Fibromodulin belongs to the family of small interstitial proteoglycans. The encoded protein possesses a central region containing leucine-rich repeats with 4 keratan sulfate chains, flanked by terminal domains containing disulphide bonds. Owing to the interaction with type I and type II collagen fibrils and in vitro inhibition of fibrillogenesis, the encoded protein may play a role in the assembly of extracellular matrix. It may also regulate TGF-beta activities by sequestering TGF-beta into the extracellular matrix. Sequence variations in this gene may be associated with the pathogenesis of high myopia. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jun 2013]
Forensic Context
A study in humans demonstrated that transcriptomic profiling of left ventricular myocardium from autopsy-defined arrhythmic sudden deaths revealed 31 up-regulated and 36 down-regulated genes compared to nonarrhythmic deaths [Caudal et al. DOI:10.1016/j.jacep.2024.08.013].