Cell surface protease activity of human lymphocytes; its inhibition by α 1-antitrypsin

1981 ◽  
Vol 37 (5) ◽  
pp. 518-519 ◽  
Author(s):  
J. Bata ◽  
J. P. Martin ◽  
J. P. Revillard
Keyword(s):  
Cell Surface ◽  
Protease Activity ◽  
Human Lymphocytes ◽  
Cell Surface Protease

Effect of UV irradiation on cell surface protease activity and amino acid uptake

1998 ◽  
Vol 422 (1) ◽  
pp. 55-67 ◽  
Author(s):  
Terrence J. Piva ◽  
Kari G. Francis ◽  
Darren R. Krause ◽  
Grace M. Chojnowski ◽  
Kay A.O. Ellem
Keyword(s):  
Amino Acid ◽  
Cell Surface ◽  
Uv Irradiation ◽  
Protease Activity ◽  
Amino Acid Uptake ◽  
Acid Uptake ◽  
Cell Surface Protease

Degradation of Insulin by Isolated Mouse Pancreatic Acini: Evidence for Cell Surface Protease Activity

Diabetes ◽  
1984 ◽  
Vol 33 (1) ◽  
pp. 64-72 ◽  
Author(s):  
I. D. Goldfine ◽  
J. A. Williams ◽  
A. C. Bailey ◽  
K. Y. Wong ◽  
Y. Iwamoto ◽  
...  
Keyword(s):  
Cell Surface ◽  
Protease Activity ◽  
Pancreatic Acini ◽  
Cell Surface Protease

Degradation of insulin by isolated mouse pancreatic acini. Evidence for cell surface protease activity

Diabetes ◽  
1984 ◽  
Vol 33 (1) ◽  
pp. 64-72 ◽  
Author(s):  
I. D. Goldfine ◽  
J. A. Williams ◽  
A. C. Bailey ◽  
K. Y. Wong ◽  
Y. Iwamoto ◽  
...  
Keyword(s):  
Cell Surface ◽  
Protease Activity ◽  
Pancreatic Acini ◽  
Cell Surface Protease

Increased cell surface protease activity in UV-irradiated cells undergoing apoptosis

Redox Report ◽  
2000 ◽  
Vol 5 (2-3) ◽  
pp. 133-136
Author(s):  
T.J. Piva ◽  
C.M. Davern ◽  
C.M. Winterford ◽  
K.A.O. Ellem
Keyword(s):  
Cell Surface ◽  
Protease Activity ◽  
Cell Surface Protease

Relationship between cell surface protease activity and doubling time in various normal and transformed cells

1976 ◽  
Vol 451 (2) ◽  
pp. 499-510 ◽  
Author(s):  
Victor B. Hatcher ◽  
Michael S. Wertheim ◽  
Choo Y. Rhee ◽  
Grace Tsien ◽  
Peter G. Burk
Keyword(s):  
Cell Surface ◽  
Protease Activity ◽  
Doubling Time ◽  
Transformed Cells ◽  
Cell Surface Protease

EFFECT OF UV-INDUCED APOPTOSIS ON HeLa CELL SURFACE PROTEASE ACTIVITY

1996 ◽  
Vol 24 (4) ◽  
pp. 560S-560S
Author(s):  
T.J. Piva ◽  
D.R. Krause ◽  
G.M. Chojnowski ◽  
K.A.O. Ellem
Keyword(s):  
Cell Surface ◽  
Hela Cell ◽  
Protease Activity ◽  
Induced Apoptosis ◽  
Cell Surface Protease

Surface morphology and agglutination of lectin-treated human lymphocytes and lymphoblasts

1976 ◽  
Vol 21 (3) ◽  
pp. 563-578
Author(s):  
J.H. Temmink ◽  
J.G. Collard ◽  
J. Roosien ◽  
J.F. Van den Bosch
Keyword(s):  
Cell Surface ◽  
Surface Morphology ◽  
Human Lymphocytes ◽  
Cell Type ◽  
A Cell ◽  
Human Peripheral Lymphocytes ◽  
Normal Human ◽  
Altered Cell ◽  
Induced Changes ◽  
Cell Surface Morphology

Two human lymphoblasts (Raji and EB3) and normal human peripheral lymphocytes were exposed to different concentrations of Concanavalin A and wheat germ agglutinin. The lectin-induced agglutination was determined and correlated with lectin-induced changes in the surface morphology of these cells as studied in a scanning electron microscope. Whenever the lectin induced high agglutinability in a cell type, it also invariably had a smoothing effect on the cell surface. In contrast, when cells did not agglutinate well with a certain lectin, their cell surface remained essentially rough (villous) after addition of the lectin. The correlation found between increased agglutinability and altered cell surface morphology upon treatment with certain lectins suggests that both phenomena result from one and the same process. Additional evidence for this postulate is presented.

scholarly journals β-blockers Reverse Agonist-Induced β2-AR Downregulation Regardless of Their Signaling Profile

2020 ◽  
Vol 21 (2) ◽  
pp. 512
Author(s):  
Sonia Maccari ◽  
Vanessa Vezzi ◽  
Federica Barbagallo ◽  
Tonino Stati ◽  
Barbara Ascione ◽  
...  
Keyword(s):  
Cell Surface ◽  
Human Lymphocytes ◽  
Cell Types ◽  
Hek293 Cells ◽  
Enzyme Linked Immunosorbent Assay ◽  
Mrna Levels ◽  
Receptor Density ◽  
Biased Agonism ◽  
Β Blocker ◽  
Β Blockers

Altered β-adrenergic receptor (β-AR) density has been reported in cells, animals, and humans receiving β-blocker treatment. In some cases, β-AR density is upregulated, but in others, it is unaffected or even reduced. Collectively, these results would imply that changes in β-AR density and β-blockade are not related. However, it has still not been clarified whether the effects of β-blockers on receptor density are related to their ability to activate different β-AR signaling pathways. To this aim, five clinically relevant β-blockers endowed with inverse, partial or biased agonism at the β2-AR were evaluated for their effects on β2-AR density in both human embryonic kidney 293 (HEK293) cells expressing exogenous FLAG-tagged human β2-ARs and human lymphocytes expressing endogenous β2-ARs. Cell surface β2-AR density was measured by enzyme-linked immunosorbent assay (ELISA) and flow cytometry. Treatment with propranolol, carvedilol, pindolol, sotalol, or timolol did not induce any significant change in surface β2-AR density in both HEK293 cells and human lymphocytes. On the contrary, treatment with the β-AR agonist isoproterenol reduced the number of cell surface β2-ARs in the tested cell types without affecting β2-AR-mRNA levels. Isoproterenol-induced effects on receptor density were completely antagonized by β-blocker treatment. In conclusion, the agonistic activity of β-blockers does not exert an important effect on short-term regulation of β2-AR density.

Sign in / Sign up

Export Citation Format

Share Document