Elastic fiber during development and aging

Baccarani-Contri, M.

doi:10.1002/(sici)1097-0029(19970815)38:4<428::aid-jemt10>3.0.co;2-l

Cited by 176 publications

(108 citation statements)

References 70 publications

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“…The RAGE-dependent lung function suggested an effect of RAGE on the lung elasticity, which is determined by surfactants and extracellular matrix proteins (33), including elastin and collagen (8,35). Although RAGE had no effect on the mRNA expressions of surfactant proteins (gene microarray analysis; data not shown), we found a lower mRNA and protein level of elastin in young RAGE-KO mice than in WT mice (Tables 3 and 4, Fig.…”

Section: Rage Trans Interaction In Alveolar Epithelial Cellsmentioning

confidence: 68%

The receptor for advanced glycation end-products supports lung tissue biomechanics

Al‐Robaiy

Weber

Simm

et al. 2013

American Journal of Physiology-Lung Cellular and Molecular Phys

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The receptor for advanced glycation end-products (RAGE) and its soluble forms are predominantly expressed in lung but its physiological importance in this organ is not yet fully understood. Since RAGE acts as a cell adhesion molecule, we postulated its physiological importance in the respiratory mechanics. Respiratory function in a buffer-perfused isolated lung system and biochemical parameters of the lung were studied in young, adult, and old RAGE knockout (RAGE-KO) mice and wild-type (WT) mice. Lungs from RAGE-KO mice showed a significant increase in the dynamic lung compliance and a decrease in the maximal expiratory air flow independent of age-related changes. We also determined lower mRNA and protein levels of elastin in lung tissue of RAGE-KO mice. RAGE deficiency did not influence the collagen protein level, lung capillary permeability, and inflammatory parameters (TNF-␣, high-mobility group box protein 1) in lung. Overexpressing RAGE as well as soluble RAGE in lung fibroblasts or cocultured lung epithelial cells increased the mRNA expression of elastin. Moreover, immunoprecipitation studies indicated a trans interaction of RAGE in lung epithelial cells. Our findings suggest the physiological importance of RAGE and its soluble forms in supporting the respiratory mechanics in which RAGE trans interactions and the influence on elastin expression might play an important role.receptor for advanced glycation end-products; aging; biomechanics; elastin; mouse THE RECEPTOR FOR ADVANCED glycation end-products (RAGE) is a pattern recognition receptor of the immunoglobulin superfamily (32). RAGE is predominantly expressed in lung, particularly in the type I alveolar epithelial (ATI) cells (12,15,46). This specific localization suggests its important physiological function in the alveolar epithelium. In other cell types and tissues, the expression of RAGE is activated in response to pathophysiological conditions, such as the accumulation of advanced glycation end-products (AGEs) and inflammation (1). RAGE expression is highly associated with lung development and increases during the alveolarization (29,40). High RAGE expression prior to the alveolarization period has adverse effects associated with a severe pulmonary dysplasia (16,41). A reduced alveolar expression of RAGE is related to pathophysiological changes of the lung tissue, such as carcinoma (3), fibrosis (34, 37), and chronic obstructive pulmonary disease (COPD) (34). In addition to the membrane-bound receptor, soluble RAGE (sRAGE) forms exist as the result of either alternative splicing (22) or protein shedding by metalloproteinases (39, 52). sRAGE normally exists in the bronchoalveolar lavage (BAL) at a high level (53), but it is deficient in neutrophilic asthma and COPD (47, 49).The physiological importance of RAGE in lung is not yet fully understood because mice lacking RAGE do not show obvious pulmonary alterations (5, 9). Only intervention studies indicated an adverse effect of RAGE in the development of lung fibrosis (14, 19) and acute lung injury (4...

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Section: Rage Trans Interaction In Alveolar Epithelial Cellsmentioning

confidence: 68%

The receptor for advanced glycation end-products supports lung tissue biomechanics

Al‐Robaiy

Weber

Simm

et al. 2013

American Journal of Physiology-Lung Cellular and Molecular Phys

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“…Once laid down, they are thought to remain stable 2 , except in the uterine tract where cycles of active remodeling occur 3 . Loss of elastic fibers underlies connective tissue aging and important diseases including emphysema [4][5][6][7] . Failure to maintain elastic fibers is explained by a theory of antielastase-elastase imbalance 8 , but little is known about the role of renewal.…”

mentioning

confidence: 99%

Elastic fiber homeostasis requires lysyl oxidase–like 1 protein

et al. 2004

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“…Immunohistochemical studies on human skin have suggested that decorin may be associated with fibrillin-containing, elastin-associated microfibrils, whereas biglycan may be associated with the elastin core of the elastic fibers (10,11). Kielty et al (12) have shown that chondroitinase AC treatment disrupts the bead component of fibrillin-containing microfibrils and that a chondroitinase AC-sensitive proteoglycan can be co-precipitated with fibrillin from smooth muscle cell conditioned medium.…”

mentioning

confidence: 99%

Molecular Interactions of Biglycan and Decorin with Elastic Fiber Components

Reinboth

Hanssen

Cleary

et al. 2002

Journal of Biological Chemistry

146

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The interactions of the dermatan sulfate proteoglycans biglycan and decorin have been investigated with the elastic fiber components, tropoelastin, fibrillin-containing microfibrils, and microfibril-associated glycoproteins (MAGP) 1 and 2. Both proteoglycans were found to bind tropoelastin and fibrillin-containing microfibrils but not MAGPs 1 and 2 in solid phase binding assays. The specificity of the binding of biglycan and decorin to tropoelastin was confirmed by co-immunoprecipitation experiments and by the blocking of the interactions with elastin-derived peptides. Isolated core proteins from biglycan and decorin bound to tropoelastin more strongly than the intact proteoglycans, and there were no differences in the tropoelastin binding characteristics of distinct glucuronate-rich and iduronate-rich glycoforms of biglycan. These findings indicated that the binding sites were contained in the protein cores of the proteoglycans rather than the glycosaminoglycan side chains. Scatchard analysis showed that biglycan bound more avidly than decorin to tropoelastin with K d values estimated as 1.95 ؋ 10 ؊7 M and 5.3 ؋ 10 ؊7 M, respectively. In blocking experiments each proteoglycan showed extensive inhibition of binding of the other to tropoelastin but was most effective at blocking its own binding. This result suggested that biglycan and decorin had closely spaced but distinct binding sites on tropoelastin. Addition of the elastin-binding protein MAGP-1 to the assays enhanced the binding of biglycan to tropoelastin but had no effect on the decorin-tropoelastin interaction. Co-immunoprecipitation experiments showed that MAGP-1 interacted with biglycan but not decorin in the solution phase. The results indicated that biglycan specifically formed a ternary complex with tropoelastin and MAGP-1. Overall the study supports the concept that biglycan may have a specific role in the elastinogenic phase of elastic fiber formation.

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Elastic fiber during development and aging

Cited by 176 publications

References 70 publications

The receptor for advanced glycation end-products supports lung tissue biomechanics

The receptor for advanced glycation end-products supports lung tissue biomechanics

Elastic fiber homeostasis requires lysyl oxidase–like 1 protein

Molecular Interactions of Biglycan and Decorin with Elastic Fiber Components

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