scholarly journals Naturally Occurring Sclareol Diterpene Augments the Chemosensitivity of Human Hela Cervical Cancer Cells by Inducing Mitochondrial Mediated Programmed Cell Death, S-Phase Cell Cycle Arrest and Targeting Mitogen-Activated Protein Kinase (MAPK)/Extracellular-Signal-Regulated Kinase (ERK) Signaling Pathway

2020 ◽  
Vol 26 ◽  
Author(s):  
Wang Li ◽  
Zhou Ping ◽  
Gao Xuemei ◽  
Luo Minglian ◽  
Meng Hongjuan ◽  
...  
Keyword(s):  
S Phase ◽  
Mitogen Activated Protein Kinase ◽  
Erk Signaling ◽  
Phase Cell ◽  
Extracellular Signal Regulated Kinase ◽  
Cycle Arrest ◽  
Naturally Occurring ◽  
Extracellular Signal ◽  
Mitogen Activated Protein ◽  
Cervical Cancer Cells

scholarly journals PERAN LATIHAN FISIK DALAM PENANGANAN OBESITAS: AKSI IRISIN PADA PROSES PENCOKELATAN

2021 ◽  
Vol 3 (1) ◽  
pp. 27
Author(s):  
Dewi Irawati Soeria Santoso ◽  
Imelda Rosalyn Sianipar ◽  
Neng Tine Kartinah
Keyword(s):  
Treatment Approach ◽  
Public Health Problem ◽  
Mitogen Activated Protein Kinase ◽  
Erk Signaling ◽  
Brown Adipocyte ◽  
White Adipocyte ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
Mitogen Activated Protein ◽  
Prevalence Of Obesity

In recent years, the prevalence of obesity continues to increase, leading to a public health problem. Therefore, the obesity problem needs serious attention and treatment approaches. Exercise is one of the treatment approach to combat obesity because exercise plays a role in beiging/browning process. Beiging is a differentiation process from white adipocyte to beige adipocyte, which has similar characteristics to brown adipocyte and is marked with an increase of UCP-1 expression. Irisin plays a role in increasing UCP-1 expression by activating p38 mitogen-activated protein kinase (MAPK) and extracellular-signal regulated kinase (ERK) signaling. Muscle contraction during exercise can activate PGC-1α, which leads to the synthesis of irisin. Exercise may increase irisin levels in skeletal muscle and consequently, play as a mediator of beiging process in adipose tissue.

Delivery of Sorafenib and Metformin Against Hepatocellular Carcinoma with Amphiphilic Polypeptide-based Micelles

2021 ◽  
Author(s):  
Lanqing Cao ◽  
Guangmeng Xu ◽  
Hongyu He ◽  
Jiannan Li
Keyword(s):  
Mapk Pathway ◽  
Synergistic Effects ◽  
Mitogen Activated Protein Kinase ◽  
High Recurrence Rate ◽  
Extracellular Signal Regulated Kinase ◽  
Cycle Arrest ◽  
Extracellular Signal ◽  
Mitogen Activated Protein ◽  
Poly Ethylene

Abstract Hepatoma is a common clinical disease with poor prognosis and a high recurrence rate. Chemotherapy is important for hepatoma treatment because only a small amount of hepatoma patients are suitable for local resection, and the effects of transarterial chemoembolization (TACE) are unsatisfactory. But many limitations restrict further application of chemotherapy. In this study, sorafenib (Sor) and metformin (Met) co-loaded poly(ethylene glycol)-block-poly(L-glutamic acid-co-L-phenylalanine) (mPEG-b-P(Glu-co-Phe)) micelles were developed. Sor is a common molecular target agent which can inhibit the mitogen-activated protein kinase (MAPK) pathway to treat hepatoma clinically. Met can also regulate the MAPK pathway and inhibit the expression of the phosphorylated extracellular signal-regulated kinase (p-ERK). Moreover, both Sor and Met play important roles in cell cycle arrest. The integration of these two drugs aims to achieve synergistic effects against hepatoma. The micelles can be targeted to cancer cells and possess longer blood circulation time. The two agents can be released rapidly in the tumor sites. Both orthotopic and patient-derived xenograft (PDX) hepatoma models were developed to analyze the treatment efficacy of the Sor and Met loaded micelles. The in vivo study showed that the micelles can prevent hepatoma progression by inhibiting the expressions of p-ERK and cyclin D1. This study indicated that the Sor/Met-loaded micelles are suitable for hepatoma treatment.

scholarly journals Extracellular Signal-regulated Kinase Regulates Clathrin-independent Endosomal Trafficking

2006 ◽  
Vol 17 (2) ◽  
pp. 645-657 ◽  
Author(s):  
Sarah E. Robertson ◽  
Subba Rao Gangi Setty ◽  
Anand Sitaram ◽  
Michael S. Marks ◽  
Robert E. Lewis ◽  
...  
Keyword(s):  
Surface Expression ◽  
Mek Inhibitor ◽  
Endocytic Pathway ◽  
Mitogen Activated Protein Kinase ◽  
Erk Signaling ◽  
Endosomal Trafficking ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
Kinase Suppressor Of Ras ◽  
Mitogen Activated Protein

Extracellular signal-regulated kinase (Erk) is widely recognized for its central role in cell proliferation and motility. Although previous work has shown that Erk is localized at endosomal compartments, no role for Erk in regulating endosomal trafficking has been demonstrated. Here, we report that Erk signaling regulates trafficking through the clathrin-independent, ADP-ribosylation factor 6 (Arf6) GTPase-regulated endosomal pathway. Inactivation of Erk induced by a variety of methods leads to a dramatic expansion of the Arf6 endosomal recycling compartment, and intracellular accumulation of cargo, such as class I major histocompatibility complex, within the expanded endosome. Treatment of cells with the mitogen-activated protein kinase kinase (MEK) inhibitor U0126 reduces surface expression of MHCI without affecting its rate of endocytosis, suggesting that inactivation of Erk perturbs recycling. Furthermore, under conditions where Erk activity is inhibited, a large cohort of Erk, MEK, and the Erk scaffold kinase suppressor of Ras 1 accumulates at the Arf6 recycling compartment. The requirement for Erk was highly specific for this endocytic pathway, because its inhibition had no effect on trafficking of cargo of the classical clathrin-dependent pathway. These studies reveal a previously unappreciated link of Erk signaling to organelle dynamics and endosomal trafficking.

scholarly journals Extracellular Signal-Regulated Kinase Promotes Rho-Dependent Focal Adhesion Formation by Suppressing p190A RhoGAP

2010 ◽  
Vol 30 (13) ◽  
pp. 3233-3248 ◽  
Author(s):  
Ashok K. Pullikuth ◽  
Andrew D. Catling
Keyword(s):  
Adhesion Formation ◽  
Rho Kinase ◽  
Focal Adhesions ◽  
Mitogen Activated Protein Kinase ◽  
Erk Signaling ◽  
Extracellular Signal Regulated Kinase ◽  
Erk Phosphorylation ◽  
C Terminus ◽  
Extracellular Signal ◽  
Mitogen Activated Protein

ABSTRACT Cell migration is critical for normal development and for pathological processes including cancer cell metastasis. Dynamic remodeling of focal adhesions and the actin cytoskeleton are crucial determinants of cell motility. The Rho family and the mitogen-activated protein kinase (MAPK) module consisting of MEK-extracellular signal-regulated kinase (ERK) are important regulators of these processes, but mechanisms for the integration of these signals during spreading and motility are incompletely understood. Here we show that ERK activity is required for fibronectin-stimulated Rho-GTP loading, Rho-kinase function, and the maturation of focal adhesions in spreading cells. We identify p190A RhoGAP as a major target for ERK signaling in adhesion assembly and identify roles for ERK phosphorylation of the C terminus in p190A localization and activity. These observations reveal a novel role for ERK signaling in adhesion assembly in addition to its established role in adhesion disassembly.

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