Immuno-electron microscopy reveals that the excitotoxin quinolinate is associated with the plasma membrane in human peripheral blood monocytes/macrophages

1997 ◽  
Vol 290 (3) ◽  
pp. 633-639 ◽  
Author(s):  
V. Sung ◽  
C. N. Venkateshan ◽  
J. R. Moffett ◽  
L. Williamson ◽  
C. J. Gibbs Jr. ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Plasma Membrane ◽  
Peripheral Blood ◽  
Human Peripheral Blood ◽  
Blood Monocytes ◽  
Peripheral Blood Monocytes ◽  
Immuno Electron Microscopy

scholarly journals Thromboplastin (tissue factor) in plasma membranes of human monocytes

1985 ◽  
Vol 228 (3) ◽  
pp. 735-743 ◽  
Author(s):  
O Hetland ◽  
A B Brovold ◽  
R Holme ◽  
G Gaudernack ◽  
H Prydz
Keyword(s):  
Plasma Membrane ◽  
Phospholipase C ◽  
Peripheral Blood ◽  
Plasma Membranes ◽  
Human Peripheral Blood ◽  
Indirect Evidence ◽  
Blood Monocytes ◽  
Peripheral Blood Monocytes ◽  
Whole Cells ◽  
Hydrolysis Of

The synthesis of thromboplastin, a potent trigger of blood coagulation, can be induced in human peripheral blood monocytes. Indirect evidence suggests that newly synthesized thromboplastin becomes in part available on the cell surface. We have attempted to study the localization and availability of thromboplastin more directly by isolating plasma membranes from isolated human peripheral blood monocytes. The specific activities of the plasma membrane markers increased 16-22-fold in these preparations with a recovery of about 15%. The contamination by mitochondria, lysosomes, nuclei and endoplasmic reticulum was low as estimated by marker enzymes and electron microscopy. In both unstimulated and stimulated monocytes thromboplastin was largely recovered in this plasma membrane fraction, providing direct evidence for its membrane localization. Phospholipase C (E.C. 3.1.4.3) is a potent inactivator of thromboplastin through its hydrolysis of the phospholipids necessary for thromboplastin activity [Otnaess, Prydz, Bjørklid & Berre (1972) Eur. J. Biochem. 27, 238-243]. About 70% of the total membrane thromboplastin activity was inactivated when whole cells were treated with phospholipase C and the membranes subsequently isolated. Following stimulation to induce thromboplastin synthesis, the plasma membranes showed a shift in their relative content of phosphatidylcholine and phosphatidylethanolamine consistent with a transmethylation process.

scholarly journals Identification of normal human peripheral blood monocytes and liver as sites of synthesis of coagulation factor XIII a-chain

Blood ◽  
1987 ◽  
Vol 70 (2) ◽  
pp. 579-582
Author(s):  
LJ Weisberg ◽  
DT Shiu ◽  
PR Conkling ◽  
MA Shuman
Keyword(s):  
Peripheral Blood ◽  
Factor Xiii ◽  
Human Peripheral Blood ◽  
Cdna Probe ◽  
Coagulation Factor ◽  
Blood Monocytes ◽  
Peripheral Blood Monocytes ◽  
Normal Human ◽  
Normal Human Peripheral Blood ◽  
A Chain

Factor XIII is the fibrin-stabilizing factor that covalently cross- links fibrin monomers to form a highly organized, stable fibrin clot. The plasma form of factor XIII is a heterodimer, a2b2, consisting of two a-chains and two b-chains; the intracellular form, such as in platelets and placenta, is a dimer, a2, consisting of a-chains only. The catalytic function of factor XIII, a transglutaminase, resides in the a-chain. To address questions regarding sites of synthesis of factor XIII a-chain, an EcoRI restriction fragment from the protein- coding region of the factor XIII a-chain cDNA was used as a probe for Northern blot analysis. The cDNA probe showed hybridization with a single approximately 4.0-kilobase (kb) message in poly (A)+ mRNA prepared from normal human peripheral blood monocytes and normal human liver. The results demonstrate conclusively that factor XIII a-chains are actively synthesized in circulating monocytes and in liver. To our knowledge, these data represent the first demonstration of synthesis of any blood coagulation factor in primary uncultured and unstimulated monocytes or macrophage cells.

scholarly journals Peroxynitrite reduces endotoxin-induced tissue factor expression in human peripheral blood monocytes

Critical Care ◽  
10.1186/cc29 ◽  
1997 ◽  
Vol 1 (Suppl 1) ◽  
pp. P023
Author(s):  
M Gerlach ◽  
D Keh ◽  
S Spielmann ◽  
T Kerner ◽  
R Peter ◽  
...  
Keyword(s):  
Tissue Factor ◽  
Peripheral Blood ◽  
Human Peripheral Blood ◽  
Tissue Factor Expression ◽  
Blood Monocytes ◽  
Peripheral Blood Monocytes ◽  
Factor Expression

scholarly journals Evidence for specific annexin I-binding proteins on human monocytes

1996 ◽  
Vol 316 (2) ◽  
pp. 593-597 ◽  
Author(s):  
Nicolas J. GOULDING ◽  
L PAN ◽  
Kathleen WARDWELL ◽  
Veronica C. GUYRE ◽  
Paul M. GUYRE
Keyword(s):  
Monoclonal Antibody ◽  
Peripheral Blood ◽  
Binding Proteins ◽  
Human Peripheral Blood ◽  
Flow Cytometric Analysis ◽  
Blood Monocytes ◽  
Surface Binding ◽  
Peripheral Blood Monocytes ◽  
Cell Functions ◽  
Annexin I

Recombinant human annexin I and a monoclonal antibody specific for this protein (mAb 1B) were used to investigate surface binding of this member of the annexin family of proteins to peripheral blood monocytes. Flow cytometric analysis demonstrated trypsin-sensitive, saturable binding of annexin I to human peripheral blood monocytes but not to admixed lymphocytes. A monoclonal antibody that blocks the anti-phospholipase activity of annexin I also blocked its binding to monocytes. These findings suggest the presence of specific binding sites on monocytes. Furthermore, surface iodination, immunoprecipitation and SDS/PAGE analysis were used to identify two annexin I-binding proteins on the surface of monocytes with molecular masses of 15 kDa and 18 kDa respectively. The identification and characterization of these annexin I-binding molecules should help us to better understand the specific interactions of annexin I with monocytes that lead to down-regulation of pro-inflammatory cell functions.

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