Ligation of selectin L and integrin CD11b/CD18 (Mac-1) induces release of gelatinase B (MMP-9) from human neutrophils

1998 ◽  
Vol 47 (8) ◽  
pp. 325-327 ◽  
Author(s):  
J. Wize ◽  
I. Sopata ◽  
A. Smerdel ◽  
S. Maśliński
Keyword(s):  
Human Neutrophils ◽  
Gelatinase B ◽  
Selectin L

scholarly journals BorreliaSpirochetes Upregulate Release and Activation of Matrix Metalloproteinase Gelatinase B (MMP-9) and Collagenase 1 (MMP-1) in Human Cells

2001 ◽  
Vol 69 (1) ◽  
pp. 456-462 ◽  
Author(s):  
Joseph A. Gebbia ◽  
James L. Coleman ◽  
Jorge L Benach
Keyword(s):  
Lyme Disease ◽  
Matrix Metalloproteinase ◽  
Human Peripheral Blood ◽  
Umbilical Vein ◽  
Active Form ◽  
Human Neutrophils ◽  
Blood Monocytes ◽  
Gelatinase B ◽  
Matrix Metalloproteinase 1

ABSTRACT Borrelia burgdorferi, the spirochetal agent of Lyme disease, stimulated human peripheral blood monocytes to release pro-matrix metalloproteinase-9 (gelatinase B; pro-MMP-9) and active matrix metalloproteinase-1 (collagenase-1; MMP-1). Human neutrophils also released pro-MMP-9 and a 130-kDa protein with gelatinolytic activity in response to live B. burgdorferi. In addition, U937 cells and human keratinocyte cells were also stimulated to release pro-MMP-9 under the same conditions. However, human umbilical vein endothelial cells (HUVECs) released pro-MMP-9 and pro-MMP-2 in a constitutive manner and were not influenced by live spirochetes. MMPs produced by human monocytes also enhanced the penetration of B. burgdorferi through extracellular matrix component barriers in vitro. Plasmin stabilized on the surface of the Lyme disease spirochete was shown to activate pro-MMP-9 to its active form. This active form was also observed in the plasma of mice infected with a relapsing fever borrelia. These results suggest that borreliae can upregulate MMPs and possibly mediate an activation cascade initiated by plasmin bound to the microbial surface. MMPs may play a role in dissemination of the Lyme disease spirochete and in the pathogenesis ofBorrelia infection.

scholarly journals Structural Characterization of the Catalytic Active Site in the Latent and Active Natural Gelatinase B from Human Neutrophils

2000 ◽  
Vol 275 (44) ◽  
pp. 34335-34343 ◽  
Author(s):  
Oded Kleifeld ◽  
Philippe E. Van den Steen ◽  
Anatoly Frenkel ◽  
Feng Cheng ◽  
Hua Liang Jiang ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Active Site ◽  
Human Neutrophils ◽  
Gelatinase B ◽  
Catalytic Active Site ◽  
Active Natural

Neutrophil Myeloperoxidase Destruction by Ultraviolet Irradiation

1988 ◽  
Vol 46 ◽  
pp. 138-139
Author(s):  
J. Hanker ◽  
B. Giammara ◽  
G. Strauss
Keyword(s):  
Uv Radiation ◽  
Myeloid Leukemia ◽  
Stratospheric Ozone ◽  
Psoriasis Patient ◽  
Whole Body ◽  
Human Neutrophils ◽  
Cupric Nitrate ◽  
The Earth ◽  
Routine Handling ◽  
Uvb Phototherapy

Only a fraction of the UV radiation emitted by the sun reaches the earth; most of the UVB (290-320nm) is eliminated by stratospheric ozone. There is increasing concern, however, that man-made chemicals are damaging this ozone layer. Although the effects of UV on DNA or as a carcinogen are widely known, preleukemia and acute myeloid leukemia (AML) have only rarely been reported in psoriasis patients treated with 8-methoxypsoralen and UV (PUVA). It was therefore of interest to study the effects of UV on the myeloperoxidase (MP) activity of human neutrophils. The peroxidase activity of enriched leukocyte preparations on coverslips was shown cytochemically with a diaminobenzidine medium and cupric nitrate intensification.Control samples (Figs. 1,4,5) of human bloods that were not specifically exposed to UV radiation or light except during routine handling were compared with samples which had been exposed in one of several different ways. One preparation (Fig. 2) was from a psoriasis patient who had received whole-body UVB phototherapy repeatedly.

Application of high-resolution field-emission LVSEM, backscatter imaging, immunogold staining to definition of the spatial distributions of two human neutrophil adherence receptors

1993 ◽  
Vol 51 ◽  
pp. 36-37
Author(s):  
Robert D. Nelson ◽  
Sharon R. Hasslen ◽  
Stanley L. Erlandsen
Keyword(s):  
Cell Surface ◽  
Surface Membrane ◽  
Three Dimensional ◽  
Human Neutrophils ◽  
Spatial Distributions ◽  
Immunogold Staining ◽  
Functional Control ◽  
Neutrophil Adherence ◽  
Definition Of ◽  
Mode Of Attachment

Receptors are commonly defined in terms of number per cell, affinity for ligand, chemical structure, mode of attachment to the cell surface, and mechanism of signal transduction. We propose to show that knowledge of spatial distribution of receptors on the cell surface can provide additional clues to their function and components of functional control.L-selectin and Mac-1 denote two receptor populations on the neutrophil surface that mediate neutrophil-endothelial cell adherence interactions and provide for targeting of neutrophil recruitment to sites of inflammation. We have studied the spatial distributions of these receptors using LVSEM and backscatter imaging of isolated human neutrophils stained with mouse anti-receptor (primary) antibody and goat anti-mouse (secondary) antibody conjugated to 12 nm colloidal gold. This combination of techniques provides for three-dimensional analysis of the expression of these receptors on different surface membrane domains of the neutrophil: the ruffles and microvilli that project from the cell surface, and the cell body between these projecting structures.

Inhibition of Apoptosis in Human Neutrophils by Helicobacter pylori Water-Soluble Surface Proteins

2001 ◽  
Vol 36 (6) ◽  
pp. 589-600 ◽  
Author(s):  
J. S. Kim ◽  
J. M. Kim ◽  
H. C. Jung ◽  
I. S. Song ◽  
C. Y. Kim
Keyword(s):  
Helicobacter Pylori ◽  
Water Soluble ◽  
Surface Proteins ◽  
Human Neutrophils

Author response for "T cell‐derived cytokines enhance the antigen‐presenting capacity of human neutrophils"

2019 ◽  
Author(s):  
Nazanin Samadi ◽  
Dominika Polak ◽  
Claudia Kitzmüller ◽  
Peter Steinberger ◽  
Gerhard J. Zlabinger ◽  
...  
Keyword(s):  
T Cell ◽  
Author Response ◽  
Human Neutrophils ◽  
Antigen Presenting

The Inhibitory Effect of Heparin and Related Glycosaminoglycans on Neutrophil Chemotaxis

1984 ◽  
Vol 52 (02) ◽  
pp. 134-137 ◽  
Author(s):  
Yaacov Matzner ◽  
Gerard Marx ◽  
Ruth Drexler ◽  
Amiram Eldor
Keyword(s):  
Specific Binding ◽  
Anticoagulant Activity ◽  
Neutrophil Migration ◽  
Inhibitory Effect ◽  
Chemotactic Factor ◽  
Human Neutrophils ◽  
Boyden Chamber ◽  
Neutrophil Chemotaxis ◽  
Inhibitory Effects ◽  
Chemotactic Factors

SummaryClinical observations have shown that heparin has antiinflammatory activities. The effect of heparin on neutrophil chemotaxis was evaluated in vitro in the Boyden Chamber. This method enabled differentiation between the direct effects of heparin on neutrophil migration and locomotion, and its effects on chemotactic factors. Heparin inhibited both the random migration and directed locomotion of human neutrophils toward zymosan-activated serum (ZAS) and F-met-leu-phe (FMLP). Inhibition was found to be dependent on the concentrations of the heparin and of the chemotactic factors. No specific binding of heparin to the neutrophils could be demonstrated, and heparin’s inhibitory effects were eliminated by simple washing of the cells. When added directly to the chamber containing chemotactic factor, heparin inhibited the chemotactic activity of ZAS but not that of FMLP, suggesting a direct inhibitory effect against C5a, the principal chemotactic factor in ZAS.Experiments performed with low-molecular-weight heparin, N-desulfated heparin, dextran sulfate, chondroitin sulfate and dextran indicated that the inhibitory effects of heparin on neutrophil chemotaxis are not related to its anticoagulant activity, but probably depend on the degree of sulfation of the heparin molecule.

Sign in / Sign up

Export Citation Format

Share Document