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Lysinuric protein intolerance
Published in William L. Nyhan, Georg F. Hoffmann, Aida I. Al-Aqeel, Bruce A. Barshop, Atlas of Inherited Metabolic Diseases, 2020
William L. Nyhan, Georg F. Hoffmann, Aida I. Al-Aqeel, Bruce A. Barshop
Lysinuric protein intolerance (LPI) was first described by Perheentupa and Visakorpi [1] from Finland in 1965, in a report of three patients with familial intolerance to protein and abnormal transport of the basic amino acids. The disease is prevalent in Finland, where it has been estimated to occur in one in 60,000 [2], and Finns or Finnish Lapps have comprised nearly half of the patients reported [1–5]. Later, a similar cluster and incidence was identified in northern Japan [6]. However, the disease may be found in any ethnic population. The fundamental defect is an abnormality in the transport of basic amino acids in the basolateral or antiluminal membrane of epithelial cells (Figure 32.1) [7–9]. The abnormality is in the efflux of these amino acids and can be demonstrated in cultured fibroblasts [10, 11]. The gene for the transporter has been mapped to chromosome 14q11.2 [12]. Founder mutations, c.895-2A>T, a splice-site acceptor change leading to a frameshift and a premature termination, in the Finnish population [13] and R410X in Japan [6], were found in the SLC7A7 gene. Mutations in other populations are diverse, and more than 50 mutations have been found worldwide [14, 15].
Glutamine, Glutamate, and GABA in Human Diseases
Published in Elling Kvamme, Glutamine and Glutamate in Mammals, 1988
Glutamine concentrations in plasma and CSF, and glutamine content in the brain, are usually elevated, and sometimes very markedly so, in conditions where ammonia is no longer converted into urea (Table 2). These may result either from structural or biochemical failure in the liver or as a result of any of the six genetically determined metabolic defects in the urea cycle.18,19 In addition, plasma concentrations of glutamine are sometimes elevated in the autosomal recessive disorder lysinuric protein intolerance.18,20
Metabolomics reveals the renoprotective effect of n-butanol extract and amygdalin extract from Amygdalus mongolica in rats with renal fibrosis
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2021
Wanfu Bai, Qing Liu, Hong Chang, Quanli Liu, Chen Gao, Yingchun Bai, Hongbing Zhou, Songli Shi
Ornithine can improve athletic performance through anabolic and wound-healing effects, and it can enhance immune function in cells. L-Ornithine is located in the mitochondria and cytoplasm [28]. Moreover, ornithine is associated with cystinuria, hyperdibasic aminoaciduria, and lysinuric protein intolerance, which are genetic metabolic defects. Ornithine is produced in the urea cycle through the cleavage of urea from arginine [26]. L-Ornithine is also a precursor of proline, citrulline, and arginine. Proline is the elementary element of collagen tissue and can promote collagen synthesis and deposition at the lesion site. Ornithine metabolism is involved in the arginine biosynthesis pathway. Arginine biosynthesis may reduce renal tubular interstitial fibrosis and ameliorate renal function [29].
Pediatric bronchoscopy: recent advances and clinical challenges
Published in Expert Review of Respiratory Medicine, 2021
P Goussard, P Pohunek, E Eber, F Midulla, G Di Mattia, M Merven, JT Janson
The main indication for WLL are disorders associated with alveolar filling by abnormal material. The most frequent of these disorders is pulmonary alveolar proteinosis [180], but WLL has also been performed in children with metabolic disorders such as lysinuric protein intolerance [181], Niemann Pick disease [182], or lipoid pneumonia [183].