Developing product quality standards for wheelchairs used in less-resourced environments.

BACKGROUND: Premature failures of wheelchairs in less-resourced environments (LREs) may be because of shortcomings in product regulation and quality standards. The standards published by the International Organization for Standardization (ISO) specify wheelchair tests for durability, safety and performance, but their applicability to products used in the rugged conditions of LREs is unclear. Because of this, wheelchair-related guidelines published by the World Health Organization recommended developing more rigorous durability tests for wheelchairs. OBJECTIVES: This study was performed to identify the additional tests needed for LREs. METHODS: First, a literature review of the development of ISO test standards, wheelchair standards testing studies and wheelchair evaluations in LREs was performed. Second, expert advice from members of the Standards Working Group of the International Society of Wheelchair Professionals (ISWP) was compiled and reviewed. RESULTS: A total of 35 articles were included in the literature review. Participation from LREs was not observed in the ISO standards development. As per wheelchair testing study evidence, wheelchair models delivered in LREs did not meet the minimum standards requirement. Multiple part failures and repairs were observed with reviewed field evaluation studies. ISWP experts noted that several testing factors responsible for premature failures with wheelchair parts are not included in the standards and accordingly provided advice for additional test development. CONCLUSION: The study findings indicate the need to develop a wide range of tests, with specific tests for measuring corrosion resistance of the entire wheelchair, rolling resistance of castors and rear wheels, and durability of whole wheelchair and castor assemblies.

Cathepsin L expression is directed to secretory vesicles for enkephalin neuropeptide biosynthesis and secretion.

Proteases within secretory vesicles are required for conversion of neuropeptide precursors into active peptide neurotransmitters and hormones. This study demonstrates the novel cellular role of the cysteine protease cathepsin L for producing the (Met)enkephalin peptide neurotransmitter from proenkephalin (PE) in the regulated secretory pathway of neuroendocrine PC12 cells. These findings were achieved by coexpression of PE and cathepsin L cDNAs in PC12 cells with analyses of PE-derived peptide products. Expression of cathepsin L resulted in highly increased cellular levels of (Met)enkephalin, resulting from the conversion of PE to enkephalin-containing intermediates of 23, 18-19, 8-9, and 4.5 kDa that were similar to those present in vivo. Furthermore, expression of cathepsin L with PE resulted in increased amounts of nicotine-induced secretion of (Met)enkephalin. These results indicate increased levels of (Met)enkephalin within secretory vesicles of the regulated secretory pathway. Importantly, cathespin L expression was directed to secretory vesicles, demonstrated by colocalization of cathepsin L-DsRed fusion protein with enkephalin and chromogranin A neuropeptides that are present in secretory vesicles. In vivo studies also showed that cathepsin L in vivo was colocalized with enkephalin. The newly defined secretory vesicle function of cathepsin L for biosynthesis of active enkephalin opioid peptide contrasts with its function in lysosomes for protein degradation. These findings demonstrate cathepsin L as a distinct cysteine protease pathway for producing the enkephalin member of neuropeptides.