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Elastin expression

It has been demonstrated in other cell types that lutein can inhibit expression of MMPs and/ or activity (Philips et al., 2007). For example, in dermal fibroblasts lutein inhibits expression of MMP-1 and decreases levels of MMP-2 protein (Philips et al., 2007). In melanoma cells, lutein inhibits MMP-1 expression while stimulating TIMP-2 (Philips et al., 2007). Moreover it has been shown that lutein inhibits elastin expression in fibroblasts subjected to oxidative stress by exposure to ultraviolet light (Philips et al., 2007). These results clearly indicate that lutein can play an important role in remodeling of the extracellular matrix. [Pg.336]

Elastogenesis occurs primarily during late fetal and early neonatal periods. Elastin is synthesized and secreted from several cell types including smooth muscle cells, fibroblasts, endothelial cells, chondroblasts, and mesothelial cells (Uitto et al, 1991) with tissue-specific induction of elastin expression during development (Swee et al, 1995). After elastin has been deposited, its synthesis ceases and very little turnover of elastin is seen during adult life, unless the elastic fibers are subject to injury. In this case,... [Pg.442]

Increased elastin expression in astrocytes ofthe lamina cribrosa in response to elevated intraocular pressure. Invest Ophthalmol Vis Sci 42 2303-2314,... [Pg.87]

Keeley, F.W., Bellingham, C.M., and Woodhouse, K.A., Elastin as a self-organising biomaterial Use of recombinantly expressed human elastin polypeptides as a model system for investigations of structure and self-assembly of elastin, Philos. Trans. R. Soc. Lond. B Biol. Sci., 357, 185-189, 2002. [Pg.274]

Therefore it is of interest to determine whether carotenoids can modulate the turnover of the extracellular matrix by the RPE by affecting the expression of MMPs, elastin, and/or collagen. Cultured RPE cells are a suitable model for such investigations. [Pg.336]

Figure 3 Biosynthesis and purification of 90-kD elastin analogue analyzed by denaturing polyacrylamide gel electrophoresis (10-15% gradient, visualized by silver staining). Lanes 1-7 time course of target protein expression at 0, 30, 60, 90, 120, 150, and 180 minutes after induction. Lane 9 soluble lysate of induced E. coli expression strain BLR(DE3)pRAMl. Lanes 10-13 protein fractions obtained from immobilized metal affinity chromatography of the lysate on nickel-NTA agarose (imidazole gradient elution). Lanes 8,14 protein molecular weight standards of 50, 75, 100, and 150 kD. Figure 3 Biosynthesis and purification of 90-kD elastin analogue analyzed by denaturing polyacrylamide gel electrophoresis (10-15% gradient, visualized by silver staining). Lanes 1-7 time course of target protein expression at 0, 30, 60, 90, 120, 150, and 180 minutes after induction. Lane 9 soluble lysate of induced E. coli expression strain BLR(DE3)pRAMl. Lanes 10-13 protein fractions obtained from immobilized metal affinity chromatography of the lysate on nickel-NTA agarose (imidazole gradient elution). Lanes 8,14 protein molecular weight standards of 50, 75, 100, and 150 kD.
McGowan, S. E., Doro, M. M., and Jackson, S. (1997). Endogenous retinoids increase perinatal elastin gene expression in rat lung fibroblasts and fetal explants. Am. J. Physiol. 273, L410-L416. [Pg.214]

Fibrillin microfibrils are widely distributed extracellular matrix assemblies that endow elastic and non elastic connective tissues with long-range elasticity. They direct tropoelastin deposition during elastic fibrillogenesis and form an outer mantle for mature elastic fibers. Microfibril arrays are also abundant in dynamic tissues that do not express elastin, such as the ciliary zonules of the eye. Mutations in fibrillin-1—the principal structural component of microfibrils—cause Marfan syndrome, a heritable disease with severe aortic, ocular, and skeletal defects. Isolated fibrillin-rich microfibrils have a complex 56 nm beads-on-a-string appearance the molecular basis of their assembly and... [Pg.405]

Kahari, V. M., Chen, Y. Q., Bashir, M. M., Rosenbloom, J., and Uitto, J. (1992). Tumor necrosis factor-alpha down-regulates human elastin gene expression. Evidence for the role of AP-1 in the suppression of promoter activity. J. Biol. Chem. 267, 26134-26141. [Pg.456]

Reitamo, S., Remitz, A., Tamai, K., Ledo, I., and Uitto, J. (1994). Interleukin 10 up-regulates elastin gene expression in vivo and in vitro at the transcriptional level. Biochem. J. 302, 331-333. [Pg.459]

Swee, M. H., Parks, W. C., and Pierce, R. A. (1995). Developmental regulation of elastin production. Expression of tropoelastin pre-mRNA persists after down-regulation of steady-state mRNA levels. / Biol. Chem. 270, 14899-14906. [Pg.460]

AMINO ACID COMPOSITION (EXPRESSED AS RESIDUES PER 1000 TOTAL RESIDUES) OF TYPICAL MATURE ELASTIN, MATRIX COLLAGEN AND MICROFIBRILLAR PROTEIN PREPARATIONS. [Pg.67]

AMINO ACID COMPOSITION OF TROPOELASTIN AND A PUTATIVE TROPO-ELASTIN PRECURSOR (EXPRESSED AS MOLES PER 1000 MOLES OF AMINO ACID RESIDUE). [Pg.71]

Mahmoodian F and Peterkofsky B (1999) Vitamin C deficiency in guinea pigs differentially affects the expression of type fV collagen, laminin, and elastin in blood vessels. Journal of Nutrition 129, 83-91. [Pg.438]


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See also in sourсe #XX -- [ Pg.441 , Pg.442 ]




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Elastin

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