar cells, Ca# + may be mobilized from the granule itself by the second messengers inositol 1,4,5-trisphosphate (IP $ ) or cyclic ADP-ribose [4]. Given the slow diffusion characteristics of Ca# + in the cell cytosol [5], it may be predicted that release of Ca# + from granule stores may produce a domain of high Ca# + around each granule.…”

Section: Introductionmentioning

confidence: 99%

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A phogrin–aequorin chimaera to image free Ca2+ in the vicinity of secretory granules

Pouli

Karagenc

Wasmeier

et al. 1998

Biochemical Journal

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Microdomains of high Ca2+ concentration ([Ca2+]) may be critical to the control of intracellular processes such as secretion and metabolism without compromising other cell functions. To explore changes in [Ca2+] in the outer mantle (< 30 nm deep) that surrounds the surface of dense-core secretory granules, we have designed a recombinant chimaera between the granule protein phogrin and aequorin. When expressed in populations of insulin-secreting MIN6 or phaeochromocytoma PC12 cells, the chimaera was targeted to secretory granules as expected. The recombinant protein reported a similar [Ca2+] at the granule surface to that in the bulk cytosol, measured with untargeted aequorin. This was the case both at rest ([Ca2+] = 80-120 nM) and after stimulation with agents that provoke Ca2+ entry or Ca2+ mobilization from intracellular pools, and during activated secretion. Thus depolarization of MIN6 cell populations with high K+ increased [Ca2+] both in the bulk cytosol and close to the granules to approx. 4 μM, with near-identical kinetics of increase and recovery. Similarly, stimulation of PC12 cells with ATP provoked an increase in [Ca2+] in either domain to 1.3 μM. These data argue that, in MIN6 and PC12 neuroendocrine cells (i) significant mobilization of Ca2+ from most secretory granules probably does not occur during activated Ca2+ influx or mobilization of internal Ca2+ stores, and (ii) agonist-stimulated Ca2+-dependent secretion can occur without development of a large gradient of [Ca2+] between the surface of most secretory vesicles and the rest of the cytosol.

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Section: Role Of Granule Ca 2 + Mobilization In Secretionmentioning

confidence: 82%

Section: Introductionmentioning

confidence: 99%

A phogrin–aequorin chimaera to image free Ca2+ in the vicinity of secretory granules

Pouli

Karagenc

Wasmeier

et al. 1998

Biochemical Journal

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“…Accordingly, it was reported that cADPR, an activator of the RyR (15), releases Ca 2ϩ from the IS of pancreatic acini (16). More recently Gerasimenko et al (17) reported that the secretory granules, which are located in the LP, release Ca 2ϩ in response to IP 3 and cADPR.…”

mentioning

confidence: 99%

Polarized Expression of Ca2+ Channels in Pancreatic and Salivary Gland Cells

Lee¹,

Xu²,

Zeng³

et al. 1997

Journal of Biological Chemistry

265

200

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In polarized epithelial cells [Ca 2؉ ] i waves are initiated in discrete regions and propagate through the cytosol. The structural basis for these compartmentalized and coordinated events are not well understood. In the present study we used a combination of [Ca 2؉ ] i imaging at high temporal resolution, recording of Ca 2؉ -activated Cl ؊ current, and immunolocalization by confocal microscopy to study the correlation between initiation and propagation of [Ca 2؉ ] i waves and localization of Ca 2؉ release channels in pancreatic acini and submandibular acinar and duct cells. In all cells Ca 2؉ waves are initiated in the luminal pole and propagate through the cell periphery to the basal pole. All three cell types express the three known inositol 1,4,5-trisphosphate receptors (IP 3 Rs). Expression of IP 3 Rs was confined to the area just underneath the luminal and lateral membranes, with no detectable receptors in the basal pole or other regions of the cells. In pancreatic acini and SMG ducts IP 3 R3 was also found in the nuclear envelope. Expression of ryanodine receptor was detected in submandibular salivary gland cells but not pancreatic acini. Accordingly, cyclic ADP ribose was very effective in mobilizing Ca 2؉ from internal stores of submandibular salivary gland but not pancreatic acinar cells. Measurement of [Ca 2؉ ] i and localization of IP 3 Rs in the same cells suggests that only a small part of IP 3 Rs participate in the initiation of the Ca 2؉ wave, whereas most receptors in the cell periphery probably facilitate the propagation of the Ca 2؉ wave. The combined results together with our previous studies on this subject lead us to conclude that the internal Ca 2؉ pool is highly compartmentalized and that compartmentalization is achieved in part by polarized expression of Ca 2؉ channels.

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“…Isolated zymogen granules were found to release Ca 2+ in the presence of InsP 3 [55], although the same authors have also reported that in intact cells most of the Ca 2+ released by InsP 3 comes from the ER [56]. In mast cell granules [19] and mucin granules of goblet cells [57], InsP 3 induced periodic oscillations of luminal [Ca 2+ ] by coupling Ca 2+ release with the activity of a Ca 2+ -dependent K + channel in the granules.…”

Section: Mechanisms Of Ca 2+ Release From the Secretory Granulesmentioning

confidence: 97%

“…The ryanodine receptor activator cyclic ADP ribose (cADPR) has been reported to release Ca 2+ from zymogen granules [55,69]. Both cADPR and caffeine released also Ca 2+ from the secretory granules of insulin-secreting MIN6 cells [20], and caffeine, but not cADPR, released Ca 2+ from secretory granules in chromaffin cells [23].…”

Section: Mechanisms Of Ca 2+ Release From the Secretory Granulesmentioning

confidence: 99%

Calcium dynamics in the secretory granules of neuroendocrine cells

Álvarez¹

2012

Cell Calcium

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a b s t r a c t Cellular Ca 2+ signaling results from a complex interplay among a variety of Ca 2+ fluxes going across the plasma membrane and across the membranes of several organelles, together with the buffering effect of large numbers of Ca 2+ -binding sites distributed along the cell architecture. Endoplasmic and sarcoplasmic reticulum, mitochondria and even nucleus have all been involved in cellular Ca 2+ signaling, and the mechanisms for Ca 2+ uptake and release from these organelles are well known. In neuroendocrine cells, the secretory granules also constitute a very important Ca 2+ -storing organelle, and the possible role of the stored Ca 2+ as a trigger for secretion has attracted considerable attention. However, this possibility is frequently overlooked, and the main reason for that is that there is still considerable uncertainty on the main questions related with granular Ca 2+ dynamics, e.g., the free granular [Ca 2+ ], the physical state of the stored Ca 2+ or the mechanisms for Ca 2+ accumulation and release from the granules. This review will give a critical overview of the present state of knowledge and the main conflicting points on secretory granule Ca 2+ homeostasis in neuroendocrine cells.

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Inositol Trisphosphate and Cyclic ADP-Ribose–Mediated Release of Ca2+ from Single Isolated Pancreatic Zymogen Granules

Cited by 237 publications

References 37 publications

A phogrin–aequorin chimaera to image free Ca2+ in the vicinity of secretory granules

A phogrin–aequorin chimaera to image free Ca2+ in the vicinity of secretory granules

Polarized Expression of Ca2+ Channels in Pancreatic and Salivary Gland Cells

Calcium dynamics in the secretory granules of neuroendocrine cells

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