scholarly journals Neutrophil Elastase and Proteinase 3 Cleavage Sites Are Adjacent to the Polybasic Sequence within the Proteolytic Sensitive Activation Loop of the SARS-CoV-2 Spike Protein

ACS Omega ◽  
2021 ◽  
Author(s):  
Zhadyra Mustafa ◽  
Anuar Zhanapiya ◽  
Hubert Kalbacher ◽  
Timo Burster
Keyword(s):  
Neutrophil Elastase ◽  
Spike Protein ◽  
Activation Loop ◽  
Proteinase 3 ◽  
Cleavage Sites

scholarly journals Functional analysis of potential cleavage sites in the MERS-coronavirus spike protein

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Hannah Kleine-Weber ◽  
Mahmoud Tarek Elzayat ◽  
Markus Hoffmann ◽  
Stefan Pöhlmann
Keyword(s):  
Functional Analysis ◽  
Spike Protein ◽  
Cleavage Sites

scholarly journals Neutrophil Elastase and Proteinase-3 Trigger G Protein-biased Signaling through Proteinase-activated Receptor-1 (PAR1)

2013 ◽  
Vol 288 (46) ◽  
pp. 32979-32990 ◽  
Author(s):  
Koichiro Mihara ◽  
Rithwik Ramachandran ◽  
Bernard Renaux ◽  
Mahmoud Saifeddine ◽  
Morley D. Hollenberg
Keyword(s):  
G Protein ◽  
Neutrophil Elastase ◽  
Proteinase 3 ◽  
Biased Signaling

scholarly journals Oxidized elafin and trappin poorly inhibit the elastolytic activity of neutrophil elastase and proteinase 3

FEBS Journal ◽  
2005 ◽  
Vol 272 (22) ◽  
pp. 5883-5893 ◽  
Author(s):  
Shila M. Nobar ◽  
Marie-Louise Zani ◽  
Christian Boudier ◽  
Thierry Moreau ◽  
Joseph G. Bieth
Keyword(s):  
Neutrophil Elastase ◽  
Proteinase 3 ◽  
Elastolytic Activity

Abnormal Localization of Neutrophil Elastase in Patients with Severe Congenital Neutropenia.

Blood ◽  
2006 ◽  
Vol 108 (11) ◽  
pp. 1279-1279
Author(s):  
Takashi Sato ◽  
Masakazu Habara ◽  
Hiroki Kihara ◽  
Hiroshi Kawaguchi ◽  
Mizuka Miki ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Dimensional Analysis ◽  
Protein Trafficking ◽  
Neutrophil Elastase ◽  
Plasma Membranes ◽  
Normal Subjects ◽  
Precursor Cells ◽  
Proteinase 3 ◽  
Severe Congenital Neutropenia ◽  
Congenital Neutropenia

Abstract Mutations in the ELA2 gene encoding neutrophil elastase (NE) in patients with severe congenital neutropenia (SCN) are involved in the pathogenesis of this disorder, possibly due to the abnormal protein trafficking and accelerated apoptosis of myeloid cells. In this study we precisely examined the localization of NE in neutrophils and myeloid precursor cells in bone marrow in patients with SCN using immunofluorescence microscopy equipped with three-dimensional analysis program. Three patients with SCN were enrolled in this study. All patients with SCN showed heterozygous mutation in the ELA2 gene. In normal subjects the pattern of localization of NE in mature neutrophils was almost similar to those of myeloperoxidase (MPO), proteinase 3, lysosomal associated membrane protein 2 (LAMP2). Administration of G-CSF to normal subjects did not affect the pattern of the localization of these proteins in neutrophils. In contrast, mature neutrophils elicited by the administration of G-CSF in patients with SCN NE predominantly localized to the plasma membranes. A small part of NE was detected in the cytoplasmic compartment. The pattern of localization of NE was significantly different from those of MPO, proteinase 3, and LAMP2 in SCN patients, suggesting the abnormal traffic of NE to granules. Adaptor proteins 3 (AP3) specifically shuttles transmembrane cargo proteins from the trans-Golgi to lysosomes. AP3 of myeloid progenitor cells enriched for CD33-positive cells in normal bone marrow was localized in both cytoplasm and plasma membranes. The localization pattern of AP3 was completely consistent with those of NE, MPO, and LAMP2. The localization of AP3 of promyelocytes in patients with SCN was observed in both plasma membranes and cytoplasm. This finding was completely similar to that in normal myeloid precursor cells. However, the localization of NE of promyelocytes in SCN patients was predominantly in plasma membrane. The figures merged apparently presented the different localization of NE and AP3. This result was confirmed by the 3-dimensional analysis with histogram. The localizations of other constituents of primary granules, MPO, poteinase 3, and LAMP2, were consistent with those of AP3. These observations suggest that the mislocalization of NE in myeloid precursor cells in SCN patients does not result from a generalized impairment of protein trafficking but is specific to the mutant NE. The abnormal localization of NE may be involved in the pathogenesis of SCN associated with ELA2 mutation.

A new proteinase 3 substrate with improved selectivity over human neutrophil elastase

2013 ◽  
Vol 442 (1) ◽  
pp. 75-82 ◽  
Author(s):  
J. Popow-Stellmaszyk ◽  
M. Wysocka ◽  
A. Lesner ◽  
B. Korkmaz ◽  
K. Rolka
Keyword(s):  
Neutrophil Elastase ◽  
Human Neutrophil ◽  
Human Neutrophil Elastase ◽  
Proteinase 3
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