Database : MEDLINE
Search on : Renal and Aminoacidurias [Words]
References found : 532 [refine]
Displaying: 1 .. 10   in format [Detailed]

page 1 of 54 go to page                         

  1 / 532 MEDLINE  
              next record last record
select
to print
Photocopy
Full text

[PMID]: 26563427
[Au] Autor:Jackson CB; Bauer MF; Schaller A; Kotzaeridou U; Ferrarini A; Hahn D; Chehade H; Barbey F; Tran C; Gallati S; Haeberli A; Eggimann S; Bonafé L; Nuoffer JM
[Ad] Address:Institute of Clinical Chemistry, University Hospital Berne, Berne, Switzerland. christopher.jackson@helsinki.fi.
[Ti] Title:A novel mutation in BCS1L associated with deafness, tubulopathy, growth retardation and microcephaly.
[So] Source:Eur J Pediatr;175(4):517-25, 2016 Apr.
[Is] ISSN:1432-1076
[Cp] Country of publication:Germany
[La] Language:eng
[Ab] Abstract:UNLABELLED: We report a novel homozygous missense mutation in the ubiquinol-cytochrome c reductase synthesis-like (BCS1L) gene in two consanguineous Turkish families associated with deafness, Fanconi syndrome (tubulopathy), microcephaly, mental and growth retardation. All three patients presented with transitory metabolic acidosis in the neonatal period and development of persistent renal de Toni-Debré-Fanconi-type tubulopathy, with subsequent rachitis, short stature, microcephaly, sensorineural hearing impairment, mild mental retardation and liver dysfunction. The novel missense mutation c.142A>G (p.M48V) in BCS1L is located at a highly conserved region associated with sorting to the mitochondria. Biochemical analysis revealed an isolated complex III deficiency in skeletal muscle not detected in fibroblasts. Native polyacrylamide gel electrophoresis (PAGE) revealed normal super complex formation, but a shift in mobility of complex III most likely caused by the absence of the BCS1L-mediated insertion of Rieske Fe/S protein into complex III. These findings expand the phenotypic spectrum of BCS1L mutations, highlight the importance of biochemical analysis of different primary affected tissue and underline that neonatal lactic acidosis with multi-organ involvement may resolve after the newborn period with a relatively spared neurological outcome and survival into adulthood. CONCLUSION: Mutation screening for BCS1L should be considered in the differential diagnosis of severe (proximal) tubulopathy in the newborn period. WHAT IS KNOWN: • Mutations in BCS1L cause mitochondrial complex III deficiencies. • Phenotypic presentations of defective BCS1L range from Bjornstad to neonatal GRACILE syndrome. What is New: • Description of a novel homozygous mutation in BCS1L with transient neonatal acidosis and persistent de Toni-Debré-Fanconi-type tubulopathy. • The long survival of patients with phenotypic presentation of severe complex III deficiency is uncommon.
[Mh] MeSH terms primary: Acidosis, Lactic/genetics
Cholestasis/genetics
Deafness/genetics
Electron Transport Complex III/deficiency
Fanconi Syndrome/genetics
Fetal Growth Retardation/genetics
Hemosiderosis/genetics
Metabolism, Inborn Errors/genetics
Microcephaly/genetics
Mitochondrial Diseases/congenital
Renal Aminoacidurias/genetics
[Mh] MeSH terms secundary: ATPases Associated with Diverse Cellular Activities
Adolescent
Adult
Blotting, Western
Diagnosis, Differential
Electron Transport Complex III/genetics
Electrophoresis, Polyacrylamide Gel
Fanconi Syndrome/etiology
Female
Growth Disorders/genetics
Homozygote
Humans
Infant, Newborn
Intellectual Disability/genetics
Male
Mitochondrial Diseases/genetics
Mutation, Missense
[Pt] Publication type:CASE REPORTS; JOURNAL ARTICLE
[Nm] Name of substance:0 (BCS1L protein, human); EC 1.10.2.2 (Electron Transport Complex III); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities)
[Em] Entry month:1612
[Cu] Class update date: 171116
[Lr] Last revision date:171116
[Js] Journal subset:IM
[Da] Date of entry for processing:151114
[St] Status:MEDLINE
[do] DOI:10.1007/s00431-015-2661-y

  2 / 532 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 25618772
[Au] Autor:Chesney RW
[Ad] Address:Department of Pediatrics, The University of Tennessee Health Science Center, and the Children's Foundation Research Institute at Le Bonheur Children's Hospital, Memphis, TN, USA. rchesney@uthsc.edu.
[Ti] Title:Interactions of vitamin D and the proximal tubule.
[So] Source:Pediatr Nephrol;31(1):7-14, 2016 Jan.
[Is] ISSN:1432-198X
[Cp] Country of publication:Germany
[La] Language:eng
[Ab] Abstract:Severe vitamin D deficiency (reduction in serum 25(OH)D concentration) in infants and children can cause features of the Fanconi syndrome, including phosphaturia, glycosuria, aminoaciduria, and renal tubular acidosis. This indicates that vitamin D and its metabolites influence proximal tubule function. Filtered 25(OH)D bound to vitamin D binding protein (DBP) is endocytosed by megalin-cubilin in the apical membrane. Intracellular 25(OH)D is metabolized to 1,25(OH)2D or calcitroic acid by 1-α-hydroxylase or 24-hydroxylase in tubule cell mitochondria. Bone-produced fibroblast growth factor 23 (FGF23) bound to Klotho in tubule cells and intracellular phosphate concentrations are regulators of 1-α-hydroxylase activity and cause proximal tubule phosphaturia. Aminoaciduria occurs when amino acid transporter synthesis is deficient, and 1,25(OH)2D along with retinoic acid up-regulate transporter synthesis by a vitamin D response element in the promoter region of the transporter gene. This review discusses evidence gained from studies in animals or cell lines, as well as from human disorders, that provide insight into vitamin D-proximal tubule interactions.
[Mh] MeSH terms primary: Kidney Tubules, Proximal/metabolism
Renal Aminoacidurias/etiology
Vitamin D Deficiency/complications
Vitamin D/metabolism
[Mh] MeSH terms secundary: 25-Hydroxyvitamin D3 1-alpha-Hydroxylase/genetics
25-Hydroxyvitamin D3 1-alpha-Hydroxylase/metabolism
Animals
Genetic Predisposition to Disease
Humans
Kidney Tubules, Proximal/physiopathology
Low Density Lipoprotein Receptor-Related Protein-2/genetics
Low Density Lipoprotein Receptor-Related Protein-2/metabolism
Prognosis
Receptors, Calcitriol/genetics
Receptors, Calcitriol/metabolism
Receptors, Cell Surface/genetics
Receptors, Cell Surface/metabolism
Renal Aminoacidurias/genetics
Renal Aminoacidurias/metabolism
Renal Aminoacidurias/physiopathology
Risk Factors
Signal Transduction
Vitamin D Deficiency/genetics
Vitamin D Deficiency/metabolism
Vitamin D Deficiency/physiopathology
Vitamin D3 24-Hydroxylase/genetics
Vitamin D3 24-Hydroxylase/metabolism
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (LRP2 protein, human); 0 (Low Density Lipoprotein Receptor-Related Protein-2); 0 (Receptors, Calcitriol); 0 (Receptors, Cell Surface); 0 (VDR protein, human); 0 (intrinsic factor-cobalamin receptor); 1406-16-2 (Vitamin D); EC 1.14.13.13 (25-Hydroxyvitamin D3 1-alpha-Hydroxylase); EC 1.14.13.13 (CYP27B1 protein, human); EC 1.14.15.16 (CYP24A1 protein, human); EC 1.14.15.16 (Vitamin D3 24-Hydroxylase)
[Em] Entry month:1608
[Cu] Class update date: 171010
[Lr] Last revision date:171010
[Js] Journal subset:IM
[Da] Date of entry for processing:150126
[St] Status:MEDLINE
[do] DOI:10.1007/s00467-015-3050-5

  3 / 532 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
PubMed Central Full text
Full text

[PMID]: 26076823
[Au] Autor:Kovacevic L; Lu H; Goldfarb DS; Lakshmanan Y; Caruso JA
[Ad] Address:Department of Pediatric Urology, Children's Hospital of Michigan, Detroit, MI, USA. Electronic address: lkovacev@dmc.org.
[Ti] Title:Urine proteomic analysis in cystinuric children with renal stones.
[So] Source:J Pediatr Urol;11(4):217.e1-6, 2015 Aug.
[Is] ISSN:1873-4898
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:INTRODUCTION: The gene mutations responsible for cystinuria do not fully explain kidney stone activity, suggesting that specific proteins may serve as promoters of cystine precipitation, aggregation or epithelial adherence. In this study we assessed (1) the differences in the urinary proteins between children with cystinuria and kidney stones (CYS) and healthy controls (HC), with particular attention to the fibrosis-related proteins, and (2) the presence of diagnostic biomarkers for CYS. MATERIAL AND METHODS: We conducted a pilot study comparing individual urinary proteomes of 2 newly diagnosed children with CYS and 2 age- and gender-matched HC, using liquid chromatography-mass spectrometry. Relative protein abundance was estimated using spectral counting. Proteins of interest in both CYS and HC were selected using the following criteria: i) ≥5 spectral counts; ii) ≥2-fold difference in spectral counts; and iii) ≤0.05 p-value for the Fisher's Exact Test. DISCUSSION: This study demonstrates a different urinary polypeptide profile in two children with CYS compared to two HC. Of the 623 proteins identified by proteomic analysis, 180 exhibited at least a 2-fold increased relative abundance in CYS compared to HC. Of these, 39 were involved in response to stress, 26 in response to wounding, 21 in inflammatory response, 18 in immune response, and 4 in cellular response to oxidative stress. 133 proteins were found only in children with CYS, 33 of which met the selection criteria. Of these 33 unique proteins, six are known to be associated with fibrosis pathways (Table). The major limitation of this study is the small number of samples that were analyzed. Validation using highly specific methods such as ELISA is needed. CONCLUSION: We provide proteomic evidence of oxidative injury, inflammation, wound healing and fibrosis in two children with CYS. We speculate that oxidative stress and inflammation may cause remodeling via actin and vimentin pathways, leading to fibrosis. Additionally, we identified ITIH and MMP-9 as potential diagnostic biomarkers and novel therapeutic targets in CYS. These proteins merit further investigation.
[Mh] MeSH terms primary: Biomarkers/urine
Cystinuria/urine
Kidney Calculi/urine
Proteomics/methods
[Mh] MeSH terms secundary: Adolescent
Child
Chromatography, Liquid
Cystinuria/complications
Female
Humans
Kidney Calculi/complications
Mass Spectrometry
Pilot Projects
Urinalysis
[Pt] Publication type:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Name of substance:0 (Biomarkers)
[Em] Entry month:1605
[Cu] Class update date: 170220
[Lr] Last revision date:170220
[Js] Journal subset:IM
[Da] Date of entry for processing:150617
[St] Status:MEDLINE

  4 / 532 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
PubMed Central Full text
Full text

[PMID]: 25564041
[Au] Autor:Desbats MA; Vetro A; Limongelli I; Lunardi G; Casarin A; Doimo M; Spinazzi M; Angelini C; Cenacchi G; Burlina A; Rodriguez Hernandez MA; Chiandetti L; Clementi M; Trevisson E; Navas P; Zuffardi O; Salviati L
[Ad] Address:1] Clinical Genetics Unit, Department of Woman and Child Health, University of Padova, Padova, Italy [2] IRP Città della Speranza, Padova, Italy.
[Ti] Title:Primary coenzyme Q10 deficiency presenting as fatal neonatal multiorgan failure.
[So] Source:Eur J Hum Genet;23(9):1254-8, 2015 Sep.
[Is] ISSN:1476-5438
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Coenzyme Q10 deficiency is a clinically and genetically heterogeneous disorder, with manifestations that may range from fatal neonatal multisystem failure, to adult-onset encephalopathy. We report a patient who presented at birth with severe lactic acidosis, proteinuria, dicarboxylic aciduria, and hepatic insufficiency. She also had dilation of left ventricle on echocardiography. Her neurological condition rapidly worsened and despite aggressive care she died at 23 h of life. Muscle histology displayed lipid accumulation. Electron microscopy showed markedly swollen mitochondria with fragmented cristae. Respiratory-chain enzymatic assays showed a reduction of combined activities of complex I+III and II+III with normal activities of isolated complexes. The defect was confirmed in fibroblasts, where it could be rescued by supplementing the culture medium with 10 µM coenzyme Q10. Coenzyme Q10 levels were reduced (28% of controls) in these cells. We performed exome sequencing and focused the analysis on genes involved in coenzyme Q10 biosynthesis. The patient harbored a homozygous c.545T>G, p.(Met182Arg) alteration in COQ2, which was validated by functional complementation in yeast. In this case the biochemical and morphological features were essential to direct the genetic diagnosis. The parents had another pregnancy after the biochemical diagnosis was established, but before the identification of the genetic defect. Because of the potentially high recurrence risk, and given the importance of early CoQ10 supplementation, we decided to treat with CoQ10 the newborn child pending the results of the biochemical assays. Clinicians should consider a similar management in siblings of patients with CoQ10 deficiency without a genetic diagnosis.
[Mh] MeSH terms primary: Alkyl and Aryl Transferases/genetics
Ataxia/diagnosis
Ataxia/genetics
Mitochondria, Muscle/genetics
Mitochondrial Diseases/diagnosis
Mitochondrial Diseases/genetics
Muscle Weakness/diagnosis
Muscle Weakness/genetics
Point Mutation
Ubiquinone/analogs & derivatives
Ubiquinone/deficiency
[Mh] MeSH terms secundary: Acidosis, Lactic/blood
Acidosis, Lactic/genetics
Acidosis, Lactic/pathology
Alkyl and Aryl Transferases/deficiency
Ataxia/blood
Ataxia/pathology
Consanguinity
Fatal Outcome
Female
Gene Expression
Hepatic Insufficiency/blood
Hepatic Insufficiency/genetics
Hepatic Insufficiency/pathology
Humans
Infant, Newborn
Intellectual Disability/blood
Intellectual Disability/genetics
Intellectual Disability/pathology
Mitochondria, Muscle/enzymology
Mitochondria, Muscle/pathology
Mitochondrial Diseases/blood
Mitochondrial Diseases/pathology
Muscle Weakness/blood
Muscle Weakness/pathology
Muscle, Skeletal/enzymology
Muscle, Skeletal/pathology
Proteinuria/blood
Proteinuria/genetics
Proteinuria/pathology
Renal Aminoacidurias/blood
Renal Aminoacidurias/genetics
Renal Aminoacidurias/pathology
Sequence Analysis, DNA
Ubiquinone/blood
Ubiquinone/genetics
[Pt] Publication type:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:1339-63-5 (Ubiquinone); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.- (4-hydroxybenzoate polyprenyltransferase); EJ27X76M46 (coenzyme Q10)
[Em] Entry month:1605
[Cu] Class update date: 170922
[Lr] Last revision date:170922
[Js] Journal subset:IM
[Da] Date of entry for processing:150108
[St] Status:MEDLINE
[do] DOI:10.1038/ejhg.2014.277

  5 / 532 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
PubMed Central Full text
Full text

[PMID]: 25299125
[Au] Autor:Meury M; Costa M; Harder D; Stauffer M; Jeckelmann JM; Brühlmann B; Rosell A; Ilgü H; Kovar K; Palacín M; Fotiadis D
[Ad] Address:Institute of Biochemistry and Molecular Medicine, and Swiss National Centre of Competence in Research (NCCR) TransCure, University of Bern, Bern, Switzerland.
[Ti] Title:Detergent-induced stabilization and improved 3D map of the human heteromeric amino acid transporter 4F2hc-LAT2.
[So] Source:PLoS One;9(10):e109882, 2014.
[Is] ISSN:1932-6203
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Human heteromeric amino acid transporters (HATs) are membrane protein complexes that facilitate the transport of specific amino acids across cell membranes. Loss of function or overexpression of these transporters is implicated in several human diseases such as renal aminoacidurias and cancer. HATs are composed of two subunits, a heavy and a light subunit, that are covalently connected by a disulphide bridge. Light subunits catalyse amino acid transport and consist of twelve transmembrane α-helix domains. Heavy subunits are type II membrane N-glycoproteins with a large extracellular domain and are involved in the trafficking of the complex to the plasma membrane. Structural information on HATs is scarce because of the difficulty in heterologous overexpression. Recently, we had a major breakthrough with the overexpression of a recombinant HAT, 4F2hc-LAT2, in the methylotrophic yeast Pichia pastoris. Microgram amounts of purified protein made possible the reconstruction of the first 3D map of a human HAT by negative-stain transmission electron microscopy. Here we report the important stabilization of purified human 4F2hc-LAT2 using a combination of two detergents, i.e., n-dodecyl-ß-D-maltopyranoside and lauryl maltose neopentyl glycol, and cholesteryl hemisuccinate. The superior quality and stability of purified 4F2hc-LAT2 allowed the measurement of substrate binding by scintillation proximity assay. In addition, an improved 3D map of this HAT could be obtained. The detergent-induced stabilization of the purified human 4F2hc-LAT2 complex presented here paves the way towards its crystallization and structure determination at high-resolution, and thus the elucidation of the working mechanism of this important protein complex at the molecular level.
[Mh] MeSH terms primary: Adaptor Proteins, Signal Transducing/isolation & purification
Amino Acid Transport Systems/isolation & purification
Fusion Regulatory Protein 1, Heavy Chain/isolation & purification
Recombinant Proteins/isolation & purification
[Mh] MeSH terms secundary: Adaptor Proteins, Signal Transducing/chemistry
Adaptor Proteins, Signal Transducing/metabolism
Amino Acid Transport Systems/chemistry
Amino Acid Transport Systems/metabolism
Amino Acids/chemistry
Amino Acids/metabolism
Detergents/pharmacology
Fusion Regulatory Protein 1, Heavy Chain/chemistry
Fusion Regulatory Protein 1, Heavy Chain/metabolism
Humans
Maltose/analogs & derivatives
Maltose/pharmacology
Multiprotein Complexes/chemistry
Multiprotein Complexes/isolation & purification
Pichia
Protein Stability/drug effects
Recombinant Proteins/drug effects
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Adaptor Proteins, Signal Transducing); 0 (Amino Acid Transport Systems); 0 (Amino Acids); 0 (Detergents); 0 (Fusion Regulatory Protein 1, Heavy Chain); 0 (LAT2 protein, human); 0 (Multiprotein Complexes); 0 (Recombinant Proteins); 0 (dodecyl maltopyranoside); 69-79-4 (Maltose)
[Em] Entry month:1512
[Cu] Class update date: 171116
[Lr] Last revision date:171116
[Js] Journal subset:IM
[Da] Date of entry for processing:141010
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0109882

  6 / 532 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 24761004
[Au] Autor:Akahoshi N; Kamata S; Kubota M; Hishiki T; Nagahata Y; Matsuura T; Yamazaki C; Yoshida Y; Yamada H; Ishizaki Y; Suematsu M; Kasahara T; Ishii I
[Ad] Address:Department of Molecular and Cellular Neurobiology, Gunma University Graduate School of Medicine, Gunma, Japan; Japan Science and Technology Agency (JST), Exploratory Research for Advanced Technology (ERATO), Suematsu Gas Biology Project, Tokyo, Japan; Department of Immunology, Akita University Gradu
[Ti] Title:Neutral aminoaciduria in cystathionine ß-synthase-deficient mice; an animal model of homocystinuria.
[So] Source:Am J Physiol Renal Physiol;306(12):F1462-76, 2014 Jun 15.
[Is] ISSN:1522-1466
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The kidney is one of the major loci for the expression of cystathionine ß-synthase (CBS) and cystathionine γ-lyase (CTH). While CBS-deficient (Cbs(-/-)) mice display homocysteinemia/methioninemia and severe growth retardation, and rarely survive beyond the first 4 wk, CTH-deficient (Cth(-/-)) mice show homocysteinemia/cystathioninemia but develop with no apparent abnormality. This study examined renal amino acid reabsorption in those mice. Although both 2-wk-old Cbs(-/-) and Cth(-/-) mice had normal renal architecture, their serum/urinary amino acid profiles largely differed from wild-type mice. The most striking feature was marked accumulation of Met and cystathionine in serum/urine/kidney samples of Cbs(-/-) and Cth(-/-) mice, respectively. Levels of some neutral amino acids (Val, Leu, Ile, and Tyr) that were not elevated in Cbs(-/-) serum were highly elevated in Cbs(-/-) urine, and urinary excretion of other neutral amino acids (except Met) was much higher than expected from their serum levels, demonstrating neutral aminoaciduria in Cbs(-/-) (not Cth(-/-)) mice. Because the bulk of neutral amino acids is absorbed via a B(0)AT1 transporter and Met has the highest substrate affinity for B(0)AT1 than other neutral amino acids, hypermethioninemia may cause hyperexcretion of neutral amino acids.
[Mh] MeSH terms primary: Amino Acids, Neutral/metabolism
Cystathionine beta-Synthase/deficiency
Homocystinuria/epidemiology
Homocystinuria/metabolism
Renal Aminoacidurias/epidemiology
Renal Aminoacidurias/metabolism
[Mh] MeSH terms secundary: Animals
Comorbidity
Cystathionine/metabolism
Cystathionine beta-Synthase/genetics
Cystathionine beta-Synthase/metabolism
Cystathionine gamma-Lyase/deficiency
Cystathionine gamma-Lyase/genetics
Disease Models, Animal
Female
Hyperhomocysteinemia/metabolism
Kidney Tubules, Proximal/pathology
Male
Methionine/metabolism
Mice
Mice, Inbred C57BL
Mice, Knockout
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Amino Acids, Neutral); 375YFJ481O (Cystathionine); AE28F7PNPL (Methionine); EC 4.2.1.22 (Cystathionine beta-Synthase); EC 4.4.1.1 (Cystathionine gamma-Lyase)
[Em] Entry month:1409
[Cu] Class update date: 140616
[Lr] Last revision date:140616
[Js] Journal subset:IM
[Da] Date of entry for processing:140425
[St] Status:MEDLINE
[do] DOI:10.1152/ajprenal.00623.2013

  7 / 532 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 24692143
[Au] Autor:Makrides V; Camargo SM; Verrey F
[Ti] Title:Transport of amino acids in the kidney.
[So] Source:Compr Physiol;4(1):367-403, 2014 Jan.
[Is] ISSN:2040-4603
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Amino acids are the building blocks of proteins and key intermediates in the synthesis of biologically important molecules, as well as energy sources, neurotransmitters, regulators of cellular metabolism, etc. The efficient recovery of amino acids from the primary filtrate is a well-conserved key role of the kidney proximal tubule. Additionally, renal metabolism participates in the whole body disposition of amino acids. Therefore, a wide array of axially heterogeneously expressed transporters is localized on both epithelial membranes. For transepithelial transport, luminal uptake, which is carried out mainly by active symporters, is coupled with a mostly passive basolateral efflux. Many transporters require partner proteins for appropriate localization, or to modulate transporter activity, and/or increase substrate supply. Interacting proteins include cell surface antigens (CD98), endoplasmic reticulum proteins (GTRAP3-18 or 41), or enzymes (ACE2 and aminopeptidase N). In the past two decades, the molecular identification of transporters has led to significant advances in our understanding of amino acid transport and aminoacidurias arising from defects in renal transport. Furthermore, the three-dimensional crystal structures of bacterial homologues have been used to yield new insights on the structure and function of mammalian transporters. Additionally, transgenic animal models have contributed to our understanding of the role of amino acid transporters in the kidney and other organs and/or at critical developmental stages. Progress in elucidation of the renal contribution to systemic amino acid homeostasis requires further integration of kinetic, regulatory, and expression data of amino acid transporters into our understanding of physiological regulatory networks controlling metabolism.
[Mh] MeSH terms primary: Amino Acids/metabolism
Kidney/metabolism
[Mh] MeSH terms secundary: Amino Acid Transport Systems/physiology
Animals
Animals, Genetically Modified
Biological Transport/physiology
Extracellular Space/metabolism
Homeostasis/physiology
Humans
Kidney Tubules, Proximal/metabolism
Structure-Activity Relationship
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Name of substance:0 (Amino Acid Transport Systems); 0 (Amino Acids)
[Em] Entry month:1412
[Cu] Class update date: 140402
[Lr] Last revision date:140402
[Js] Journal subset:IM
[Da] Date of entry for processing:140403
[St] Status:MEDLINE
[do] DOI:10.1002/cphy.c130028

  8 / 532 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 24655110
[Au] Autor:Kasapkara ÇS; Tümer L; Ezgü FS; Küçükçongar A; Hasanoglu A
[Ad] Address:Department of Pediatric Metabolism and Nutrition, Gazi University Hospital , Ankara , Turkey.
[Ti] Title:BCS1L gene mutation causing GRACILE syndrome: case report.
[So] Source:Ren Fail;36(6):953-4, 2014 Jul.
[Is] ISSN:1525-6049
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:GRACILE syndrome is a rare autosomal recessive disease characterized by fetal growth retardation, Fanconi type aminoaciduria, cholestasis, iron overload, profound lactic acidosis, and early death. It is caused by homozygosity for a missense mutation in the BCS1L gene. The BCS1L gene encodes a chaperone responsible for assembly of respiratory chain complex III. Here we report that a homozygous mutation c.296C > T (p.P99L), in the first exon of BCS1L gene found in an affected 2-month-old boy of asymptomatic consanguineous parents results in GRACILE syndrome. This genotype is associated with a severe clinical presentation. So far no available treatments have changed the fatal course of the disease, and the metabolic disturbance responsible is still not clearly identified. Therefore, providing prenatal diagnosis in families with previous affected infants is of major importance. Mitochondrial disorders are an extremely heterogeneous group of diseases sharing, in common, the fact that they all ultimately impair the function of the mitochondrial respiratory chain. A clinical picture with fetal growth restriction, postnatal lactacidosis, aminoaciduria, hypoglycemia, coagulopathy, elevated liver enzymes, and cholestasis should direct investigations on mitochondrial disorder.
[Mh] MeSH terms primary: Acidosis, Lactic/genetics
Cholestasis/genetics
Electron Transport Complex III/genetics
Fetal Growth Retardation/genetics
Hemosiderosis/genetics
Metabolism, Inborn Errors/genetics
Mitochondrial Diseases/congenital
Renal Aminoacidurias/genetics
[Mh] MeSH terms secundary: ATPases Associated with Diverse Cellular Activities
Humans
Infant
Male
Mitochondrial Diseases/genetics
Mutation, Missense
[Pt] Publication type:CASE REPORTS; JOURNAL ARTICLE
[Nm] Name of substance:0 (BCS1L protein, human); EC 1.10.2.2 (Electron Transport Complex III); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities)
[Em] Entry month:1503
[Cu] Class update date: 171116
[Lr] Last revision date:171116
[Js] Journal subset:IM
[Da] Date of entry for processing:140325
[St] Status:MEDLINE
[do] DOI:10.3109/0886022X.2014.900422

  9 / 532 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 23506863
[Au] Autor:Fotiadis D; Kanai Y; Palacín M
[Ad] Address:Institute of Biochemistry and Molecular Medicine, and Swiss National Centre of Competence in Research TransCure, University of Bern, CH-3012 Bern, Switzerland.
[Ti] Title:The SLC3 and SLC7 families of amino acid transporters.
[So] Source:Mol Aspects Med;34(2-3):139-58, 2013 Apr-Jun.
[Is] ISSN:1872-9452
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Amino acids are necessary for all living cells and organisms. Specialized transporters mediate the transfer of amino acids across plasma membranes. Malfunction of these proteins can affect whole-body homoeostasis giving raise to diverse human diseases. Here, we review the main features of the SLC3 and SLC7 families of amino acid transporters. The SLC7 family is divided into two subfamilies, the cationic amino acid transporters (CATs), and the L-type amino acid transporters (LATs). The latter are the light or catalytic subunits of the heteromeric amino acid transporters (HATs), which are associated by a disulfide bridge with the heavy subunits 4F2hc or rBAT. These two subunits are glycoproteins and form the SLC3 family. Most CAT subfamily members were functionally characterized and shown to function as facilitated diffusers mediating the entry and efflux of cationic amino acids. In certain cells, CATs play an important role in the delivery of L-arginine for the synthesis of nitric oxide. HATs are mostly exchangers with a broad spectrum of substrates and are crucial in renal and intestinal re-absorption and cell redox balance. Furthermore, the role of the HAT 4F2hc/LAT1 in tumor growth and the application of LAT1 inhibitors and PET tracers for reduction of tumor progression and imaging of tumors are discussed. Finally, we describe the link between specific mutations in HATs and the primary inherited aminoacidurias, cystinuria and lysinuric protein intolerance.
[Mh] MeSH terms primary: Amino Acid Transport Systems, Basic/genetics
Amino Acid Transport Systems, Basic/physiology
Amino Acid Transport Systems, Neutral/genetics
Amino Acid Transport Systems, Neutral/physiology
Models, Biological
Models, Molecular
Multigene Family/genetics
Neoplasms/metabolism
[Mh] MeSH terms secundary: Amino Acid Transport Systems, Basic/metabolism
Amino Acid Transport Systems, Neutral/metabolism
Biological Transport/physiology
Humans
Phylogeny
Protein Conformation
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Name of substance:0 (Amino Acid Transport Systems, Basic); 0 (Amino Acid Transport Systems, Neutral)
[Em] Entry month:1309
[Cu] Class update date: 130319
[Lr] Last revision date:130319
[Js] Journal subset:IM
[Da] Date of entry for processing:130320
[St] Status:MEDLINE

  10 / 532 MEDLINE  
              first record previous record
select
to print
Photocopy
Full text

[PMID]: 22991165
[Au] Autor:Al-Owain M; Colak D; Albakheet A; Al-Younes B; Al-Humaidi Z; Al-Sayed M; Al-Hindi H; Al-Sugair A; Al-Muhaideb A; Rahbeeni Z; Al-Sehli A; Al-Fadhli F; Ozand PT; Taylor RW; Kaya N
[Ad] Address:Department of Medical Genetics, King Faisal Specialist Hospital and Research Center, Riyadh, Saudi Arabia.
[Ti] Title:Clinical and biochemical features associated with BCS1L mutation.
[So] Source:J Inherit Metab Dis;36(5):813-20, 2013 Sep.
[Is] ISSN:1573-2665
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Our study describes a novel phenotype in a series of nine Saudi patients with lactic acidosis, from four consanguineous families three of which are related. Detailed genetic studies including linkage, homozygosity mapping and targeted sequencing identified a causative mutation in the BCS1L gene. All affected members of the families have an identical mutation in this gene, mutations of which are recognized causes of Björnstad syndrome, GRACILE syndrome and a syndrome of neonatal tubulopathy, encephalopathy, and liver failure (MIM 606104) leading to isolated mitochondrial respiratory chain complex III deficiency. Here we report the appearance of a novel behavioral (five patients) and psychiatric (two patients) phenotype associated with a p.Gly129Arg BCS1L mutation, differing from the phenotype in a previously reported singleton patient with this mutation. The psychiatric symptoms emanated after childhood, initially as hypomania later evolving into intermittent psychosis. Neuroradiological findings included subtle white matter abnormalities, whilst muscle histopathology and respiratory chain studies confirmed respiratory chain dysfunction. The variable neuro-psychiatric manifestations and cortical visual dysfunction are most unusual and not reported associated with other BCS1L mutations. This report emphasizes the clinical heterogeneity associated with the mutation in BCS1L gene, even within the same family and we recommend that defects in this gene should be considered in the differential diagnosis of lactic acidosis with variable involvement of different organs.
[Mh] MeSH terms primary: Acidosis, Lactic/genetics
Electron Transport Complex III/genetics
Mutation
[Mh] MeSH terms secundary: ATPases Associated with Diverse Cellular Activities
Acidosis, Lactic/metabolism
Adolescent
Adult
Child
Cholestasis/genetics
Cholestasis/metabolism
Electron Transport/genetics
Electron Transport Complex III/metabolism
Female
Fetal Growth Retardation/genetics
Fetal Growth Retardation/metabolism
Genetic Predisposition to Disease
Hair Diseases/genetics
Hair Diseases/metabolism
Hearing Loss, Sensorineural/genetics
Hearing Loss, Sensorineural/metabolism
Hemosiderosis/genetics
Hemosiderosis/metabolism
Homozygote
Humans
Male
Metabolism, Inborn Errors/genetics
Metabolism, Inborn Errors/metabolism
Mitochondrial Diseases/congenital
Mitochondrial Diseases/genetics
Mitochondrial Diseases/metabolism
Phenotype
Renal Aminoacidurias/genetics
Renal Aminoacidurias/metabolism
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (BCS1L protein, human); EC 1.10.2.2 (Electron Transport Complex III); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities)
[Em] Entry month:1405
[Cu] Class update date: 171116
[Lr] Last revision date:171116
[Js] Journal subset:IM
[Da] Date of entry for processing:120920
[St] Status:MEDLINE
[do] DOI:10.1007/s10545-012-9536-4


page 1 of 54 go to page                         
   


Refine the search
  Database : MEDLINE Advanced form   

    Search in field  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/PAHO/WHO - Latin American and Caribbean Center on Health Sciences Information