Redistribution of intracellular Ca2+ stores during phagocytosis in human neutrophils

Stendahl, Olle; Krause, Karl Heinz; Krischer, Joachim; Jerström, Petra; Theler, Jean Marc; Clark, Robert A.; Carpentier, J L; Lew, Daniel Pablo

doi:10.1126/science.8073285

Cited by 137 publications

(82 citation statements)

References 36 publications

(6 reference statements)

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“…One possible identity for the peripheral Ca 2ϩ stores, identified by these older studies and by the data presented here, is calciosomes, small organelles that are widespread throughout neutrophils [26,27]. These organelles, which contain the necessary molecular characteristics for both Ca 2ϩ storage and release, are probably those which release local Ca 2ϩ in response to phagocytic events [28][29][30] and Fc receptor cross-linking [6,31,32]. They are also mobile within the neutrophil, and move to the neutrophil periphery and accumulate at sites of phagocytosis [29,33].…”

Section: Discussionmentioning

confidence: 97%

“…These organelles, which contain the necessary molecular characteristics for both Ca 2ϩ storage and release, are probably those which release local Ca 2ϩ in response to phagocytic events [28][29][30] and Fc receptor cross-linking [6,31,32]. They are also mobile within the neutrophil, and move to the neutrophil periphery and accumulate at sites of phagocytosis [29,33]. The selective photodamage induced by DiOC 6 (3) reported here also point to separate functional Ca 2ϩ release locations in the neutrophil.…”

Section: Discussionmentioning

confidence: 99%

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Two distinct Ca2+ storage and release sites in human neutrophils

Pettit

Hallett

1998

Journal of Leukocyte Biology

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in response to N-formyl-methionyl-leucyl-phenylalanine, whereas engagement and clustering of CD11b/CD18 integrins causes Ca 2؉ release from the peripheral stores. The release sites also correlated with organelles that stained with DiOC 6 (3). Localized phototoxicity generated by DiOC 6 (3) excitation resulted in inhibition of the release of stored Ca 2؉ , which was selective for the stimulus used. The presence of two distinct cellular locations for these Ca 2؉ stores and their independent release raises the possibility that separate intracellular messengers for their release are generated.

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Two distinct Ca2+ storage and release sites in human neutrophils

Pettit

Hallett

1998

Journal of Leukocyte Biology

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“…CRT and calcium-ATPase are redistributed during the process of phagocytosis, with CRT becoming concentrated around particles being ingested (Stendahl et al, 1994). This concentration occurs before phagocytosis is complete and also before the measurable increase in the concentration of intracellular calcium occur, indicating that redistribution of the stores precedes calcium release.…”

mentioning

confidence: 97%

Abundant Accumulation of the Calcium-Binding Molecular Chaperone Calreticulin in Specific Floral Tissues of Arabidopsis thaliana

1997

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Calreticulin (CRT) is a calcium-binding protein in the endoplasmic reticulum (ER) with an established role as a molecular chaperone. An additional function in signal transduction, specifically in calcium distribution, is suggested but not proven. We have analyzed the expression pattern of Arabidopsis thaliana CRTs for a comparison with these proposed roles. Three CRT genes were expressed, with identities of the encoded proteins ranging from 54 to 86%. Protein motifs with established functions found in CRTs of other species were conserved. CRT was found in all of the cells in low amounts, whereas three distinct floral tissues showed abundant expression: secreting nectaries, ovules early in development, and a set of subepidermal cells near the abaxial surface of the anther. Localization in the developing endosperm, which is characterized by high protein synthesis rates, can be reconciled with a specific chaperone function. Equally, nectar production and secretion, a developmental stage marked by abundant ER, may require abundant CRT to accommodate the traffic of secretory proteins through the ER. Localization of CRT in the anthers, which are degenerating at the time of maximum expression of CRT, cannot easily be reconciled with a chaperone function but may indicate a role for CRT in anther maturation or dehiscence.

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“…Because of the periphagosomal translocation of gelsolin, we analyzed late events in CR-mediated phagocytosis in Gsn Ϫ neutrophils. During particle ingestion, an actin ring forms around the phagosome (11). The actin ring is later dissolved in a Ca 2ϩ -dependent fashion (10), possibly to facilitate the fusion of granules with the phagosome.…”

Section: Phagosomal Actin Reorganization Granule Translocation and mentioning

confidence: 99%

“…and O.S., unpublished observations). Intracellular Ca 2ϩ stores and granules also translocate to the phagosome and phagolysosome fusion takes place (11). In neutrophils, this is a calcium-dependent process (12).…”

mentioning

confidence: 99%

Selective Inhibition of IgG-Mediated Phagocytosis in Gelsolin-Deficient Murine Neutrophils

Serrander

Skarman

Rasmussen

et al. 2000

The Journal of Immunology

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Phagocytosis and the microbicidal functions of neutrophils require dynamic changes of the actin cytoskeleton. We have investigated the role of gelsolin, a calcium-dependent actin severing and capping protein, in peripheral blood neutrophils from gelsolin-null (Gsn−) mice. The phagocytosis of complement opsonized yeast was only minimally affected. In contrast, phagocytosis of IgG-opsonized yeast was reduced close to background level in Gsn− neutrophils. Thus, gelsolin is essential for efficient IgG- but not complement-mediated phagocytosis. Furthermore, attachment of IgG-opsonized yeast to Gsn− neutrophils was reduced (∼50%) but not to the same extent as ingestion (∼73%). This was not due to reduced surface expression of the Fcγ-receptor or its lateral mobility. This suggests that attachment and ingestion of IgG-opsonized yeast by murine neutrophils are actin-dependent and gelsolin is important for both steps in phagocytosis. We also investigated granule exocytosis and several steps in phagosome processing, namely the formation of actin around the phagosome, translocation of granules, and activation of the NADPH-oxidase. All these functions were normal in Gsn− neutrophils. Thus, the role of gelsolin is specific for IgG-mediated phagocytosis. Our data suggest that gelsolin is part of the molecular machinery that distinguishes complement and IgG-mediated phagocytosis. The latter requires a more dynamic reorganization of the cytoskeleton.

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Redistribution of intracellular Ca2+ stores during phagocytosis in human neutrophils

Cited by 137 publications

References 36 publications

Two distinct Ca2+ storage and release sites in human neutrophils

Two distinct Ca2+ storage and release sites in human neutrophils

Abundant Accumulation of the Calcium-Binding Molecular Chaperone Calreticulin in Specific Floral Tissues of Arabidopsis thaliana

Selective Inhibition of IgG-Mediated Phagocytosis in Gelsolin-Deficient Murine Neutrophils

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