Defining elastic fiber interactions by molecular fishing: an affinity purification and mass spectrometry approach.

ABSTRACT: Deciphering interacting networks of the extracellular matrix is a major challenge. We describe an affinity purification and mass spectrometry strategy that has provided new insights into the molecular interactions of elastic fibers, essential extracellular assemblies that provide elastic recoil in dynamic tissues. Using cell culture models, we defined primary and secondary elastic fiber interaction networks by identifying molecular interactions with the elastic fiber molecules fibrillin-1, MAGP-1, fibulin-5, and lysyl oxidase. The sensitivity and validity of our method was confirmed by identification of known interactions with the bait proteins. Our study revealed novel extracellular protein interactions with elastic fiber molecules and delineated secondary interacting networks with fibron

SUBMITTER: Cain SA 

PROVIDER: S-EPMC2816023 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature