Identification of the complement 9‐binding protein in Setaria equina excretory‐secretory products

2019 ◽  
Vol 42 (2) ◽  
Author(s):  
Mahmoud Abdel‐Latif
Keyword(s):  
Binding Protein ◽  
Secretory Products ◽  
Setaria Equina

scholarly journals Neutrophils autoinactivate secretory products by myeloperoxidase- catalyzed oxidation

Blood ◽  
1985 ◽  
Vol 65 (2) ◽  
pp. 375-381 ◽  
Author(s):  
RA Clark ◽  
N Borregaard
Keyword(s):  
Vitamin B12 ◽  
Enzyme Inhibitors ◽  
Binding Protein ◽  
Extracellular Fluid ◽  
Kinetic Studies ◽  
Human Neutrophils ◽  
Resting Cells ◽  
Heme Enzyme ◽  
Inflammatory Stimuli ◽  
Secretory Products

Abstract The neutrophil response to inflammatory stimuli involves the formation of reactive oxygen species and secretion of granule enzymes. In studying secretion of vitamin B12 binding protein by human neutrophils, we noted a major decrease in total recoverable activity from the extracellular fluid plus the stimulated cells (54% of resting cells). Recovery of B12 binding protein from neutrophils exposed to phorbol myristate acetate or opsonized zymosan was significantly enhanced on addition of heme enzyme inhibitors (azide, cyanide) or catalase or when halide-free medium was used. The changes in B12 binding protein recovery were attributable entirely to increases in extracellular fluid levels, and cell pellet content was unaffected. These data indicate extracellular destruction of functional B12 binding protein by the halide-dependent heme enzyme myeloperoxidase and H2O2. Kinetic studies demonstrated rapid secretion of B12 binding protein in the first two to five minutes, followed by its inactivation over the next 20 to 30 minutes. A cell-free extract of vitamin B12 binding protein was readily inactivated on exposure to purified myeloperoxidase, H2O2, and a halide. These findings document a functional interaction among products of the neutrophil specific granules (B12 binding protein), azurophil granules (myeloperoxidase), and metabolic burst (H2O2). They provide an interesting model for the modulation of the inflammatory response by oxidation of secretory products of neutrophils.

scholarly journals Hookworm NK cell binding protein: identifying the 80kDa protein in Necator americanus excretory/secretory products

2008 ◽  
Vol 22 (S1) ◽  
Author(s):  
Soraya Gaze ◽  
Stephanie Constant ◽  
Jeff Bethony ◽  
Michael Smout ◽  
Alex Loukas
Keyword(s):  
Nk Cell ◽  
Binding Protein ◽  
Cell Binding ◽  
Necator Americanus ◽  
Secretory Products

Glycosaminoglycan: a candidate to stimulate the repair of chronic wounds

2005 ◽  
Vol 94 (07) ◽  
pp. 4-16 ◽  
Author(s):  
Philip V. Peplow
Keyword(s):  
Chronic Wounds ◽  
Binding Protein ◽  
Cathepsin G ◽  
Sustained Delivery ◽  
Heparin Binding ◽  
Anionic Polymers ◽  
Heparin Binding Protein ◽  
Persistent Inflammation ◽  
Large Numbers ◽  
Secretory Products

SummaryA persistent inflammation with large numbers of neutrophils is found in chronic wounds. Secretory products released from the neutrophils, which include proteinases and a heparin-binding protein, are detrimental to wound healing as they cause degradation of the extracellular matrix and growth factors, and promote further recruitment of neutrophils to the wound area. The neutrophil-derived elastase, cathepsin G, proteinase-3 and heparin-binding protein are cationic, and it is hypothesized that their effects can be inhibited by electrostatic binding with certain anionic polymers such as glycosaminoglycans or functionalized dextrans. A sustained delivery of such compounds alone or in combination from a biodegradable carrier may provide a stimulus for these wounds to pass to the next stage of repair.

scholarly journals Neutrophils autoinactivate secretory products by myeloperoxidase- catalyzed oxidation

Blood ◽  
1985 ◽  
Vol 65 (2) ◽  
pp. 375-381 ◽  
Author(s):  
RA Clark ◽  
N Borregaard
Keyword(s):  
Vitamin B12 ◽  
Enzyme Inhibitors ◽  
Binding Protein ◽  
Extracellular Fluid ◽  
Kinetic Studies ◽  
Human Neutrophils ◽  
Resting Cells ◽  
Heme Enzyme ◽  
Inflammatory Stimuli ◽  
Secretory Products

The neutrophil response to inflammatory stimuli involves the formation of reactive oxygen species and secretion of granule enzymes. In studying secretion of vitamin B12 binding protein by human neutrophils, we noted a major decrease in total recoverable activity from the extracellular fluid plus the stimulated cells (54% of resting cells). Recovery of B12 binding protein from neutrophils exposed to phorbol myristate acetate or opsonized zymosan was significantly enhanced on addition of heme enzyme inhibitors (azide, cyanide) or catalase or when halide-free medium was used. The changes in B12 binding protein recovery were attributable entirely to increases in extracellular fluid levels, and cell pellet content was unaffected. These data indicate extracellular destruction of functional B12 binding protein by the halide-dependent heme enzyme myeloperoxidase and H2O2. Kinetic studies demonstrated rapid secretion of B12 binding protein in the first two to five minutes, followed by its inactivation over the next 20 to 30 minutes. A cell-free extract of vitamin B12 binding protein was readily inactivated on exposure to purified myeloperoxidase, H2O2, and a halide. These findings document a functional interaction among products of the neutrophil specific granules (B12 binding protein), azurophil granules (myeloperoxidase), and metabolic burst (H2O2). They provide an interesting model for the modulation of the inflammatory response by oxidation of secretory products of neutrophils.

Identification of enolase as a plasminogen-binding protein in excretory-secretory products of Fasciola hepatica

FEBS Letters ◽  
2004 ◽  
Vol 563 (1-3) ◽  
pp. 203-206 ◽  
Author(s):  
Dolores Bernal ◽  
Jose Enrique de la Rubia ◽  
Ana M Carrasco-Abad ◽  
Rafael Toledo ◽  
Santiago Mas-Coma ◽  
...  
Keyword(s):  
Fasciola Hepatica ◽  
Binding Protein ◽  
Secretory Products

Kupffer cell activation by LPS is mediated via LPS binding protein and CD14

2001 ◽  
Vol 120 (5) ◽  
pp. A27-A27
Author(s):  
M FAN ◽  
S GOYERT ◽  
A AMINLARI ◽  
R KLEIN ◽  
L STEINSTRAESSER ◽  
...  
Keyword(s):  
Kupffer Cell ◽  
Cell Activation ◽  
Binding Protein ◽  
Lps Binding

Annexin VI is a Ca2+-sensitive CHSP-28 binding protein present on secretory granule membranes in acini

2001 ◽  
Vol 120 (5) ◽  
pp. A336-A336
Author(s):  
G GROBLEWSKI ◽  
D THOMAS ◽  
W TAFT ◽  
K KASPAR
Keyword(s):  
Secretory Granule ◽  
Binding Protein ◽  
Annexin Vi

235: The RNA-Binding Protein IMP3: A Novel Molecular Marker Predicts Progression of Superficial (TA and T1) Urothelial Carcinomas of Bladder

2007 ◽  
Vol 177 (4S) ◽  
pp. 78-79
Author(s):  
Lioudmila Sitnikova ◽  
Gary Mendese ◽  
Qin Lui ◽  
Bruce A. Woda ◽  
Di Lu ◽  
...  
Keyword(s):  
Molecular Marker ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Urothelial Carcinomas
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