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001-es BibID:	BIBFORM038431
Első szerző:	Chioza, B. A.
Cím:	Mutations in the lysyl oxidase gene are not associated with amyotrophic lateral sclerosis / Chioza B. A., Ujfalusi A., Csiszár K., Leigh P. N., Powell J. F., Radunovic A.
Dátum:	2001
Megjegyzések:	BACKGROUND: There is an urgent need to identify genes involved in familial ALS (FALS), as mutations in the CuZn superoxide dismutase (SOD1) gene can account for 20% of FALS cases. The mechanisms by which the many mutations in the SOD1 gene lead to motoneuron degeneration are unknown, although current experimental evidence supports a toxic gain of function, possibly through copper-induced cytotoxicity. Copper is an integral component of a number of enzymes as well as SOD1. Since abnormalities in connective tissue cross-linking have been reported in ALS patients, an enzyme of possible relevance is lysyl oxidase (LOX), a copper-containing enzyme which catalyses the crosslinking of collagens and elastin. The aim of this study was to investigate the hypothesis that allelic variants or mutants of LOX gene result in altered function of LOX in ALS patients. METHODS: The coding regions of the LOX gene were screened for polymorphism and mutations in a cohort of sporadic and familial ALS patients. RESULTS: A novel polymorphism, Pro159Gln, was identified in eight individuals with sporadic ALS (5.0%) and five controls (3.6%). The previously identified Arg158Gln polymorphism was also detected in ALS patients and controls. These polymorphisms were genotyped in 192 ALS patients, including 31 unrelated familial cases and 138 controls, and no association was found between any of these polymorphisms and amyotrophic lateral sclerosis or its phenotype. CONCLUSION: Mutations in the LOX gene are unlikely to be directly causative of ALS.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Amyotrophic Lateral Sclerosis and Other Motor Neuron Disorders. - 2 : 2 (2001), p. 93-97. -
További szerzők:	Ujfalusi Anikó (1968-) (gyermekorvos, laboratóriumi szakorvos) Csiszár Katalin Leigh, P. Nigel Powell, J. F. Radunovic, A.
Internet cím:	Szerző által megadott URL Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM038428
Első szerző:	Csiszár Katalin
Cím:	Somatic mutations of the lysyl oxidase gene on chromosome 5q23.1 in colorectal tumors / Csiszar Katalin, Fong Sheri F. T., Ujfalusi Aniko, Krawetz Stephen A., Salvati Eugene P., Mackenzie James W., Boyd Charles D.
Dátum:	2002
ISSN:	0020-7136
Megjegyzések:	Lysyl oxidase (LOX), a copper-dependent amine oxidase, has been implicated in tumor suppression and cell growth regulation. The chromosomal locus of LOX, 5q23, is affected by loss of heterozygosity (LOH) in colon cancer, suggesting that the LOX gene could be affected by LOH and consequently, loss or reduction of LOX function contribute to the tumorigenic process. Identification of microsatellite markers within the LOX locus has allowed us to map the LOX gene within the 5q23.1 region. Analysis of this locus and flanking loci in matched tumor and blood DNA samples from a panel of colorectal cancer patients, demonstrated that 38% (16/42) of informative samples were affected by LOH or allelic imbalance. Furthermore, 75% (6/8) of these tumor samples were shown to have significantly reduced LOX mRNA levels. Similar reduction in LOX levels were detected in a panel of matched normal colon and colon tumor samples. Tumor samples demonstrating LOH by RFLP, were subject to mutational analysis, including RT-PCR, exonic deletion detection by PCR, cDNA and genomic DNA sequencing, and were found to have a spectrum of alterations and mutations affecting the LOX gene. These results confirm that loss or reduction of LOX function during tumor development is a direct consequence of somatic mutations and is associated with colon tumor pathogenesis.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	International Journal Of Cancer. - 97 : 5 (2002), p. 636-642. -
További szerzők:	Fong, Sheri F. T. Ujfalusi Anikó (1968-) (gyermekorvos, laboratóriumi szakorvos) Krawetz, Stephen A. Salvati, Eugene P. Mackenzie, James W. Boyd, Charles D.
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM009566
Első szerző:	Jourdan-Le Saux, Claude
Cím:	Central nervous system, uterus, heart and leukocyte expression of the LOXL3 gene, encoding a novel lysyl oxidase-like protein / Jourdan-Le Saux C., Tomsche A., Ujfalusi A., Jia L., Csiszár K.
Dátum:	2001
Megjegyzések:	A BLASTN search using the mouse lor-2 cDNA identified three overlapping ESTs (AI752772, AA852888, and R55706) in the GenBank database. These expressed sequence tags were assembled into a contig of 3121 nucleotides with an open reading frame of 2262 bp. The encoded putative polypeptide of 754 amino acids presented all structural characteristics of the lysyl oxidase (LOX) enzyme family, a copper-binding site with four histidyl residues, the lysyl and tyrosyl residues known to be involved in LOX enzyme in the formation of the quinone cofactor and surrounding sequences, and the cytokine receptor-like domain. In addition, four scavenger receptor cysteine-rich (SRCR) domains were found in the N-terminal region of the protein. The gene encoding this new cDNA, which we have referred to as human lysyl oxidase-like 3 (humanLOXL3), has been mapped to chromosome 2p13.3, overlapping at its 3' end the HtrA2 serine protease gene. The structure of the humanLOXL3 gene was deduced from the BAC clone bac91a19 sequence and contained 14 exons. The expression pattern of this new member of the LOX gene family appears to be different from that of the LOX and LOX-like genes, as the central nervous system, neurons, and also leukocytes expressed humanLOXL3. A BLASTN search of the human EST database indicated the presence of ESTs, corresponding to alternative splice variants of LOXL3, that lacked exon 5 and exon 8. The putative resulting protein retained the region encoding the structural and functional elements of the amine oxidase but the second and fourth SRCR domains were truncated and the potential BMP-1 cleavage site was not present. The presence of domains unrelated to the traditional amine oxidase activity is a strong indication that humanLOXL3 might fulfill other functions in addition to intrinsic enzyme activity.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Genomics. - 74 : 2 (2001), p. 211-218. -
További szerzők:	Tomsche, Arianne Ujfalusi Anikó (1968-) (gyermekorvos, laboratóriumi szakorvos) Jia, Libin Csiszár Katalin
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001-es BibID:	BIBFORM009643
Első szerző:	Martins, R. P.
Cím:	Characterization of the region encompassing the human lysyl oxidase locus / Martins R. P., Ujfalusi A., Csiszár K., Krawetz S. A.
Dátum:	2001
Megjegyzések:	A 46,823 bp region of human chromosome 5q23.1 encompassing the seven-exon lysyl oxidase gene was characterized at the primary sequence level. Approximately 17.4% of this region is comprised of repetitive elements. The gene colocalizes with microsatellite marker D5S467. It is flanked by two candidate nuclear matrix association regions (MARs). The 5' MAR centered at position 12,500 is of the AT-rich and curved DNA class. This is followed by a large CpG island containing fifty-seven putative regulatory elements which extend from just upstream of exon 1 to intron 2. The larger 3' MAR, spans position 35,050-39,750 and is characterized by a TG-rich kinked structure that also contains a topoisomerase II binding site. Based on these results model of the transcriptional regulation of the lysy/oxidase gene is presented.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	DNA Sequence. - 12 : 4 (2001), p. 215-227. -
További szerzők:	Ujfalusi Anikó (1968-) (gyermekorvos, laboratóriumi szakorvos) Csiszár Katalin Krawetz, Stephen A.
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