scholarly journals Erratum: Corrigendum: Irisin promotes osteoblast proliferation and differentiation via activating the MAP kinase signaling pathways

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Xiaoyong Qiao ◽  
Ying Nie ◽  
Yaxian Ma ◽  
Yan Chen ◽  
Ran Cheng ◽  
...  
Keyword(s):  
Map Kinase ◽  
Signaling Pathways ◽  
Kinase Signaling ◽  
Osteoblast Proliferation ◽  
Proliferation And Differentiation ◽  
Map Kinase Signaling

scholarly journals Irisin promotes osteoblast proliferation and differentiation via activating the MAP kinase signaling pathways

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Xiaoyong Qiao ◽  
Ying Nie ◽  
Yaxian Ma ◽  
Yan Chen ◽  
Ran Cheng ◽  
...  
Keyword(s):  
Map Kinase ◽  
P38 Mapk ◽  
Calcium Deposition ◽  
Kinase Signaling ◽  
Osteoblast Proliferation ◽  
Skeletal Health ◽  
Alp Activity ◽  
Proliferation And Differentiation ◽  
Map Kinase Signaling

Abstract Physical exercise is able to improve skeletal health. However, the mechanisms are poorly known. Irisin, a novel exercise-induced myokine, secreted by skeletal muscle in response to exercise, have been shown to mediate beneficial effects of exercise in many disorders. In the current study, we demonstrated that irisin promotes osteoblast proliferation and increases the expression of osteoblastic transcription regulators, such as Runt-related transcription factor-2, osterix/sp7; and osteoblast differentiation markers, including alkaline phosphatase, collagen type 1 alpha-1, osteocalcin and osteopontin in vitro. Irisin also increase ALP activity and calcium deposition in cultured osteoblast. These osteogenic effects were mediated by activating the p38 mitogen-activated protein kinase (p-p38 MAPK) and extracellular signal-regulated kinase (ERK). Inhibition of p38 MAPK by SB203580 or pERK by U0126 abolished the proliferation and up-regulatory effects of irisin on Runx2 expression and ALP activity. Together our observation suggest that irisin directly targets osteoblast, promoting osteoblast proliferation and differentiation via activating P38/ERK MAP kinase signaling cascades in vitro. Whether irisin can be utilized as the therapeutic agents for osteopenia and osteoporosis is worth to be further pursued

Modification of glucocorticoid sensitivity by MAP kinase signaling pathways in glucocorticoid-induced T-cell apoptosis

2006 ◽  
Vol 34 (11) ◽  
pp. 1542-1552 ◽  
Author(s):  
Tomoko Tanaka ◽  
Taijiro Okabe ◽  
Shigeki Gondo ◽  
Mitsue Fukuda ◽  
Masahiro Yamamoto ◽  
...  
Keyword(s):  
T Cell ◽  
Map Kinase ◽  
Signaling Pathways ◽  
Cell Apoptosis ◽  
Kinase Signaling ◽  
Glucocorticoid Sensitivity ◽  
T Cell Apoptosis ◽  
Map Kinase Signaling

Control of the eukaryotic cell cycle by MAP kinase signaling pathways

2000 ◽  
Vol 14 (14) ◽  
pp. 2147-2157 ◽  
Author(s):  
Marc G. Wilkinson ◽  
Jonathan B. A. Millar
Keyword(s):  
Cell Cycle ◽  
Map Kinase ◽  
Signaling Pathways ◽  
Eukaryotic Cell ◽  
Kinase Signaling ◽  
Map Kinase Signaling

Mechanical strain regulates syndecan-4 expression and shedding in smooth muscle cells through differential activation of MAP kinase signaling pathways

2007 ◽  
Vol 292 (1) ◽  
pp. C517-C525 ◽  
Author(s):  
Matheau A. Julien ◽  
Peiyi Wang ◽  
Carolyn A. Haller ◽  
Jing Wen ◽  
Elliot L. Chaikof
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Map Kinase ◽  
Signaling Pathways ◽  
Map Kinases ◽  
Muscle Cells ◽  
Kinase Signaling ◽  
Fold Reduction ◽  
Map Kinase Signaling

Syndecan-4 (S4) belongs to a family of transmembrane proteoglycans, acts as a coreceptor for growth factor binding as well as cell-matrix and cell-cell interactions, and is induced in neointimal smooth muscle cells (SMCs) after balloon catheter injury. We investigated S4 expression in SMCs in response to several force profiles and the role of MAP kinase signaling pathways in regulating these responses. S4 mRNA expression increased in response to 5% and 10% cyclic strain (4 h: 200 ± 34% and 182 ± 17%, respectively; P < 0.05) before returning to basal levels by 24 h. Notably, the SMC mechanosensor mechanism was reset after an initial 24-h “preconditioning” period, as evident by an increase in S4 gene expression following a change in cyclic stress from 10% to 20% (28 h: 181 ± 1%; P < 0.05). Mechanical stress induced a late decrease in cell-associated S4 protein levels (24 h: 70 ± 6%; P < 0.05), with an associated increase in S4 shedding (24 h: 537 ± 109%; P < 0.05). To examine the role of MAP kinases, cells were treated with U-0126 (ERK1/2 inhibitor), SB-203580 (p38 inhibitor), or JNKI I (JNK/SAPK inhibitor). Late reduction in cell-associated S4 levels was attributed to ERK1/2 and p38 signaling. In contrast, accelerated S4 shedding required both ERK1/2 (5-fold reduction in accelerated shedding; P < 0.05) and JNK/SAPK (4-fold reduction; P < 0.05) signaling. Given the varied functions of S4, stress-induced effects on SMC S4 expression and shedding may represent an additional component of the proinflammatory, growth-stimulating pathways that are activated in response to changes in the mechanical microenvironment of the vascular wall.

Activated glia induce neuron death via MAP kinase signaling pathways involving JNK and p38

Glia ◽  
2004 ◽  
Vol 45 (2) ◽  
pp. 170-179 ◽  
Author(s):  
Zhong Xie ◽  
Carolyn J. Smith ◽  
Linda J. Van Eldik
Keyword(s):  
Map Kinase ◽  
Signaling Pathways ◽  
Kinase Signaling ◽  
Neuron Death ◽  
Map Kinase Signaling

Mitogen-activated protein kinase activation and regulation in the pressure-loaded fetal ovine heart

2006 ◽  
Vol 290 (4) ◽  
pp. H1587-H1595 ◽  
Author(s):  
Aaron K. Olson ◽  
Kristin N. Protheroe ◽  
Jeffrey L. Segar ◽  
Thomas D. Scholz
Keyword(s):  
Map Kinase ◽  
Signaling Pathways ◽  
Fetal Heart ◽  
Left Ventricular ◽  
Heart Weight ◽  
Kinase Signaling ◽  
Protein Levels ◽  
Pressure Load ◽  
Map Kinase Signaling ◽  
Mitogen Activated Protein

The mitogen-activated protein (MAP) kinase signaling pathways help to mediate the hypertrophic response of the pressure-loaded adult heart, although their importance in fetal myocardium is less known. The goal of this study was to determine the role the MAP kinase signaling pathways play in regulating the response of the fetal heart to a pressure load. Aortic (Ao) and pulmonary artery (PA) bands were placed in 132-day fetal sheep for 7 days. Protein levels of the total and active (phosphorylated) terminal MAP kinases extracellular signal-regulated kinase (ERK/P-ERK), c-Jun NH2-terminal kinase (JNK/P-JNK), and p38/P-p38 and the MAP kinase phosphatases MKP-1, MKP-2, and MKP-3 were made in the right and left ventricular (RV and LV) free walls. In both Ao- and PA-banded animals, total heart weight normalized to body weight was significantly increased, largely due to an increase in RV free wall mass in the Ao-banded animals and an increase in septal mass in the PA-banded fetuses. Total protein levels of the three terminal kinases and of P-ERK and P-JNK remained stable in both groups of banded animals. However, P-p38 was significantly increased in RV and LV of Ao- and PA-banded fetuses. Whereas MKP-1 and MKP-2 protein levels were unchanged following Ao- and PA-banding, MKP-3 protein levels were significantly increased in the RV of the PA-banded animals. These findings indicate that the MAP kinase signaling pathways are active in the fetal heart and help to modulate the response of prenatal myocardium to a pressure load.

Sign in / Sign up

Export Citation Format

Share Document