scholarly journals A Novel Netrin-1-Derived Peptide Enhances Protection against Neuronal Death and Mitigates of Intracerebral Hemorrhage in Mice

2021 ◽  
Vol 22 (9) ◽  
pp. 4829
Author(s):  
Lin Liu ◽  
Kai-Jie Liu ◽  
Jian-Bo Cao ◽  
Jing Yang ◽  
Hua-Li Yu ◽  
...  
Keyword(s):  
Intracerebral Hemorrhage ◽  
Focal Adhesion ◽  
Neuronal Death ◽  
Neuroprotective Effect ◽  
Recovery Process ◽  
Functional Domain ◽  
Candidate Peptide ◽  
The Central Nervous System ◽  
Focal Adhesion Kinase Phosphorylation ◽  
Kinase Phosphorylation

It has been reported that Netrin-1 is involved in neuroprotection following injury to the central nervous system. However, the minimal functional domain of Netrin-1 which can preserve the neuroprotection but avoid the major side effects of Netrin remains elusive. Here, we investigated the neuroprotective effect of a peptide E1 derived from Netrin-1′s EGF3 domain (residues 407–422). We found that it interacts with deleted colorectal carcinoma (DCC) to activate focal adhesion kinase phosphorylation exhibiting neuroprotection. The administration of the peptide E1 was able to improve functional recovery through reduced apoptosis in an experimental murine model of intracerebral hemorrhage (ICH). In summary, we reveal a functional sequence of Netrin-1 that is involved in the recovery process after ICH and identify a candidate peptide for the treatment of ICH.

scholarly journals Evaluation of the Correlation between Focal Adhesion Kinase Phosphorylation and Cell Adhesion Force Using “DEP” Technology

Sensors ◽  
2012 ◽  
Vol 12 (5) ◽  
pp. 5951-5965 ◽  
Author(s):  
Chyung Ay ◽  
Chih-Chang Yeh ◽  
Min-Chih Hsu ◽  
Huaang-Youh Hurng ◽  
Philip Chi Lip Kwok ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Adhesion Force ◽  
Focal Adhesion Kinase Phosphorylation ◽  
Kinase Phosphorylation

scholarly journals Multiplexed High Content Screening Reveals That Cigarette Smoke Condensate-Altered Cell Signaling Pathways Are Accentuated Through FAK Inhibition in Human Bronchial Cells

2012 ◽  
Vol 31 (3) ◽  
pp. 257-266 ◽  
Author(s):  
Charleata A. Carter
Keyword(s):  
Focal Adhesion Kinase ◽  
Cigarette Smoke ◽  
Focal Adhesion ◽  
Cell Number ◽  
Cell Periphery ◽  
Cigarette Smoke Condensate ◽  
Mitogen Activated Protein ◽  
Focal Adhesion Kinase Phosphorylation ◽  
Altered Cell ◽  
Kinase Phosphorylation

The mechanisms by which cigarette smoke condensate (CSC) disrupts F-actin and decreases cell motility in human bronchial (BEAS-2B) cells were assessed. The hypothesis that CSC activated focal adhesion kinase (FAK), mitogen-activated protein kinases (MAPKs), and paxillin in BEAS-2B cells was tested. When BEAS-2B cells were treated with 20 to 100 μg/mL CSC for 1 hour, FAK increased. The CSC caused F-actin disruption, while FAK inhibition alone caused actin aggregates to collapse to the cell periphery, but FAK inhibition combined with CSC caused actin aggregates to distribute throughout the cells. The CSC treatment of BEAS-2B cells showed a dose-dependent increase in the activation of the MAPKs, c-Jun, JNK, ERK, p38, and heat shock protein 27 (Hsp27) and paxillin. Focal adhesion kinase phosphorylation inhibition combined with CSC treatment increased p38 and ERK at 1 hour and 24 hours along with decreased cell number and motility compared with CSC treatment alone. CSC exerts changes in BEAS-2B cells by altering morphology and activating MAPK pathways.

scholarly journals Monitoring focal adhesion kinase phosphorylation dynamics in live cells

The Analyst ◽  
2017 ◽  
Vol 142 (15) ◽  
pp. 2713-2716 ◽  
Author(s):  
Nur P. Damayanti ◽  
Kevin Buno ◽  
Nagarajan Narayanan ◽  
Sherry L. Voytik Harbin ◽  
Meng Deng ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Focal Adhesion Kinase ◽  
Real Time ◽  
Focal Adhesion ◽  
Receptor Tyrosine Kinase ◽  
Live Cells ◽  
Real Time Monitoring ◽  
Cellular Functions ◽  
Focal Adhesion Kinase Phosphorylation ◽  
Kinase Phosphorylation

Focal adhesion kinase (FAK) is a cytoplasmic non-receptor tyrosine kinase essential for a diverse set of cellular functions. FAK FLIM-peptide biosensor enables real-time monitoring of FAK phopshorylation activity.

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