Nonspecific Lipid Transfer Protein (Sterol Carrier Protein-2) Defective in Patients with Deficient Peroxisomes

Cell Structure and Function

Yutaka Tashiro²  Tadao Orii¹  Seiji Yamaguchi¹  Yasuyuki Suzuki¹  Makoto Tsuneoka² 

[1] Department of Pediatrics, Gifu University School of Medicine;Department of Physiology, Kansai Medical University, Moriguchi

关键词: human nonspecific lipid transfer protein;    peroxisomes;    Zellweger syndrome;    neonatal adrenoleukodystrophy;   

DOI  :  10.1247/csf.15.301

学科分类：分子生物学，细胞生物学和基因

来源: Japan Society for Cell Biology

【 摘 要 】

References(23)Cited-By(31)The biosynthesis and intracellular localization of nonspecific lipid transfer protein (nsLTP) in control human subjects and in patients with peroxisome-deficient disorders were investigated. The molecular mass of human nsLTP was indistinguishable from that of rat nsLTP (13 kDa) by an immunoblot analysis. Intracellular localization was identical with that of catalase, a marker enzyme of peroxisomal matrix, by a double immunofluorescence study. The nsLTP was deficient in liver tissues or fibroblasts from patients with peroxisomedeficient disorders such as Zellweger syndrome and neonatal adrenoleukodystrophy (ALD). Pulse-chase experiments showed that nsLTP was synthesized as a large precursor in both the control and Zellweger fibroblasts. However, the processing to the 13 kDa mature protein was disturbed and the degradation was rapid in Zellweger fibroblasts. After somatic cell fusion using Zellweger fibroblasts from different genetic groups, the processing was normalized. These results suggest that the biosynthesis and localization of human nsLTP are similar to those of rat nsLTP and that the defect of nsLTP in peroxisome-deficient disorders is a phenomenon secondary to an abnormal transport mechanism of peroxisomal proteins. The defect of nsLTP may play an important role in metabolic disturbances in bile acid synthesis and steroidogenesis in peroxisome-deficient disorders.

【 授权许可】

Unknown