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147 results on '"Trache, Andreea"'

9. Endothelial NCK2 promotes atherosclerosis progression in male but not female Nck1-null atheroprone mice

Author

Bywaters, Briana C., Pedraza, Gladys, Trache, Andreea, and Rivera, Gonzalo M.

Subjects
Cardiology and Cardiovascular Medicine
Abstract

A better understanding of endothelial dysfunction holds promise for more effective interventions for atherosclerosis prevention and treatment. Endothelial signaling by the non-catalytic region of the tyrosine kinase (NCK) family of adaptors, consisting of NCK1 and NCK2, has been implicated in cardiovascular development and postnatal angiogenesis but its role in vascular disease remains incompletely understood. Here, we report stage- and sex-dependent effects of endothelial NCK2 signaling on arterial wall inflammation and atherosclerosis development. Male and female Nck1-null atheroprone mice enabling inducible, endothelial-specific Nck2 inactivation were fed a high fat diet (HFD) for 8 or 16 weeks to model atherosclerosis initiation and progression, respectively. Analysis of aorta preparations en face during disease progression, but not initiation, showed a significant reduction in plaque burden in males, but not females, lacking endothelial NCK2 relative to controls. Markers of vascular inflammation were reduced by endothelial NCK2 deficiency in both males and females during atherosclerosis progression but not initiation. At advanced stages of disease, plaque size and severity of atherosclerotic lesions were reduced by abrogation of endothelial NCK2 signaling only in males. Collectively, our results demonstrate stage- and sex-dependent modulation of atherosclerosis development by endothelial NCK2 signaling.

Published
2022

12. Myosin and α-actinin regulation of stress fiber contractility under tensile stress.

Author

Ni, Haoran, Ni, Qin, Papoian, Garegin A., Trache, Andreea, and Jiang, Yi

Subjects
CONTRACTILE proteins, STRAINS & stresses (Mechanics), PROTEIN crosslinking, FOCAL adhesions, MYOSIN, MOLECULAR motor proteins, VISCOELASTIC materials
Abstract

Stress fibers are actomyosin bundles that regulate cellular mechanosensation and force transduction. Interacting with the extracellular matrix through focal adhesion complexes, stress fibers are highly dynamic structures regulated by myosin motors and crosslinking proteins. Under external mechanical stimuli such as tensile forces, the stress fiber remodels its architecture to adapt to external cues, displaying properties of viscoelastic materials. How the structural remodeling of stress fibers is related to the generation of contractile force is not well understood. In this work, we simulate mechanochemical dynamics and force generation of stress fibers using the molecular simulation platform MEDYAN. We model stress fiber as two connecting bipolar bundles attached at the ends to focal adhesion complexes. The simulated stress fibers generate contractile force that is regulated by myosin motors and α -actinin crosslinkers. We find that stress fibers enhance contractility by reducing the distance between actin filaments to increase crosslinker binding, and this structural remodeling ability depends on the crosslinker turnover rate. Under tensile pulling force, the stress fiber shows an instantaneous increase of the contractile forces followed by a slow relaxation into a new steady state. While the new steady state contractility after pulling depends only on the overlap between actin bundles, the short-term contractility enhancement is sensitive to the tensile pulling distance. We further show that this mechanical response is also sensitive to the crosslinker turnover rate. Our results provide new insights into the stress fiber mechanics that have significant implications for understanding cellular adaptation to mechanical signaling. [ABSTRACT FROM AUTHOR]

Published
2023
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19. Mechanical properties of the interaction between fibronectin and [[alpha].sub.5]] [[beta].sub.1]-integrin on vascular smooth muscle cells studied using atomic force microscopy

Author

Sun, Zhe, Martinez-Lemus, Luis A., Trache, Andreea, Trzeciakowski, Jerome P., Davis, George E., Pohl, Ulrich, and Meininger, Gerald A.

Subjects
Fibronectins -- Mechanical properties, Vascular smooth muscle -- Research, Biological sciences
Abstract

The mechanical properties of integrin-extracellular matrix (ECM) interactions are important for the mechanotransduction of vascular smooth muscle cells (VSMC), a process that is associated with focal adhesions, and can be of particular significance in cardiovascular disease. In this study, we characterized the unbinding force and binding activity of the initial fibronectin (FN)-[[alpha].sub.5] [[beta].sub.1] interaction on the surface of VSMC using atomic force microscopy (AFM). It is postulated that these initial binding events are important to the subsequent focal adhesion assembly. FN-VSMC adhesions were selectively blocked by antibodies against [[alpha].sub.5]- and [[beta].sub.1]-integfins as well as RGD-containing peptides but not by antibodies against [[alpha].sub.4]- and [[beta].sub.3]-integrins, indicating that FN primarily bound to [[alpha].sub.5][[beta].sub.1]. A characteristic unbinding force of 39 [+ or -] 8 pN was observed and interpreted to represent the FN-[[alpha].sub.5][[beta].sub.1] single-bond strength. The ability of FN to adhere to VSMC (binding probability) was significantly reduced by integrin antagonists, serum starvation, and platelet-derived growth factor (PDGF)-BB, whereas lysophosphatidic acid (LPA) increased FN binding. However, no significant change in the resolved unbinding force was observed. After engagement, the force required to dislodge the FN-coated bead from VSMC increased with increasing of contact time, suggesting a time-dependent increase in number of adhesions and/or altered binding affinity. LPA enhanced this process, whereas PDGF reduced it, suggesting that these factors also affect the multimolecular process of focal contact assembly. Thus AFM is a powerful tool for the characterization of the mechanical properties of integrin-ECM interactions and their regulation. Our results indicate that the functional activity of [[alpha].sub.5][[beta].sub.1] and focal contact assembly can be rapidly regulated. bond strength; lysophosphatidic acid; platelet-derived growth factor; mechanical forces; mechanobiology; focal adhesions; focal contacts

Published
2005

20. Smooth muscle hyperplasia due to loss of smooth muscle α-actin is driven by activation of focal adhesion kinase, altered p53 localization and increased levels of platelet-derived growth factor receptor-β

Author

Papke, Christina L., Cao, Jiumei, Kwartler, Callie S., Villamizar, Carlos, Byanova, Katerina L., Lim, Soon-Mi, Sreenivasappa, Harini, Fischer, Grant, Pham, John, Rees, Meredith, Wang, Miranda, Chaponnier, Christine, Gabbiani, Giulio, Khakoo, Aarif Y., Chandra, Joya, Trache, Andreea, Zimmer, Warren, and Milewicz, Dianna M.

Published
2013
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21. Measurements of the cross-bridge attachment/detachment process within intact sarcomeres by surface plasmon resonance

Author

Tong, Carl W., Kolomenskii, Alexander, Lioubimov, Vladimir A., Schuessler, Hans A., Trache, Andreea, Granger, Harris J., and Muthuchamy, Mariappan

Subjects
Muscle proteins -- Physiological aspects, Resonance -- Analysis, Plasmons (Physics) -- Analysis, Protein research -- Analysis, Biological sciences, Chemistry
Abstract

Results show that cross-bridge attachment within the sarcomere induces a positive surface plasmon resonance shift and blockage of the cross-bridge cycle increases the shift in a calcium dependent manner. This is a first demonstration of the capability of surface plasmon resonance measurements to monitor cross-bridge attachment/detachment within sarcomeres.

Published
2001

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