Management of arthrofibrosis in neuromuscular disorders: a review

Abstract

Arthrofibrosis, or rigid contracture of major articular joints, is a significant morbidity of many neurodegenerative disorders. The pathogenesis depends on the mechanism and severity of the precipitating neuromuscular disorder. Most neuromuscular disorders, whether spastic or hypotonic, culminate in decreased joint range of motion. Limited range of motion precipitates a cascade of pathophysiological changes in the muscle-tendon unit, the joint capsule, and the articular cartilage. Resulting joint contractures limit functional mobility, posing both physical and psychosocial burdens to patients, economic burdens on the healthcare system, and lost productivity to society. This article reviews the pathophysiology of arthrofibrosis in the setting of neuromuscular disorders. We describe current non-surgical and surgical interventions for treating arthrofibrosis of commonly affected joints. In addition, we preview several promising modalities under development to ameliorate arthrofibrosis non-surgically and discuss limitations in the field of arthrofibrosis secondary to neuromuscular disorders.

Poly‐L‐Lactic acid increases collagen gene expression and synthesis in cultured dermal fibroblast (Hs68) through the TGF‐β/Smad pathway

“…In our study, we first examined the effect of PLLA on collagen synthesis, and the PIP EIA assay confirmed that procollagen synthesis in dermal fibroblasts gradually increased with increasing PLLA concentration. It is known that type I collagen is the most common type of collagen in the human body, consisting of a type I collagen α 1 chain and a type I collagen α 2 chains, encoded by the COL1A1 and COL1A2 genes 22 . Here, we confirmed that the mRNA levels of COL1A1 and COL1A2 gradually increased with increasing PLLA concentration.…”

“…It is known that type I collagen is the most common type of collagen in the human body, consisting of a type I collagen α 1 chain and a type I collagen α 2 chains, encoded by the COL1A1 and COL1A2 genes. 22 Here, we confirmed that the mRNA levels of COL1A1 and COL1A2 gradually increased with increasing PLLA concentration. The protein level of COL1A1 also increased gradually.…”

Octanoyl esterification of low molecular weight sulfated galactan enhances the cellular uptake and collagen expression in fibroblast cells

“…Collagen, a major protein in the ECM produced by fibroblasts, has a crucial role in providing structural support, strength and elasticity to tissues (4). Among the different types of collagens, type I collagen is the most abundant in the human body and is composed of the Col1A1 and Col1A2 proteins (30). A previous study indicated that Col1A1 is predominantly expressed in fibroblasts, with a higher production ratio compared to Col1A2 (ratio, 2:1) (31).…”

Results of Surgical Correction of Fixed Flexion Deformity during Total Knee Arthroplasty in Patient of Knee Osteoarthritis: A Comprehensive Review

“…Soft tissue releases have shown promising outcomes in terms of improving knee extension and reducing flexion contracture. However, excessive release can lead to instability or weakening of the soft tissues, requiring careful consideration and surgical planning [16] .…”