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12 results on '"Lahiry, Piya"'

3. A novel ICK mutation causes ciliary disruption and lethal endocrine-cerebro-osteodysplasia syndrome

Author

Oud, Machteld M., primary, Bonnard, Carine, additional, Mans, Dorus A., additional, Altunoglu, Umut, additional, Tohari, Sumanty, additional, Ng, Alvin Yu Jin, additional, Eskin, Ascia, additional, Lee, Hane, additional, Rupar, C. Anthony, additional, de Wagenaar, Nathalie P., additional, Wu, Ka Man, additional, Lahiry, Piya, additional, Pazour, Gregory J., additional, Nelson, Stanley F., additional, Hegele, Robert A., additional, Roepman, Ronald, additional, Kayserili, Hülya, additional, Venkatesh, Byrappa, additional, Siu, Victoria M., additional, Reversade, Bruno, additional, and Arts, Heleen H., additional

Published
2016
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5. Kinase Mutations in Human Disease: Interpreting Genotype-phenotype Relationships

Author

Lahiry, Piya, Torkamani, Ali, Schork, Nicholas J., Hegele, Robert A., Lahiry, Piya, Torkamani, Ali, Schork, Nicholas J., and Hegele, Robert A.

Abstract

Protein kinases are one of the largest families of evolutionarily related proteins and comprise one of the most abundant gene families in humans. Here we survey kinase gene mutations from the perspective of human disease phenotypes and further analyse the structural features of mutant kinases, including mutational hotspots. Our evaluation of the genotype-phenotype relationship across 915 human kinase mutations - that underlie 67 single-gene diseases, mainly inherited developmental and metabolic disorders and also certain cancers - enhances our understanding of the role of kinases in development, kinase dysfunction in pathogenesis and kinases as potential targets for therapy.

Published
2010

11. APOC1T45S polymorphism is associated with reduced obesity indices and lower plasma concentrations of leptin and apolipoprotein C-I in aboriginal Canadians

Author

Lahiry, Piya, Cao, Henian, Ban, Matthew R., Pollex, Rebecca L., Mamakeesick, Mary, Zinman, Bernard, Harris, Stewart B., Hanley, Anthony J.G., Huff, Murray W., Connelly, Philip W., and Hegele, Robert A.

Abstract

Apolipoprotein (apo) C-I is a constituent of chylomicrons, very low density lipoprotein, and high density lipoprotein. The role of apo C-I in human metabolism is incompletely defined. We took advantage of a naturally occurring amino acid polymorphism that is present in aboriginal North Americans, namely apo C-I T45S. We assessed the hypothesis that metabolic traits, including obesity-related and lipoprotein-related traits, would differ between carriers and noncarriers of apo C-I T45S. A genotyping assay was developed for APOC1T45S and genotypes were determined in a sample of 410 Canadian Oji-Cree subjects. The allele frequency of the apo C-I S45 allele was ∼8% in this sample. We observed the apo C-I S45 allele was significantly associated with 1) lower percent body fat (P< 0.05), 2) lower waist circumference (P= 0.058), 3) lower serum leptin levels (P< 0.05), and 4) lower plasma apo C-I levels (P< 0.0001), using a newly developed ELISA-based method. Taken together, these results suggest that at the whole human phenotype level, apo C-I is associated with the complex metabolic trait of obesity as well as with serum leptin levels.

Published
2010
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12. Exome sequencing identifies NFS1 deficiency in a novel Fe-S cluster disease, infantile mitochondrial complex II/III deficiency.

Author

Farhan SM, Wang J, Robinson JF, Lahiry P, Siu VM, Prasad C, Kronick JB, Ramsay DA, Rupar CA, and Hegele RA

Abstract

Iron-sulfur (Fe-S) clusters are a class of highly conserved and ubiquitous prosthetic groups with unique chemical properties that allow the proteins that contain them, Fe-S proteins, to assist in various key biochemical pathways. Mutations in Fe-S proteins often disrupt Fe-S cluster assembly leading to a spectrum of severe disorders such as Friedreich's ataxia or iron-sulfur cluster assembly enzyme (ISCU) myopathy. Herein, we describe infantile mitochondrial complex II/III deficiency, a novel autosomal recessive mitochondrial disease characterized by lactic acidemia, hypotonia, respiratory chain complex II and III deficiency, multisystem organ failure and abnormal mitochondria. Through autozygosity mapping, exome sequencing, in silico analyses, population studies and functional tests, we identified c.215G>A, p.Arg72Gln in NFS1 as the likely causative mutation. We describe the first disease in man likely caused by deficiency in NFS1, a cysteine desulfurase that is implicated in respiratory chain function and iron maintenance by initiating Fe-S cluster biosynthesis. Our results further demonstrate the importance of sufficient NFS1 expression in human physiology.

Published
2014
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