With aging and cancer there is increased expression or activity of matrix metalloproteinases (MMPs) that degrade and remodel the structural extracellular matrix (ECM). In addition, exposure of skin to ultraviolet (UV) radiation (photoaging) leads to loss of cell viability, membrane damage, and deposition of excessive elastotic material. Lutein has antioxidant, anti-inflammatory, photoprotective, and anti-carcinogenic properties. The goal of this research was to investigate lutein's anti-aging and anti-carcinogenic effects via the regulation of the extracellular matrix remodeling. To this purpose, the effects of lutein on the expression of MMPs and their inhibitors (TIMPs, tissue inhibitors of metalloproteinases) in dermal fibroblasts (intrinsic aging) and melanoma cells were examined. Further, for lutein's photoprotective effects, the regulation of cell viability, membrane integrity, and elastin expression in the non-irradiated, and UVA or UVB radiation exposed fibroblasts were analyzed. Lutein significantly inhibited MMP-1 expression, transcriptionally, and MMP-2 protein levels in dermal fibroblasts, without altering TIMPs expression. It significantly inhibited MMP-1 expression in melanoma cells while stimulating TIMP-2. Lutein did not alter fibroblast or melanoma cell viability or membrane integrity. In ultraviolet radiation exposed fibroblasts, lutein improved cell viability, membrane integrity and inhibited elastin expression, though more significantly in the UVB exposed fibroblasts. In summary, the mechanism to lutein's anti-aging and anti-carcinogenic effects include the inhibition of MMP to TIMP ratio in dermal fibroblasts and melanoma cells, and the inhibition of cell loss, membrane damage and elastin expression in ultraviolet radiation exposed fibroblasts.

Physical properties of the cross-linked polypentapeptide of tropoelastin are reported along with chemical characterization of key intermediates in its synthesis. 220 MHz proton magnetic resonance spectra are reported on the constituent pentamers and their respective high polymers which verify structural and conformational integrity. Scanning electron microscopy of the cross-linked material formed without orientation and with flow orientation is reported. The former demonstrates the inherent fibrillar and anisotropic nature of the synthetic product. Stress-strain studies show the cross-linked polypentapeptide to exhibit elastomeric properties that are dependent on the water content of the matrix. At high water contents the elastic modulus is less than that of wet native aortic elastin and becomes greater on drying.

The synthetic, cross-linked polypentapeptide of tropoelastin has been shown to calcify from serum alone even when separated from the serum medium by a dialysis membrane with a low-molecular-weight cut off. By microprobe analysis, it appeared that the only serum elements required for the calcification were calcium and phosphorus. Furthermore, thin sections of the calcified matrix showed the calcification to occur throughout the matrix, and thereby verified that it is a bulk property of the matrix and not an interfacial property. To our knowledge this is the first demonstration of an insoluble, synthetic polypeptide to function as a serum calcifiable matrix and by doing so it opens the door to potential medical applications.

Scanning electron microscopy and electron probe microanalysis studies are reported on thin sections of calcified coacervates of alpha-elastin. It is found that the capacity of elastin coacervates to initiate calcification is a bulk property of the coacervate and not limited to the serum-coacervate interface, that the calcium phosphate deposits act to bind the protein units together and slow the dissolution and spreading of the coacervate as it floats on an airwater interface, and that, within the limits of detectability, there is no involvement of sulfur. As the charged groups of alpha-elastin had been blocked, the initiation of deposition is due to neutral sites in the protein which are tightly bound to the calcium phosphate deposits.