scholarly journals Subcellular localization of the superoxide-forming enzyme in human neutrophils.

1979 ◽  
Vol 63 (1) ◽  
pp. 21-29 ◽  
Author(s):  
B Dewald ◽  
M Baggiolini ◽  
J T Curnutte ◽  
B M Babior
Keyword(s):  
Subcellular Localization ◽  
Human Neutrophils

scholarly journals Subcellular localization and translocation of the receptor for N-formylmethionyl-leucyl-phenylalanine in human neutrophils

1994 ◽  
Vol 299 (2) ◽  
pp. 473-479 ◽  
Author(s):  
H Sengeløv ◽  
F Boulay ◽  
L Kjeldsen ◽  
N Borregaard
Keyword(s):  
Plasma Membrane ◽  
Subcellular Localization ◽  
Plasma Membranes ◽  
Secretory Vesicle ◽  
Human Neutrophils ◽  
Secretory Vesicles ◽  
Beta Band ◽  
Neutrophil Gelatinase Associated Lipocalin ◽  
Specific Granules ◽  
Inflammatory Stimuli

The subcellular localization of N-formylmethionyl-leucyl-phenylalanine (fMLP) receptors in human neutrophils was investigated. The fMLP receptor was detected with a high-affinity, photoactivatable, radioiodinated derivative of N-formyl-methionyl-leucyl-phenylalanyl-lysine (fMLFK). Neutrophils were disrupted by nitrogen cavitation and fractionated on Percoll density gradients. fMLP receptors were located in the beta-band containing gelatinase and specific granules, and in the gamma-band containing plasma membrane and secretory vesicles. Plasma membranes and secretory vesicles were separated by high-voltage free-flow electrophoresis, and secretory vesicles were demonstrated to be highly enriched in fMLP receptors. The receptors found in secretory vesicles translocated fully to the plasma membrane upon stimulation with inflammatory mediators. The receptor translocation from the beta-band indicated that the receptor present there was mainly located in gelatinase granules. A 25 kDa fMLP-binding protein was found in the beta-band. Immunoprecipitation revealed that this protein was identical with NGAL (neutrophil gelatinase-associated lipocalin), a novel protein found in specific granules. In summary, we demonstrate that the compartment in human neutrophils that is mobilized most easily and fastest, the secretory vesicle, is a major reservoir of fMLP receptors. This explains the prompt and extensive upregulation of fMLP receptors on the neutrophil surface in response to inflammatory stimuli.

scholarly journals The Thyroid Hormone Inactivating Enzyme Type 3 Deiodinase is Present in Bactericidal Granules and the Cytoplasm of Human Neutrophils

Endocrinology ◽  
2016 ◽  
Vol 157 (8) ◽  
pp. 3293-3305 ◽  
Author(s):  
Anne H. van der Spek ◽  
Flavia F. Bloise ◽  
Wikky Tigchelaar ◽  
Monica Dentice ◽  
Domenico Salvatore ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Subcellular Localization ◽  
Subcellular Location ◽  
Essential Elements ◽  
Neutrophil Extracellular Trap ◽  
Human Neutrophils ◽  
Transcriptional Level ◽  
Bacterial Killing ◽  
Effector Cells ◽  
Type 3

Neutrophils are important effector cells of the innate immune system. Thyroid hormone (TH) is thought to play an important role in their function. Intracellular TH levels are regulated by the deiodinating enzymes. The TH-inactivating type 3 deiodinase (D3) is expressed in infiltrating murine neutrophils, and D3 knockout mice show impaired bacterial killing upon infection. This suggests that D3 plays an important role in the bacterial killing capacity of neutrophils. The mechanism behind this effect is unknown. We aimed to assess the presence of D3 in human neutrophils, and determine its subcellular localization using confocal and electron microscopy, because this could give important clues about its function in these cells. D3 appeared to be present in the cytoplasm and in myeloperoxidase containing azurophilic granules and as well as lactoferrin containing specific granules within human neutrophils. This subcellular localization did not change upon activation of the cells. D3 is observed intracellularly during neutrophil extracellular trap formation, followed by a reduction of D3 staining after release of the neutrophil extracellular traps into the extracellular space. At the transcriptional level, human neutrophils expressed additional essential elements of TH metabolism, including TH transporters and TH receptors. Here, we demonstrate the presence and subcellular location of D3 in human neutrophils for the first time and propose a model, in which D3 plays a role in the bacterial killing capacity of neutrophils either through generation of iodide for the myeloperoxidase system or through modulation of intracellular TH bioavailability.

scholarly journals Subcellular localization of NAD(P)H oxidase(s) in human neutrophilic polymorphonuclear leucocytes

1978 ◽  
Vol 176 (1) ◽  
pp. 175-178 ◽  
Author(s):  
D B Iverson ◽  
P Wang-Iverson ◽  
J K Spitznagel ◽  
L R DeChatelet
Keyword(s):  
Cell Membrane ◽  
Nadph Oxidase ◽  
Subcellular Localization ◽  
Density Gradient ◽  
Membrane Fraction ◽  
Sucrose Density Gradient ◽  
Human Neutrophils ◽  
Polymorphonuclear Leucocytes

NADH and NADPH oxidase activities in a homogenate of human neutrophils co-sediment in a linear sucrose density gradient under either velocity or isopycnic conditions of centrifugation. The position of these activities in the gradient does not correspond to any known subcellular granule or to the cell-membrane fraction. These data suggest that the oxidase activities may reside in a unique granule that has previously not been recognized.

Expression and subcellular localization of syntaxin 11 in human neutrophils

2009 ◽  
Vol 58 (7) ◽  
pp. 407-412 ◽  
Author(s):  
Li-xin Xie ◽  
Janis de la Iglesia-Vicente ◽  
Yun-xiang Fang ◽  
Faustino Mollinedo
Keyword(s):  
Subcellular Localization ◽  
Human Neutrophils ◽  
Syntaxin 11

scholarly journals The src-family protein-tyrosine kinase p59hck is located on the secretory granules in human neutrophils and translocates towards the phagosome during cell activation

1995 ◽  
Vol 309 (2) ◽  
pp. 657-665 ◽  
Author(s):  
H Möhn ◽  
V Le Cabec ◽  
S Fischer ◽  
I Maridonneau-Parini
Keyword(s):  
Subcellular Localization ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Cell Activation ◽  
Secretory Granules ◽  
Human Neutrophils ◽  
Intracellular Traffic ◽  
Hl60 Cells ◽  
Protein Tyrosine ◽  
Family Protein

The src-family protein-tyrosine kinase p59hck is mainly expressed in neutrophils; however, its functional role in these cells is unknown. Several other src-family members are localized on secretory vesicles and have been proposed to regulate intracellular traffic. We have established here the subcellular localization of p59hck in human neutrophils. Immunoblotting of subcellular fractions showed that approx. 60% of the p59hck per cell is localized on the secretory granules; the other 40% is distributed equally between non-granular membranes and the cytosol. Immunofluorescence of neutrophils and HL60 cells suggests that the p59hck-positive granules are azurophil granules. Granular p59hck is highly susceptible to degradation by an azurophil-granule proteinase. Different forms of p59hck occur in the three subcellular compartments: a 61 kDa form is mainly found in the granules, a 59 kDa form is predominant in the non-granular membranes, whereas cytosolic p59hck migrates as a doublet at 63 kDa. During the process of phagocytosis-linked degranulation, induced by serum-opsonized zymosan in neutrophils or HL60 cells, granular p59hck translocates towards the phagosome. The subcellular localization of p59hck suggests that the enzyme could be involved in the regulation of the degranulation process.

Subcellular localization of heparanase in human neutrophils

1992 ◽  
Vol 51 (6) ◽  
pp. 519-524 ◽  
Author(s):  
Yaacov Matzner ◽  
Israel Vlodavsky ◽  
Matia Bar-Ner ◽  
Rivka Lshai-Michaeli ◽  
Alfred I. Tauber
Keyword(s):  
Subcellular Localization ◽  
Human Neutrophils

scholarly journals Subcellular localization of Gi alpha in human neutrophils.

1988 ◽  
Vol 263 (22) ◽  
pp. 10958-10964
Author(s):  
D Rotrosen ◽  
J I Gallin ◽  
A M Spiegel ◽  
H L Malech
Keyword(s):  
Subcellular Localization ◽  
Human Neutrophils

Identification and Subcellular Localization of Neuronal Calcium Sensor-1 (NCS-1) in Human Neutrophils and HL-60 Cells

Inflammation ◽  
2003 ◽  
Vol 27 (6) ◽  
pp. 361-372 ◽  
Author(s):  
Cristiana Brochetta ◽  
Maria Giovanna Perrotta ◽  
Andreas Jeromin ◽  
Maurizio Romano ◽  
Francesca Vita ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Human Neutrophils ◽  
Calcium Sensor ◽  
Neuronal Calcium Sensor
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