Glyceraldehyde-3-Phosphate Dehydrogenase Binds to the Cytoplasmic Domain of Intercellular Adhesion Molecule-1

1996 ◽  
pp. 293-297
Author(s):  
Christian Fédérici ◽  
Luc Camoin ◽  
Maurice Hattab ◽  
Donny Strosberg ◽  
Pierre-Olivier Couraud
Keyword(s):  
Adhesion Molecule ◽  
Cytoplasmic Domain ◽  
Intercellular Adhesion ◽  
Intercellular Adhesion Molecule ◽  
Intercellular Adhesion Molecule 1

scholarly journals The cytoplasmic domain of the integrin lymphocyte function-associated antigen 1 beta subunit: sites required for binding to intercellular adhesion molecule 1 and the phorbol ester-stimulated phosphorylation site.

1991 ◽  
Vol 174 (5) ◽  
pp. 1227-1238 ◽  
Author(s):  
M L Hibbs ◽  
S Jakes ◽  
S A Stacker ◽  
R W Wallace ◽  
T A Springer
Keyword(s):  
Amino Acids ◽  
Phorbol Ester ◽  
Adhesion Molecule ◽  
Phosphorylation Site ◽  
Cytoplasmic Domain ◽  
Intercellular Adhesion ◽  
Serine Phosphorylation ◽  
Intercellular Adhesion Molecule ◽  
Lymphocyte Function ◽  
Intercellular Adhesion Molecule 1

We have defined the regions of the cytoplasmic domain of the leukocyte integrin lymphocyte function-associated antigen 1 (LFA-1) that are required for active binding of its extracellular domain to intercellular adhesion molecule 1 (ICAM-1). The NH2-terminal 28 amino acids in the cytoplasmic domain are dispensable, but a segment of 5 amino acids including three contiguous threonines (758-760) and Phe 766 in the COOH-terminal third of the cytoplasmic domain are required for binding to ICAM-1. Mutation and phosphoamino acid analysis show that Ser 756 is the major residue phosphorylated in response to phorbol ester. Furthermore, multiple mutations demonstrate that serine phosphorylation can be dissociated from phorbol ester-stimulated binding of LFA-1 to ICAM-1. The sites we have defined are previously unremarked, are well conserved in the beta 1, beta 3, and beta 7 integrin subunits, and may be of broad importance in regulating adhesiveness of integrins.

Control of islet intercellular adhesion molecule-1 expression by interferon-alpha and hypoxia

Diabetes ◽  
1996 ◽  
Vol 45 (10) ◽  
pp. 1336-1343 ◽  
Author(s):  
D. Chakrabarti ◽  
X. Huang ◽  
J. Beck ◽  
J. Henrich ◽  
N. McFarland ◽  
...  
Keyword(s):  
Interferon Alpha ◽  
Adhesion Molecule ◽  
Intercellular Adhesion ◽  
Intercellular Adhesion Molecule ◽  
Intercellular Adhesion Molecule 1

Piperine from Black Pepper Decreased the Expression of Intercellular Adhesion Molecule-1 in Macrophages

2020 ◽  
Vol 19 ◽  
Author(s):  
Nasser Gholijani ◽  
Esmaeil Hashemi ◽  
Zahra Amirghofran
Keyword(s):  
Flow Cytometry ◽  
Adhesion Molecule ◽  
Macrophage Polarization ◽  
Geometric Mean ◽  
Black Pepper ◽  
Intercellular Adhesion ◽  
Intercellular Adhesion Molecule ◽  
Intercellular Adhesion Molecule 1 ◽  
Therapeutic Benefits ◽  
Relative Fold Change

Background: Macrophages are the main players involved in inflammation. Intercellular adhesion molecule-1 (ICAM-1) facilitates macrophage polarization prior to extravasation into inflamed tissue. Piperine a natural product derived from black pepper possess useful biological and pharmacological activities. In current study, the possible anti-inflammatory effect of piperine on the expression of ICAM-1 on J774.1 murine macrophage cell line was investigated. Methods: Lipopolysaccharide (LPS)-stimulated J774.1 cells were cultured in the presence of different concentrations of piperine to examine the changes in ICAM-1 expression by real-time PCR and flow cytometry. Results: We found that piperine decreased ICAM-1 gene expression level from 2.4 ± 0.25 RFC (relative fold change) in LPS-only treated cells to 0.85 ± 0.525 RFC at 1μg/ml (p<0.05), 0.43 ± 0.27 RFC at 10μg/ml (p<0.01), and 0.26 ± 0.25 RFC at 20μg/ml (p<0.01). In flow cytometry, piperine at all concentrations significantly decreased ICAM-1 surface expressions (P<0.05). The geometric mean fluorescence intensity (g-MFI) in LPS-only treated cells (792 ± 57.3) decreased to 482±70 gMFI at 20 µg/ml piperine. Conclusion: According to the results of this study, by decreasing the expression of ICAM-1, piperine is suggested as a candidate to reduce inflammation and has the potential for therapeutic benefits for immune-mediated diseases.

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