Altered protein conformation and lower stability of the dystrophic transforming growth factor beta-induced protein mutants.

ABSTRACT:

Purpose

Transforming growth factor beta-induced protein (TGFBIp) is a widely expressed extracellular matrix protein that plays roles in cell adhesion and migration, differentiation, apoptosis, bone morphogenesis, and carcinogenesis. Mutations of TGFBIp have been linked to stromal corneal dystrophies, a group of protein conformational diseases characterized by abnormal protein aggregations in the cornea. However, the underlying pathogenic mechanism remains elusive due to a lack of insight into the molecular properties of the disease-causing mutants. In the current study, we applied spectroscopic tools to compare the conformation and protein stability of recombinant wild-type (WT) TGFBIp to two dystrophic mutants, R124C and R555W.

Methods

A serum-free expression system was use

SUBMITTER: Grothe HL 

PROVIDER: S-EPMC3611947 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature