Rapid purification of glycosyl-phosphatidylinositol-anchored alkaline phosphatase from human neutrophils after up-regulation to the cell surface.

Cain, Timothy J.; Liu, Youjiang; Kobayashi, Toshihiro; Robinson, JM

doi:10.1177/41.9.8394855

Cited by 14 publications

(7 citation statements)

References 11 publications

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“…Three others were rinsed briefly with PBSK (2.7 mM NaCl, 137 mM KCl, 6.45 mM Na 2 PO 4 , and 1.47 mM KH 2 PO4, pH 7.3) and then incubated in PBSK containing PI-PLC from Bacillus cereus (PI-PLC; Sigma, USA) for 15 and 45 min at 37C. One milliliter of PBSK, containing 500 mU PI-PLC, was used on each of the two sections in a moist chamber at room temperature (Cain et al 1993). The remaining section was incubated in the PBSK alone for 45 min.…”

Section: Release Of Alp With Pi-plcmentioning

confidence: 99%

“…However, the anchor molecules in the bond between ALP and the extracellular matrix, especially collagen fibers, have not yet been identified. Phosphatidylinositol-specific phospholipase C (PI-PLC) can split the phosphatidylinositol (PI) molecule between ALP and the plasma membrane, releasing and dissipating the activity of ALP (Cain et al 1993;Ikezawa et al 1976). Therefore, to examine the bond between ALP and collagen fibers, we used PI-PLC in a histochemical study of ALP activity in the periodontal ligament of rat molars.…”

Section: Introductionmentioning

confidence: 98%

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Phosphatidylinositol-dependent bond between alkaline phosphatase and collagen fibers in the periodontal ligament of rat molars

Nakamura

Noda

Shimpo

et al. 2004

Histochemistry and Cell Biology

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Alkaline phosphatase (ALP) is anchored to the outer leaflet of the lipid bilayer via phosphatidylinositol (PI) and ALP activity has been localized in the plasma membrane of numerous tissues. In the periodontal ligament ALP activity is found in the collagen fibers in addition to the plasma membrane of the osteoblasts and fibroblasts. In this study, we examined the distribution of ALP activity in the periodontal ligament of rat molars and also examined whether the bond between ALP and collagen fibers is dependent on PI by using phosphatidylinositol-specific phospholipase C (PI-PLC). ALP activity was distributed in the periodontal ligament. The activity mirrored the distribution of collagen fibers in the periodontal ligament. Cytochemical analysis also demonstrated that ALP activity was located not only in the plasma membrane of fibroblasts, but also in the collagen fiber bundles and fibrils in the periodontal ligament. After treatment with PI-PLC, the loss of ALP activity in the periodontal ligament was observed histochemically, and the loss of ALP activity in the fibroblasts as well as in the collagen fiber bundles and fibrils was observed cytochemically. These results strongly indicate that the bond between ALP and the collagen fibers is also dependent on PI.

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Section: Release Of Alp With Pi-plcmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

Phosphatidylinositol-dependent bond between alkaline phosphatase and collagen fibers in the periodontal ligament of rat molars

Nakamura

Noda

Shimpo

et al. 2004

Histochemistry and Cell Biology

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“…Electropermeabilized cells suspended in buffer C were stimulated with 20 µM GDPβS, 20 µM GTPγS, 10 -7 M fMLP, or 50 ng/ml PMA for 5 min at 37°C. To minimize subsequent internalization of the plasma membrane and ensure maximal detection of the ALPase activity at the cell surface in the biochemical assay, 5 µg/ml CB was simultaneously added to the incubation medium (Cain et al 1993). MAPTAMloaded cells were stimulated for 15 min at 37°C in Ca 2+ -depleted buffer B containing fMLP without CB.…”

Section: Cell Stimulationmentioning

confidence: 99%

Intracellular dynamics of alkaline phosphatase-containing granules in electropermeabilized human neutrophils

Kobayashi

Zinchuk²,

Okada³

et al. 1998

Histochemistry and Cell Biology

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Human neutrophils possess alkaline phosphatase-containing intracellular granules which are upregulated to the cell surface upon stimulation. The mechanism that governs the intracellular dynamics of these granules is, however, poorly understood. The aim of the present study was to investigate the possible participation of GTP-binding proteins in the reorganization and exocytosis of the alkaline phosphatase-containing granules using electropermeabilized cells. Biochemical assays using intact neutrophils showed that the alkaline phosphatase activity was upregulated and exocytosed into the extracellular space upon stimulation with AIF4 and N-formyl peptide. This upregulation was inhibited by treatment of cells with pertussis toxin and botulinum toxin. Alkaline phosphatase activity was also upregulated in electropermeabilized cells stimulated with guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS), but not with guanosine 5'-O-(2-thiodiphosphate) (GDPbetaS). Cytochemically, alkaline phosphatase-containing granules were dispersed throughout the cytoplasm in unstimulated electropermeabilized neutrophils. Upon stimulation with GTPgammaS, but not with GDPbetaS, these granules fused to form elongated tubular structures which eventually became associated with the plasma membrane. Nocodazole disturbed the reorganization of the alkaline phosphatase-containing granules in cells stimulated with GTPgammaS. The results from this study indicate that GTP-binding proteins participate in the reorganization and exocytosis of alkaline phosphatase-containing granules associated with the microtubules in electropermeabilized human neutrophils.

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“…Neutrophils express CD39 (9) and alkaline phosphatase (19), but lack CD73 (9). Of importance, stimulated vascular endothelial cells directly interacting with neutrophils express CD39 and CD73 (8,20,21).…”

Section: Introductionmentioning

confidence: 99%

Role of neutrophil purinergic receptors in organ dysfunction

Sullivan

Linden

2009

Journal of Organ Dysfunction

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Neutrophils [polymorphonuclear leukocytes (PMNs)] express several purinergic receptors, including the nucleotide receptors P2Y2 and P2X7 and the adenosine receptor subtypes A 1 , A 2A and A 3 . Activation of these receptors modulates PMN function and ultimately, in concert with other cells, affects the host's innate inflammatory response. PMN activities that can be altered by purinergic receptor stimulation include adhesion, aggregation, migration, phagocytosis, microbicidal function, release of tissue-damaging products and apoptosis. Interventions that alter PMN purinergic receptor stimulation are being developed to reduce organ dysfunction in conditions such as sepsis, ischemiaÁreperfusion injury and the acute respiratory distress syndrome.

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Rapid purification of glycosyl-phosphatidylinositol-anchored alkaline phosphatase from human neutrophils after up-regulation to the cell surface.

Cited by 14 publications

References 11 publications

Phosphatidylinositol-dependent bond between alkaline phosphatase and collagen fibers in the periodontal ligament of rat molars

Phosphatidylinositol-dependent bond between alkaline phosphatase and collagen fibers in the periodontal ligament of rat molars

Intracellular dynamics of alkaline phosphatase-containing granules in electropermeabilized human neutrophils

Role of neutrophil purinergic receptors in organ dysfunction

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