Extracellular matrix metabolism in bronchopulmonary dysplasia : Focus on lysyl hydroxylases and transglutaminases

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WitschJoern_2013_02_04.pdf (2.2 MB)

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2013

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DOI:
http://dx.doi.org/10.22029/jlupub-14010

Abstract

Bronchopulmonary dysplasia is a complication of premature birth characterized byimpaired alveolar development. Remodeling of the ECM is a driving force foralveolarization and, if pertubated, may impair septation, suggesting dysregulation ofECM remodeling enzymes that drive collagen fiber formation and maturation: theprocollagen-lysine, 2-oxoglutarate 5-dioxygenases (Plod) family, also known as lysylhydroxylases (which catalyzes glycosylation and hydroxylation of collagen), and thetransglutaminases Tgm1 and Tgm2, which cross-link ECM components.Expressions of Plod1, Plod2, Plod3, Tgm1 and Tgm2 were determined using apopular mouse model of BPD, in which mouse pups are exposed to hyperoxia (85%O2) or normoxia (21% O2) for 28 days after birth. The lungs of these mice wereharvested at various time-points and assessed for Plod and Tgm expression andlocalization by semi-quantitative RT-PCR, immunoblotting and immunohistochemistry.Increased expressions of Plods and Tgms could be observed at the geneand protein levels under hyperoxic conditions compared to normoxic conditions.The data suggest that BPD is characterized by elevated levels of ECM-stabilizingmolecules, which may make the ECM more resistant to remodeling. This overstabilizedstate of the ECM may, at least in part, underlie the arrested septationobserved both in the lungs of infants with BPD, and in animal models of BPD.

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