Ultraviolet radiation reduces desmosine cross-links in elastin
نویسندگان
چکیده
Elastic fibers, a major component of the extracellular matrix of the skin, are often exposed to ultraviolet (UV) radiation throughout mammalian life. We report on an in vitro study of the alterations in bovine nuchal ligament elastic fibers resulting from continuous UV-A exposure by the use of transmission electron microscopy (TEM), histology, mass spectrometry, and solid state 13C NMR methodologies. TEM images reveal distinct cracks in elastic fibers as a result of UV-A irradiation and histological measurements show a disruption in the regular array of elastic fibers present in unirradiated samples; elastic fibers appear shorter, highly fragmented, and thinner after UV-A treatment. Magic angle spinning 13C NMR was applied to investigate possible secondary structural changes or dynamics in the irradiated samples; our spectra reveal no differences between UV-A irradiated and non-irradiated samples. Lastly, MALDI mass spectrometry indicates that the concentration of desmosine, which forms cross-links in elastin, is observed to decrease by 11 [Formula: see text] following 9 days of continuous UV-A irradiation, in comparison to unirradiated samples. These alterations presumably play a significant role in the loss of elasticity observed in UV exposed skin.
منابع مشابه
Structural studies on cross-linked regions of elastin.
A novel use of Edman degradation was made in the study of desmosineand isodesmosine-containing elastolytic peptides of bovine ligamentum nuchae elastin. The elastolysis of elastin produced peptides with the cleavage at or near the NH,-terminals of desmosine and isodesmosine cross-links. Therefore, it became possible to release single chain peptides from the carboxyl groups of these cross-links ...
متن کاملElastin cross-linking in the skin from patients with amyotrophic lateral sclerosis.
Two cross-links unique to elastin, desmosine and isodesmosine were measured and compared in skin tissue (left upper arm) from 10 patients with amyotrophic lateral sclerosis (ALS) and from seven age-matched controls. The contents of desmosine and isodesmosine were significantly decreased (p < 0.01 and p < 0.01, respectively) in patients with ALS compared with those of controls, and were negative...
متن کاملLysyl oxidase: new looks on LOX.
The extracellular matrix proteins collagen and elastin determine, to a large extent, the biomechanical properties of the vessel wall. Both molecules are secreted as monomers, but are posttranslationally modified in the extracellular space in order to generate stable polymers. A critical feature of collagen and elastin fibers is the degree of cross-linking. The first step in cross-linking is the...
متن کاملChemotactic activity of elastin-derived peptides.
Elastin-derived peptides, produced by digesting human aortic elastin and bovine ligament elastin with human neutrophil elastase, were tested for chemotactic activity. At 100 micrograms protein/ml, elastin digests were nearly as active for monocytes as saturating amounts of complement-derived chemotactic activity. Neutrophils and alveolar macrophages showed less response to elastin peptidces tha...
متن کاملLiberation of desmosine and isodesmosine as amino acids from insoluble elastin by elastolytic proteases.
The development of atherosclerotic lesions and abdominal aortic aneurysms involves degradation and loss of extracellular matrix components, such as collagen and elastin. Releases of the elastin cross-links desmosine (DES) and isodesmosine (IDE) may reflect elastin degradation in cardiovascular diseases. This study investigated the production of soluble elastin cross-linking structures by protei...
متن کامل