Myocilin Regulates Metalloprotease 2 Activity Through Interaction With TIMP3.

ABSTRACT:

Purpose

To elucidate functions of wild-type myocilin, a secreted glycoprotein associated with glaucoma.

Methods

Lysates of mouse eyes were used for immunoprecipitation with affinity-purified antibodies against mouse myocilin. Shotgun proteomic analysis was used for the identification of proteins interacting with myocilin. Colocalization of myocilin and tissue inhibitor of metalloproteinases 3 (TIMP3) in different eye structures was investigated by a multiplex fluorescent in situ hybridization and immunofluorescent labeling with subsequent confocal microscopy. Matrix metalloproteinase 2 (MMP2) activity assay was used to test effects of myocilin on TIMP3 inhibitory action.

Results

TIMP3 was identified by a shotgun proteomic analysis as a protein that was coimmunoprecipi

SUBMITTER: Joe MK 

PROVIDER: S-EPMC5644706 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature