Adenosine triphosphate-dependent calcium pump in the plasma membrane of guinea pig and human neutrophils.

Lagast, H; Lew, P D; Waldvogel, Francis

doi:10.1172/jci111180

Cited by 49 publications

(29 citation statements)

References 46 publications

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“…We have recently demonstrated that inside-out vesicles from the plasma membrane of PMA-treated guinea pig and human neutrophils can accumulate large amounts of calcium in a calmodulin sensitive, Mg-ATP-dependent process (10). The calcium accumulation has been attributed to a plasma membrane calcium pump with characteristics similar to that described in other tissues (11,12).…”

Section: Introductionmentioning

confidence: 68%

Phorbol myristate acetate stimulates ATP-dependent calcium transport by the plasma membrane of neutrophils.

Lagast¹,

Pozzan²,

Waldvogel³

et al. 1984

J. Clin. Invest.

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184

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Abstract. We studied the effect of phorbol myristate acetate (PMA) on the plasma membrane ATPdependent calcium pump in neutrophils. Plasma membrane-enriched fractions ("podosomes") from PMAstimulated guinea pig neutrophils exhibited a twofold stimulation of ATP-dependent calcium transport when compared with control podosomes. The stimulatory effect was rapid (beginning less than 2 min after exposure to PMA) and reached maximal values within 5 min. PMA increased the maximum velocity but not the affinity of the calcium pump for Ca". These results suggest that the calcium pump in the plasma membrane of neutrophils may be stimulated by calcium-independent pathways, and that this activation

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Section: Introductionmentioning

confidence: 68%

Phorbol myristate acetate stimulates ATP-dependent calcium transport by the plasma membrane of neutrophils.

Lagast¹,

Pozzan²,

Waldvogel³

et al. 1984

J. Clin. Invest.

Self Cite

184

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“…We therefore looked for the effect of 10 juM digitonin, known to permeabilize the plasma membrane of neutrophils (6), and the effect of 30 gM vanadate, known to completely inhibit the Ca2' pump of the plasma membrane of neutrophils (7). At these concentrations neither agent was able to release Ca2' from the nonmitochondrial Ca2+ pool of the homogenate (Table II).…”

Section: Resultsmentioning

confidence: 99%

“…[Ca2+], of neutrophils is regulated by both intracellular compartments (6) and the plasma membrane (7). To maintain low levels of [Ca2+], in resting cells (-100 nM) against the extracellular Ca2+ concentration of 2 mM, the intracellular compartments actively take up calcium ions, whereas the plasma membrane Ca2+/Mg2+-ATPase pumps out calcium ions.…”

Section: Introductionmentioning

confidence: 99%

Subcellular distribution of Ca2+ pumping sites in human neutrophils.

Krause¹,

Lew²

1987

J. Clin. Invest.

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The distribution of nonmitochondrial Ca2l pumping sites and the site of action of inositol 1,4,5-trisphosphate (Ins 1,4,5-P3) were studied in subcellular fractions of human neutrophils.In homogenates, two different Ca2+ pools could be observed: a mitochondrial Ca"+ pool and a nonmitochondrial, ATP-dependent, Ins 1,4,5-P3-responsive Ca2+ pool. When the homogenate was separated into microsomes, primary granules, and secondary granules, the nonmitochondrial (a2+ pumping and the Ins 1,4,5-P3-induced Ca2+ release occurred only in the microsomal fraction.In a gradient developed to separate different microsomal organelles, maximal Ca" pumping activity occurred in fractions of low densities. Correlations between Ca2+ uptake and organelle markers were negative for the endoplasmic reticulum (r = -0.49) and positive for plasma membrane (r = 0.47), Golgi (r = 0.62), and endosomes (r = 0.96). Because the Ca2+ pumping organelles in these fractions were insensitive to micromolar vanadate and digitonin treatment, they are unlikely to be plasma membrane vesicles. We conclude first that microsomal fractions of human neutrophils contain organelles that lower the ambient free Ca2+ concentration and respond to Ins 1,4,5-P3. Second, granules are not involved in intracellular Ca2+ regulation in neutrophils. Third, nonendoplasmic reticulum organelles, such as endosomes, Golgi elements, or yet undefined specialized structures, play a major role in intracellular Ca22 homeostasis in human neutrophils.

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“…Our present knowledge of the plasma membrane pump of neutrophils is based upon studies in insideout plasma membrane vesicles (41,42). The enzyme seems to be, similar to the intracellular Ca 2+ -pump, a Ca 2+ -ATPase, requiring ATP-hydrolysis for activity.…”

Section: +mentioning

confidence: 99%