scholarly journals Elastase as a marker for neutrophilic myeloid cells.

1984 ◽  
Vol 32 (4) ◽  
pp. 389-394 ◽  
Author(s):  
J A Kramps ◽  
P van der Valk ◽  
M M van der Sandt ◽  
J Lindeman ◽  
C J Meijer
Keyword(s):  
Cell Lines ◽  
Neutrophil Elastase ◽  
Human Neutrophil ◽  
Myeloid Cells ◽  
Hematopoietic Cell ◽  
Human Neutrophil Elastase ◽  
Specific Marker ◽  
Neoplastic Cells ◽  
Myeloproliferative Diseases ◽  
Myelomonocytic Leukemia

The immunohistochemical results obtained with antibodies directed against human neutrophil elastase is described. It was found that neutrophil elastase can be used as a specific marker of cells of the neutrophilic lineage. In normal hematopoietic cell preparations, only promyelocytes and more differentiated myeloid cells stain positive for elastase. In acute or chronic myeloid and myelomonocytic leukemia, the same neutrophil myeloid cells stain positive, whereas neoplastic cells of the monocytoid line are negative. Using elastase in conjunction with other markers, it is possible to differentiate easily the involvement of different cell lines in myeloproliferative diseases.

scholarly journals Use of monoclonal antibody against human neutrophil elastase in normal and leukaemic myeloid cells.

1988 ◽  
Vol 41 (8) ◽  
pp. 853-860 ◽  
Author(s):  
K A Pulford ◽  
W N Erber ◽  
J A Crick ◽  
I Olsson ◽  
K J Micklem ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Neutrophil Elastase ◽  
Human Neutrophil ◽  
Myeloid Cells ◽  
Human Neutrophil Elastase

Widening the Applicability of Human Neutrophil Elastase and Proteinase 3 Peptide Vaccines by Elucidating Immunogenic Non-HLA-A2 MHC Class I Restricted Epitopes.

Blood ◽  
2006 ◽  
Vol 108 (11) ◽  
pp. 3708-3708
Author(s):  
Rachel E. Hewitt ◽  
J. Joseph Melenhorst ◽  
David A. Price ◽  
Emma Gostick ◽  
Nancy F. Hensel ◽  
...  
Keyword(s):  
Amino Acids ◽  
T Cell ◽  
Cell Lines ◽  
Neutrophil Elastase ◽  
Human Neutrophil ◽  
Peptide Sequence ◽  
Human Neutrophil Elastase ◽  
Proteinase 3 ◽  
Short Term ◽  
T Cell Lines

Abstract Human Neutrophil Elastase (HNE) and proteinase 3 (Pr3) belong to a group of myeloid tissue restricted serine proteases, aberrantly expressed by myeloid leukemia cells of interest as a source of myeloid-restricted antigens applicable to immunization strategies. HNE shares with Pr3 the antigenic PR1 peptide sequence inducing HLA-A*0201 restricted cytotoxic T cells (CTL) against leukemic cells. Our previous studies with full length HNE protein have demonstrated its potential for inducing both CD4+ and CD8+ T cell responses in healthy individuals including HLA-A2 negative individuals, suggesting an immunogenic potential of HNE beyond the PR1 peptide (Fujiwara H et al Blood 2004). To find epitopes other than PR1 in HNE and Pr3, peripheral blood mononuclear cells (PBMC) from 15 AML patients were screened at diagnosis or relapse with a peptide matrix consisting of 15mers overlapping by 11 amino acids spanning HNE and Pr3.The corresponding Pr3 and HNE 15mers were also used to generate and test short term T cell lines derived from patient samples. Responses to the peptide matrix pools were measured by a CFSE flow cytometry-based proliferation assay where the proliferating fraction in response to peptide pools was compared to the background co-stimulatory antibody only control for each assay. A positive response was defined as a proliferating fraction minimum 0.1% of the total CD8/CD3 population after subtraction of background proliferation and at least one and a half times background for each assay. These steps helped to control for variability between samples. Using this strategy we identified PR1 and 6 new candidate epitopes contained within HNE and Pr3. Corresponding immunogenic Pr3 sequences in 2 epitopes differed by only 3 amino acids from the immunogenic HNE sequence. CD8 short term T cell lines generated to these epitopes were restricted by HLA-A2, B35 and A68. Optimal peptide length was predicted using RANKPEP (http://www.mifoundation.org/Tools/rankpep.html) and confirmed with flow cytometric assays measuring responses to candidate epitopes, by interferon-gamma, tumor necrosis factor-alpha, IL-2 production and degranulation in response to HLA-matched or mismatched EBV-transformed B cell antigen-presenting cells pulsed with relevant and irrelevant peptides. This study confirms the presence of multiple immunogenic epitopes in HNE and Pr3 and represents the first step in developing a multi-peptide leukemia vaccine broadly applicable to individuals of diverse HLA type.

scholarly journals Flavonoids as inhibitors of human neutrophil elastase

2021 ◽  
Vol 36 (1) ◽  
pp. 1016-1028
Author(s):  
Katarzyna Jakimiuk ◽  
Jakub Gesek ◽  
Atanas G. Atanasov ◽  
Michał Tomczyk
Keyword(s):  
Neutrophil Elastase ◽  
Human Neutrophil ◽  
Human Neutrophil Elastase

Inhibition of Human Neutrophil Elastase with Peptidyl Electrophilic Ketones. 2. Orally Active PG-Val-Pro-Val Pentafluoroethyl Ketones

1994 ◽  
Vol 37 (26) ◽  
pp. 4538-4553 ◽  
Author(s):  
Michael R. Angelastro ◽  
Larry E. Baugh ◽  
Philippe Bey ◽  
Joseph P. Burkhart ◽  
Teng-Man Chen ◽  
...  
Keyword(s):  
Neutrophil Elastase ◽  
Human Neutrophil ◽  
Human Neutrophil Elastase ◽  
Orally Active

Optimisation of a human neutrophil elastase assay and investigation of the effect of sesquiterpene lactones

Biologicals ◽  
2005 ◽  
Vol 33 (3) ◽  
pp. 175-184 ◽  
Author(s):  
Karin Schorr ◽  
Anita Rott ◽  
FernandoBatista Da Costa ◽  
Irmgard Merfort
Keyword(s):  
Neutrophil Elastase ◽  
Human Neutrophil ◽  
Sesquiterpene Lactones ◽  
Human Neutrophil Elastase
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