scholarly journals Does caveolin‐1 knockout affect matrix metalloproteinase‐2 activity and contractile function in the isolated working mouse heart?

2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
Ava Kalyca Chow ◽  
Edwin Daniel ◽  
Richard Schulz
Keyword(s):  
Matrix Metalloproteinase ◽  
Contractile Function ◽  
Matrix Metalloproteinase 2 ◽  
Mouse Heart ◽  
Caveolin 1

Caveolin-1 inhibits matrix metalloproteinase-2 activity in the heart

2007 ◽  
Vol 42 (4) ◽  
pp. 896-901 ◽  
Author(s):  
A.K. Chow ◽  
J. Cena ◽  
A.F. El-Yazbi ◽  
B.D. Crawford ◽  
A. Holt ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Matrix Metalloproteinase 2 ◽  
Caveolin 1

scholarly journals Intracellular Regulation of Matrix Metalloproteinase-2 Activity: New Strategies in Treatment and Protection of Heart Subjected to Oxidative Stress

Scientifica ◽  
2013 ◽  
Vol 2013 ◽  
pp. 1-12 ◽  
Author(s):  
Grzegorz Sawicki
Keyword(s):  
Matrix Metalloproteinase ◽  
Molecular Mechanisms ◽  
Troponin I ◽  
Contractile Function ◽  
Ischemia Reperfusion ◽  
Matrix Metalloproteinase 2 ◽  
Acid Oxidation ◽  
Intracellular Regulation ◽  
Heart Injury ◽  
New Strategies

Much is known regarding cardiac energy metabolism in ischemia/reperfusion (I/R) injury. Under aerobic conditions, the heart prefers to metabolize fatty acids, which contribute to 60–80% of the required ATP. During ischemia, anaerobic glycolysis increases and becomes an important source of ATP for preservation of ion gradients. With reperfusion, fatty acid oxidation quickly recovers and again predominates as the major source of mitochondrial oxidative metabolism. Although a number of molecular mechanisms have been implicated in the development of I/R injury, their relative contributions remain to be determined. One such mechanism involves the proteolytic degradation of contractile proteins, such as troponin I (TnI), myosin heavy chain, titin, and the myosin light chains (MLC1 and MLC2) by matrix metalloproteinase-2 (MMP-2). However, very little is known about intracellular regulation of MMP-2 activity under physiological and pathological conditions. Greater understanding of the mechanisms that govern MMP-2 activity may lead to the development of new therapeutic strategies aimed at preservation of the contractile function of the heart subjected to myocardial infarction (MI) or I/R. This review discusses the intracellular mechanisms controlling MMP-2 activity and highlights a new intracellular therapeutic direction for the prevention and treatment of heart injury.

scholarly journals Electroacupuncture Exerts Neuroprotection through Caveolin-1 Mediated Molecular Pathway in Intracerebral Hemorrhage of Rats

2016 ◽  
Vol 2016 ◽  
pp. 1-8 ◽  
Author(s):  
Hui-Qin Li ◽  
Yan Li ◽  
Zi-Xian Chen ◽  
Xiao-Guang Zhang ◽  
Xia-wei Zheng ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Blood Brain Barrier ◽  
Neurological Deficit ◽  
Brain Barrier ◽  
Matrix Metalloproteinase 2 ◽  
Barrier Permeability ◽  
Blood Brain Barrier Permeability ◽  
Caveolin 1 ◽  
Blood Brain ◽  
Brain Barrier Permeability

Spontaneous intracerebral hemorrhage (ICH) is one of the most devastating types of stroke. Here, we aim to demonstrate that electroacupuncture on Baihui (GV20) exerts neuroprotection for acute ICH possibly via the caveolin-1/matrix metalloproteinase/blood-brain barrier permeability pathway. The model of ICH was established by using collagenase VII. Rats were randomly divided into three groups: Sham-operation group, Sham electroacupuncture group, and electroacupuncture group. Each group was further divided into 4 subgroups according to the time points of 6 h, 1 d, 3 d, and 7 d after ICH. The methods were used including examination of neurological deficit scores according to Longa’s scale, measurement of blood-brain barrier permeability through Evans Blue content,in situimmunofluorescent detection of caveolin-1 in brains, western blot analysis of caveolin-1 in brains, andin situzymography for measuring matrix metalloproteinase-2/9 activity in brains. Compared with Sham electroacupuncture group, electroacupuncture group has resulted in a significant improvement in neurological deficit scores and in a reduction in Evans Blue content, expression of caveolin-1, and activity of matrix metalloproteinase-2/9 at 6 h, 1 d, 3 d, and 7 d after ICH (P<0.05). In conclusion, the present results suggested that electroacupuncture on GV20 can improve neurological deficit scores and reduce blood-brain barrier permeability after ICH, and the mechanism possibly targets caveolin-1/matrix metalloproteinase/blood-brain barrier permeability pathway.

scholarly journals Hyperosmolarity Impairs Human Extravillous Trophoblast Differentiation by Caveolae Internalization

2021 ◽  
Vol 12 ◽  
Author(s):  
Julieta Reppetti ◽  
Yollyseth Medina ◽  
Mariana Farina ◽  
Alicia E. Damiano ◽  
Nora Alicia Martínez
Keyword(s):  
Cell Migration ◽  
Matrix Metalloproteinase ◽  
Cell Line ◽  
Cell Invasion ◽  
Extravillous Trophoblast ◽  
Matrix Metalloproteinase 2 ◽  
Protein Abundance ◽  
Trophoblast Differentiation ◽  
Caveolin 1 ◽  
Normal Differentiation

We recently reported that an intact caveolar structure is necessary for adequate cell migration and tubulogenesis of the human extravillous trophoblast (EVT) cells. Emerging evidence supports that hyperosmolarity induces the internalization of caveolae into the cytoplasm and accelerates their turnover. Furthermore, signaling pathways associated with the regulation of trophoblast differentiation are localized in caveolae. We hypothesized that hyperosmolarity impairs EVT differentiation and caveolae/caveolin−1 (Cav-1) participates in this process. EVT cells (Swan 71 cell line) were cultured in complete Dulbecco’s Modified Eagle Medium/Nutrient Mixture F-12 and exposed to hyperosmolar condition (generated by the addition of 100 mM sucrose). Hyperosmolarity altered the EVT cell migration and the formation of tube-like structures. In addition, cell invasion was decreased along with a reduction in the latent and active forms of matrix metalloproteinase-2 (MMP−2) secreted by these cells. With respect to Cav-1 protein abundance, we found that hyperosmolarity enhanced its degradation by the lysosomal pathway. Accordingly, in the hyperosmolar condition, we also observed a significant increase in the number of vacuoles and the internalization of the caveolae into the cytoplasm. Taken together, our findings suggest that hyperosmolarity may induce caveolae internalization and increase their turnover, compromising the normal differentiation of EVT cells.

WITHDRAWN: Regulation of matrix metalloproteinase-2 in the heart by caveolin-1

2007 ◽  
Author(s):  
A.K. Chow ◽  
J. Cena ◽  
A.F. El-Yazbi ◽  
B.D. Crawford ◽  
A. Holt ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Matrix Metalloproteinase 2 ◽  
Caveolin 1

Regulation of matrix metalloproteinase-2 in the heart by caveolin-1

2007 ◽  
Vol 42 (6) ◽  
pp. S117
Author(s):  
A.K. Chow ◽  
J. Cena ◽  
A.F. El-Yazbi ◽  
B.D. Crawford ◽  
A. Holt ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Matrix Metalloproteinase 2 ◽  
Caveolin 1

Caveolin-1 exists and may function in cardiomyocytes

2010 ◽  
Vol 88 (1) ◽  
pp. 73-76 ◽  
Author(s):  
Woo Jung Cho ◽  
Ava K. Chow ◽  
Richard Schulz ◽  
Edwin E. Daniel
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
Matrix Metalloproteinase ◽  
Cardiac Myocytes ◽  
Ventricular Myocytes ◽  
Matrix Metalloproteinase 2 ◽  
Previous Evidence ◽  
Caveolin 1

Whether ventricular cardiac myocytes of mouse contain caveolin-1 is disputed. It has been claimed to be exclusively in nearby endothelial cell profiles. Recently, matrix metalloproteinase-2 (MMP-2) was reported to be present in mouse ventricular cardiac myocytes, colocalized with caveolin-1, and caveolin-1 knockout was found to cause the loss of MMP-2 from mouse ventricular cardiac myocytes and affect their functioning. To resolve this dispute, we labeled cardiac myocytes with caveolin-1 and endothelial cells with caveolin-2. Caveolin-2 is agreed to be present exclusively in endothelial cells. The results showed that mouse ventricular myocytes were labeled with caveolin-1 antibodies independently of any caveolin-2 labeling, and endothelial cells were labeled with both caveolin-1 and caveolin-2 antibodies. This confirms that caveolin-1 is present in mouse ventricular cardiac myocytes as well as endothelial cells. Previous evidence confirms that loss of caveolin-1 affects the function of mouse ventricular cardiac myocytes and suggests that MMP-2 may be involved.

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