Contribution of technology to human cell properties

2021 ◽  
pp. 1-4
Author(s):  
Carlota Saldanha
Keyword(s):  
Endothelial Cell ◽  
Human Cell ◽  
Binding Sites ◽  
Blood Cells ◽  
Specific Binding ◽  
Vascular Endothelial Cell ◽  
The Other ◽  
Vascular Endothelial ◽  
Specific Binding Sites ◽  
Human Lungs

After explaining the meaning of SARS-CoV2, the protection rules for the disease caused by this virus are described in order to eradicate the resulting pandemic. Methods to differentiate asymptomatic from symptomatic patients will be mentioned. Human lungs, heart, kidney, endothelium and erythrocyte have specific binding sites for the SARS-CoV2. The aim of this opinion was to highlight some new disposable technology to identify two cell properties. One of them is the vascular endothelial cell (EC) receptor binding to the SARS-CoV2 and the other is related with red blood cells (RBCs) as SARS-CoV2 carrier.

Chemoselective cluster labelling of biomolecules

1987 ◽  
Vol 45 ◽  
pp. 760-761
Author(s):  
C. J. Foley ◽  
L. E. Maelia ◽  
J. F. Hainfeld ◽  
J. S. Wall
Keyword(s):  
Binding Sites ◽  
Specific Binding ◽  
Heavy Atom ◽  
The Other ◽  
Biological Structure ◽  
Heavy Atoms ◽  
Specific Binding Sites ◽  
Lower Beam ◽  
High Concentrations ◽  
Beam Dose

The Brookhaven STEM is capable of visualizing single heavy atoms at a beam dose of >103 el/Å2. Heteropolytungstate clusters, including W12PO403, have been found to incorporate several desirable properties as labels for biological specimens. They may be resolved at much lower beam doses due to their high concentrations of multiple heavy atoms and are directly visible labels. A lower beam dose also helps to preserve the biological structure of the specimens. Furthermore, they are extremely stable in the electron beam. Lastly, they are capable of being derivatized as chemoselective reagents for specific binding sites on biomolecules, as in the previously reported undecagold compound.Two new classes of heavy atom labels, one specific for sulfhydryl and the other specific for both amino and sulfhydryl binding sites on proteins, have been synthesized by reactions analogous to those illustrated in Scheme 1.

Vascular endothelial growth factor binds to fibrinogen and fibrin and stimulates endothelial cell proliferation

Blood ◽  
2000 ◽  
Vol 96 (12) ◽  
pp. 3772-3778 ◽  
Author(s):  
Abha Sahni ◽  
Charles W. Francis
Keyword(s):  
Cell Proliferation ◽  
Endothelial Cell ◽  
Growth Factor ◽  
Binding Sites ◽  
Vascular Endothelial Cell ◽  
Endothelial Cell Proliferation ◽  
Scatchard Analysis ◽  
Vascular Endothelial ◽  
Binding Studies ◽  
Binding Ratio

Vascular development and response to injury are regulated by several cytokines and growth factors including the members of the fibroblast growth factor and vascular endothelial cell growth factor (VEGF) families. Fibrinogen and fibrin are also important in these processes and affect many endothelial cell properties. Possible specific interactions between VEGF and fibrinogen that could play a role in coordinating vascular responses to injury are investigated. Binding studies using the 165 amino acid form of VEGF immobilized on Sepharose beads and soluble iodine 125 (125I)–labeled fibrinogen demonstrated saturable and specific binding. Scatchard analysis indicated 2 classes of binding sites with dissociation constants (Kds) of 5.9 and 462 nmol/L. The maximum molar binding ratio of VEGF:fibrinogen was 3.8:1. Further studies characterized binding to fibrin using 125I-labeled VEGF- and Sepharose-immobilized fibrin monomer. These also demonstrated specific and saturable binding with 2 classes of sites havingKds of 0.13 and 97 nmol/L and a molar binding ratio of 3.6:1. Binding to polymerized fibrin demonstrated one binding site with a Kd of 9.3 nmol/L. Binding of VEGF to fibrin(ogen) was independent of FGF-2, indicating that there are distinct binding sites for each angiogenic peptide. VEGF bound to soluble fibrinogen in medium and to surface immobilized fibrinogen or fibrin retained its capacity to support endothelial cell proliferation. VEGF binds specifically and saturably to fibrinogen and fibrin with high affinity, and this may affect the localization and activity of VEGF at sites of tissue injury.

Specific binding sites on human phagocytic blood cells for Gly-Leu-Phe and Val-Glu-Pro-Ile-Pro-Tyr, immunostimulating peptides from human milk proteins

1992 ◽  
Vol 1160 (3) ◽  
pp. 251-261 ◽  
Author(s):  
M'hamed Jaziri ◽  
Danièle Migliore-Samour ◽  
Marie-Rose Casabianca-Pignède ◽  
Karim Keddad ◽  
Jean Louis Morgat ◽  
...  
Keyword(s):  
Human Milk ◽  
Binding Sites ◽  
Blood Cells ◽  
Specific Binding ◽  
Milk Proteins ◽  
Specific Binding Sites

Vascular endothelial growth factor binds to fibrinogen and fibrin and stimulates endothelial cell proliferation

Blood ◽  
2000 ◽  
Vol 96 (12) ◽  
pp. 3772-3778 ◽  
Author(s):  
Abha Sahni ◽  
Charles W. Francis
Keyword(s):  
Cell Proliferation ◽  
Endothelial Cell ◽  
Growth Factor ◽  
Binding Sites ◽  
Vascular Endothelial Cell ◽  
Endothelial Cell Proliferation ◽  
Scatchard Analysis ◽  
Vascular Endothelial ◽  
Binding Studies ◽  
Binding Ratio

Abstract Vascular development and response to injury are regulated by several cytokines and growth factors including the members of the fibroblast growth factor and vascular endothelial cell growth factor (VEGF) families. Fibrinogen and fibrin are also important in these processes and affect many endothelial cell properties. Possible specific interactions between VEGF and fibrinogen that could play a role in coordinating vascular responses to injury are investigated. Binding studies using the 165 amino acid form of VEGF immobilized on Sepharose beads and soluble iodine 125 (125I)–labeled fibrinogen demonstrated saturable and specific binding. Scatchard analysis indicated 2 classes of binding sites with dissociation constants (Kds) of 5.9 and 462 nmol/L. The maximum molar binding ratio of VEGF:fibrinogen was 3.8:1. Further studies characterized binding to fibrin using 125I-labeled VEGF- and Sepharose-immobilized fibrin monomer. These also demonstrated specific and saturable binding with 2 classes of sites havingKds of 0.13 and 97 nmol/L and a molar binding ratio of 3.6:1. Binding to polymerized fibrin demonstrated one binding site with a Kd of 9.3 nmol/L. Binding of VEGF to fibrin(ogen) was independent of FGF-2, indicating that there are distinct binding sites for each angiogenic peptide. VEGF bound to soluble fibrinogen in medium and to surface immobilized fibrinogen or fibrin retained its capacity to support endothelial cell proliferation. VEGF binds specifically and saturably to fibrinogen and fibrin with high affinity, and this may affect the localization and activity of VEGF at sites of tissue injury.

Effect of angiotensin(1-7) on the expression of E-selectin induced by angiotensinII and its mechanism in vascular endothelial cell

2010 ◽  
Vol 34 (8) ◽  
pp. S71-S71
Author(s):  
Xiaohui Shen ◽  
Zhi‑Bin Wen ◽  
Na Li ◽  
Qingmei Cheng ◽  
Xiaofan He ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Vascular Endothelial Cell ◽  
Vascular Endothelial
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