A Novel Decorin Gene Mutation in Congenital Hereditary Stromal Dystrophy: A Korean Family

Abstract

A 43-year-old man developed decreased vision in the right eye that had persisted for seven years. Under slit lamp examination, corneal clouding was noted with normal endothelium and ocular structure. From the clinical evidence, we suspected that the patient had congenital hereditary stromal dystrophy (CHSD). He and his family underwent a genetic analysis. Penetrating keratoplasty was conducted, and the corneal button was investigated for histopathologic confirmation via both light and electron microscopy. The histopathologic results revealed mildly loosened stromal structures, which exhibited an almost normal arrangement and differed slightly from the previous findings of CHSD cases. With regard to the genetic aspects, the patient and his mother harbored a novel point mutation of the decorin gene. This genetic mutation is also distinct from previously described deletion mutations of the decorin gene. This case involved delayed penetration of mild clinical symptoms with the histological feature of a loosened fiber arrangement in the corneal stroma. We concluded that this condition was a mild form of CHSD. However, from another perspective, this case could be considered as "decorin gene-associated corneal dystrophy," which is distinct from CHSD. Further evaluation will be required for appropriate clinical, histopathologic and genetic approaches for such cases.

Targeted proteomics effectively quantifies differences between native lung and detergent-decellularized lung extracellular matrices

“…Proteoglycans confer structure to matrix in part by organizing collagen and elastin fibrils in space [14,15] and contribute to lung elasticity and to alveolar stability at low and medium lung volumes [16], thereby enabling gas exchange. We quantified 8 proteoglycans in native and decellularized lungs (Fig.…”

The regulatory roles of small leucine‐rich proteoglycans in extracellular matrix assembly

“…A recently described decorin‐associated congenital stromal corneal dystrophy involves a novel nucleotide substitution (c.1036T>G) in decorin . The substitution of cysteine by glycine within the C‐terminus caused a milder phenotype than the truncated mutations . Presumably, loss of the Cys residue results in a deficiency in disulfide bond formation in this critical region.…”

Regulation of corneal stroma extracellular matrix assembly

“…Three different frame-shift mutations (c.947delG; c.967delT; c.941delC) have been reported at the C-terminus of decorin; all of these deletion mutations lead to identical truncations of decorin, lacking a 33 amino acid segment that includes the SLRP-specific “ear” repeat (Bouhenni et al, 2011; Bredrup et al, 2010; Kim et al, 2011; Rodahl et al, 2006). Besides the deletion mutations, a family has been described with a decorin-associated CSCD involving a novel nucleotide substitution (c.1036T>G) within the C-terminus of decorin, which has resulted in a milder phenotype than in the truncated mutations (Lee et al, 2012). Presumably, the loss of the cys residue prevents disulfide bond formations in this critical region, resulting in altered conformation rather than a truncation, and a plausible explanation for the milder functional consequences.…”