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You searched for subject:(Extracellular matrix components). Showing records 1 – 2 of 2 total matches.

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Georgia Tech

1. Konduri, Suchitra. The Influence of Normal Physiological Forces on Porcine Aortic Heart Valves in a Sterile Ex Vivo Pulsatile Organ Culture System.

Degree: MS, Chemical Engineering, 2005, Georgia Tech

The aortic valve functions in a complex mechanical environment which leads to force dependent cellular and tissue responses. Characterization of these responses provides a fundamental understanding of valve pathogenesis. The aim of this work was to develop an ex vivo organ culture system capable of simulating physiological aortic pressures and flow rates, and study the biological characteristics of native porcine aortic valves cultured in the system. Collagen, sGAG and elastin content of the valve leaflets were measured and cusp morphology, cell phenotype, cell proliferation and apoptosis were examined. Presence of endothelial cells (ECs) on the leaflet surface was also evaluated. The differences in collagen, sGAG and elastin contents were not significant (p greater than0.05) between the cultured and fresh valve leaflets. The cultured valves maintained the structural integrity of the leaflets while preserving the native morphology and cell phenotype. Cell phenotype in leaflets incubated statically under atmospheric conditions decreased compared to fresh and cultured valve leaflets, indicating the importance of mechanical forces in maintaining the natural biology of the valve leaflets. ECs were retained on the surfaces of cultured leaflets with no remodeling of the leaflets. The number of apoptotic cells in the cultured leaflets was significantly (p less than 0.05) less than in the statically incubated leaflets and comparable to fresh leaflets. The sterile ex vivo organ culture system thus maintained the viability and native biological characteristics of the aortic valves that were cultured under dynamic conditions for a period of 48 hours. Advisors/Committee Members: Dr. Ajit P.Yoganathan (Committee Chair), Dr. Athanassios Sambanis (Committee Member), Dr. Timothy M. Wick (Committee Member).

Subjects/Keywords: Flow and pressure waveforms; Porcine aortic valve leaflets; Extracellular matrix components; Cell phenotype; Endothelial cells; Organ culture system; Tissue morphology

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Konduri, S. (2005). The Influence of Normal Physiological Forces on Porcine Aortic Heart Valves in a Sterile Ex Vivo Pulsatile Organ Culture System. (Masters Thesis). Georgia Tech. Retrieved from http://hdl.handle.net/1853/6999

Chicago Manual of Style (16th Edition):

Konduri, Suchitra. “The Influence of Normal Physiological Forces on Porcine Aortic Heart Valves in a Sterile Ex Vivo Pulsatile Organ Culture System.” 2005. Masters Thesis, Georgia Tech. Accessed March 03, 2021. http://hdl.handle.net/1853/6999.

MLA Handbook (7th Edition):

Konduri, Suchitra. “The Influence of Normal Physiological Forces on Porcine Aortic Heart Valves in a Sterile Ex Vivo Pulsatile Organ Culture System.” 2005. Web. 03 Mar 2021.

Vancouver:

Konduri S. The Influence of Normal Physiological Forces on Porcine Aortic Heart Valves in a Sterile Ex Vivo Pulsatile Organ Culture System. [Internet] [Masters thesis]. Georgia Tech; 2005. [cited 2021 Mar 03]. Available from: http://hdl.handle.net/1853/6999.

Council of Science Editors:

Konduri S. The Influence of Normal Physiological Forces on Porcine Aortic Heart Valves in a Sterile Ex Vivo Pulsatile Organ Culture System. [Masters Thesis]. Georgia Tech; 2005. Available from: http://hdl.handle.net/1853/6999


University of Missouri – Columbia

2. Byrne, Todd S. Structural interactions sites of matrix metalloproteinase-12 with collagen triple helix, micelles, and a natural product from green tea.

Degree: 2012, University of Missouri – Columbia

Matrix metalloproteinase (MMP-12) is associated with many costly, life-threatening diseases, such as atherosclerosis, pulmonary emphysema, asthma, and multiple sclerosis. Therefore, macrophage secreted MMP-12 is likely found in many parts of the body likely interacting with extracellular components as have been shown and previously investigated by in vitro studies. MMP-12 is capable of cleaving elastin and may biologically cleave other extracellular components, such as collagen. This article seeks to investigate interactions of MMP-12 with a collagen-mimicking triple helical peptide (THP). The methods employed for this study involved paramagnetic relaxation enhancement (PRE). A THP paramagnetically labeled with the artificial amino acid TOAC was used to investigate the interaction between MMP-12 and a THP. This study aims to answer the question of how a THP binds to MMP-12. Preliminary structures of the complex presented here have converged. The THP binds to MMP-12 in a specific manner in one type of angle of inclination. Whereby, the orientations of the THP appear to have the N-terminus along the unprimed side of MMP-12. These results may also further hint at an exosite near the C2 calcium binding site on MMP-12. The inhibition of MMP-12 by a natural polyphenol, (-)-Epigallocatechin gallate (EGCG) was investigated. Also, structural information concerning the binding sites of EGCG to MMP-12 was obtained. The methods employed involve paramagnetic relaxation enhancement, inhibition of enzyme activity, and stability by urea denaturation. A paramagnetic ECG, an analog of EGCG, was generated by incubating briefly in the presence of peroxide and horse radish peroxidase. The radical was used in an attempt to characterize the interaction between EGCG and MMP-12. The initial NMR investigations involving paramagnetic relaxation enhancement (PRE) or/and NOE experiments with EGCG suggest two to three binding sites on MMP-12, including one near a calcium binding site. Inhibition of enzyme kinetics and denaturation melts were also carried out with MMP-12 in the presence of EGCG to better ascertain the most significant binding site of EGCG to MMP-12. The kinetic experiments indicate that inhibition appears to be non-competitive, and there is a calcium dependence for the EGCG inhibition of MMP-12. The calcium dependent inhibition suggests that the calcium site (C2 site or Ca 403) indicated in the PRE and NOE experiments could be the key site of allosteric inhibition of MMP-12 by EGCG. This study investigates the interaction of MMP-12 with dodecyl phosphatidylcholine (DPC) micelles and 1,2-dihexanoyl-sn-glycero-3-phosphocholine (DHPC) micelles. The composition of the micelles has been varied. For example, DPC/CHAPS micelles and DPC/CHAPS doped with cholesterol sulfate micelles have been investigated. Chemical shift perturbations and line broadening analysis has been conducted, and the initial results suggest a KD of physiological importance. Cross -correlation rates and the extent of chemical shift perturbation between the DPC/CHAPS… Advisors/Committee Members: Van Doren, Steven (advisor).

Subjects/Keywords: matrix metalloproteinase; extracellular components; binding site

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Byrne, T. S. (2012). Structural interactions sites of matrix metalloproteinase-12 with collagen triple helix, micelles, and a natural product from green tea. (Thesis). University of Missouri – Columbia. Retrieved from http://hdl.handle.net/10355/33129

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Byrne, Todd S. “Structural interactions sites of matrix metalloproteinase-12 with collagen triple helix, micelles, and a natural product from green tea.” 2012. Thesis, University of Missouri – Columbia. Accessed March 03, 2021. http://hdl.handle.net/10355/33129.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Byrne, Todd S. “Structural interactions sites of matrix metalloproteinase-12 with collagen triple helix, micelles, and a natural product from green tea.” 2012. Web. 03 Mar 2021.

Vancouver:

Byrne TS. Structural interactions sites of matrix metalloproteinase-12 with collagen triple helix, micelles, and a natural product from green tea. [Internet] [Thesis]. University of Missouri – Columbia; 2012. [cited 2021 Mar 03]. Available from: http://hdl.handle.net/10355/33129.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Byrne TS. Structural interactions sites of matrix metalloproteinase-12 with collagen triple helix, micelles, and a natural product from green tea. [Thesis]. University of Missouri – Columbia; 2012. Available from: http://hdl.handle.net/10355/33129

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

.