| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10737014 | Experimental Gerontology | 2013 | 9 Pages |
Abstract
⺠Changes in the extracellular matrix essentially contribute to lung aging. ⺠We examine amount and post-translational modifications with glycation end-products in fibrillar collagens from mouse lung. ⺠Aging causes a lower total amount and higher load with glycation end-products of lung collagens. ⺠Higher load with glycation end-products is associated with lower enzymatic solubility of lung collagens. ⺠Not all changes occur gradually with higher age.
Keywords
ECMCTGFTissue inhibitor of metalloproteaseMMPPBSDMEMlogFCDulbecco's modified Eagle's mediumAdenosine triphosphate synthaseArgpyrimidineATPaseLungTIMPAgingcalf serumAgesignal intensityConnective tissue growth factorExtracellular matrixMatrix metalloproteaseAdvanced glycation end-productPhosphate-buffered salineMouseISFpolymerase chain reactionPCRSoluble fractionInsoluble fractionCollagenGlycation
Related Topics
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Biochemistry, Genetics and Molecular Biology
Ageing
Authors
Paulina Rolewska, Samiya Al-Robaiy, Alexander Navarrete Santos, Andreas Simm, Rolf-Edgar Silber, Babett Bartling,