Molecular basis of Refsum disease: Sequence variations in Phytanoyl-CoA Hydroxylase (PHYH) and the PTS2 receptor (PEX7)

2004 ◽  
Vol 23 (3) ◽  
pp. 209-218 ◽  
Author(s):  
Gerbert A. Jansen ◽  
Hans R. Waterham ◽  
Ronald J. A. Wanders
Keyword(s):  
Molecular Basis ◽  
Refsum Disease ◽  
Sequence Variations

Molecular basis of Refsum disease: Identification of new mutations in the phytanoyl-CoA hydroxylase cDNA

1998 ◽  
Vol 21 (3) ◽  
pp. 288-291 ◽  
Author(s):  
G. A. Jansen ◽  
S. Ferdinandusse ◽  
O. H. Skjeldal ◽  
O. Stokke ◽  
C. J. De Groot ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Refsum Disease ◽  
Disease Identification ◽  
New Mutations

scholarly journals Molecular Basis of Rifampin and Isoniazid Resistance in Mycobacterium bovis Strains Isolated in Sardinia, Italy

2001 ◽  
Vol 45 (6) ◽  
pp. 1645-1648 ◽  
Author(s):  
L. A. Sechi ◽  
S. Zanetti ◽  
M. Sanguinetti ◽  
P. Molicotti ◽  
L. Romano ◽  
...  
Keyword(s):  
Mycobacterium Bovis ◽  
Molecular Basis ◽  
Genetic Basis ◽  
Molecular Genetic ◽  
Geographic Area ◽  
Frequent Mutation ◽  
Isoniazid Resistance ◽  
Molecular Genetic Basis ◽  
Sequence Variations ◽  
Rifampin Resistance

ABSTRACT Fourteen of 22 (68%) Mycobacterium bovis strains isolated from cattle in Sardinia were found to be resistant to rifampin and isoniazid. Analysis of the rpoB and the katG, oxyR-ahpC, and inhA gene regions of these strains was performed in order to investigate the molecular basis of rifampin and isoniazid resistance, respectively. The most frequent mutation, encountered in 6 of 10 strains (60%), was in the rpoBgene; it occurred, at codon position 521 and resulted in leucine changed to proline. This suggests that codon 521 may be important for the development of rifampin resistance in M. bovis. Resistance to isoniazid is associated in Mycobacterium tuberculosis with a variety of mutations affecting one or more genes. Our results confirm the difficulty of interpreting the sequence variations observed in clinical strains of M. bovis. M. bovis strains isolated from the same geographic area showed similar mutations within the genes responsible for rifampin and isoniazid resistance. Our results represent the first study to elucidate the molecular genetic basis of drug resistance in M. bovis isolated from cattle.

Five Novel Mutations of the Protein S Active Gene (PROS 1) in 8 Norman Families

1996 ◽  
Vol 75 (03) ◽  
pp. 437-444 ◽  
Author(s):  
Jérôme Duchemin ◽  
Jeanne-Yvonne Borg ◽  
Delphine Borgel ◽  
Marc Vasse ◽  
Hervé Lévèque ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Molecular Basis ◽  
Protein S ◽  
Type I ◽  
Factor V ◽  
Novel Mutations ◽  
Nucleotide Deletion ◽  
Active Gene ◽  
Sequence Variations ◽  
Gradient Gel Electrophoresis

SummaryTo further elucidate the molecular basis for hereditary thrombophilia, we screened the protein S active gene in 11 families with type I deficiency, using a strategy based on denaturating gradient gel electrophoresis (DGGE) of all the coding sequences. Fragments with an abnormal DGGE pattern were sequenced, and 5 novel mutations were identified in 8 families. The mutations were a 7-nucleotide deletion in exon II, a 4-nucleotide deletion in exon III, a T insertion in exon VII, a C to T transition transforming Leu 259 into Pro and a T to C transition transforming Cys 625 into Arg in 4 families. These mutations were the only sequence variations found in the propositus’ gene exons and co-segregated with the plasma phenotype. A total of 28 members of these 8 families were heterozygous for one of the 5 mutations. Twenty-four (58,5%) of the 41 deficient subjects over 18 years of age had clinical thrombophilia, whereas the 13 subjects under 18 were asymptomatic. Of the 28 subjects, 6 (21,5%) were also found to bear the factor V Arg 506 Gin mutation.

Molecular basis of altered uracil catabolism in individuals with 5-FU toxicity and normal DPD enzyme activity

2006 ◽  
Vol 24 (18_suppl) ◽  
pp. 3070-3070
Author(s):  
H. A. Reed ◽  
H. H. Ezzeldin ◽  
L. K. Mattison ◽  
R. B. Diasio
Keyword(s):  
Enzyme Activity ◽  
Amino Acid ◽  
Cancer Patients ◽  
Molecular Analysis ◽  
Molecular Basis ◽  
Significant Group ◽  
Intronic Sequence ◽  
Molecular Defects ◽  
Sequence Variations ◽  
Number Of Patients

3070 Background: Dihydropyrimidine dehydrogenase (DPD) deficiency accounts for approximately 43% of grade 3–4 toxicity to 5-Fluorouracil (5-FU). However, a significant number of patients with normal DPD enzyme activity remain with unexplained molecular basis of 5-FU toxicity. It has been suggested by the few cases previously reported that deficiency of dihydropyrimidinase (DHP)enzyme encoded by the DPYS gene and/or beta-ureidopropionase enzyme, encoded by the BUP-1 gene, could also be implicated in 5-FU toxicity. Methods: This study included 40 volunteers with known 13C-UraBT and DPD enzyme activity, 25 cancer patients with 5-FU toxicity despite normal DPD enzyme activity, and 25 liver biopsies from cancer patients with different grades of toxicity. All samples were analyzed for molecular defects in the DPYS and BUP-1 genes, using DHPLC and RT-PCR techniques. Results: Molecular analysis of the DPYS gene revealed the presence of two non-conservative amino acid changes, one frame-shift mutation that leads to a stop codon and premature termination of the DHP protein, five silent mutations, nine intronic sequence variations, two sequence variations in the 5’UTR and one in the non-coding region of exon 10. Molecular analysis of the BUP-1 gene revealed the presence of two non-conservative amino acid changes, one of which (314C>A: A85E) has already been reported to abolish enzyme activity; six silent mutations, four intronic sequence variations, one polymorphism in the 5’upstream sequence, and one sequence variation in each of the 5’UTR and the 3’UTR. Conclusions: The molecular basis of 5-FU toxicity is not limited to DPD deficiency; since molecular defects in genes downstream of DPD can potentially also impair 5-FU catabolism. Genetic testing for molecular defects in DPYS and BUP-1 may predict patients at risk of developing 5-FU toxicity despite having normal DPD enzyme activity. Assessing the integrity of the entire uracil catabolic pathway might be crucial to avoid toxicity in a significant group of patients receiving 5-FU or a related drug (CA62164). No significant financial relationships to disclose.

Renilla Bioluminescence: A Morphologic Approach to the Location of Photocytes

1974 ◽  
Vol 32 ◽  
pp. 208-209
Author(s):  
Ben O. Spurlock ◽  
Milton J. Cormier
Keyword(s):  
Excited State ◽  
Ground State ◽  
Molecular Basis ◽  
Light Emission ◽  
Chemical Basis ◽  
Electronic Excited State ◽  
Colonial Form ◽  
The Common ◽  
Eighteenth And Nineteenth Centuries ◽  
Catalyzed Oxidation

The phenomenon of bioluminescence has fascinated layman and scientist alike for many centuries. During the eighteenth and nineteenth centuries a number of observations were reported on the physiology of bioluminescence in Renilla, the common sea pansy. More recently biochemists have directed their attention to the molecular basis of luminosity in this colonial form. These studies have centered primarily on defining the chemical basis for bioluminescence and its control. It is now established that bioluminescence in Renilla arises due to the luciferase-catalyzed oxidation of luciferin. This results in the creation of a product (oxyluciferin) in an electronic excited state. The transition of oxyluciferin from its excited state to the ground state leads to light emission.

Androgen-induced plasticity at a “vocal” neuromuscular synapse

1994 ◽  
Vol 52 ◽  
pp. 32-33
Author(s):  
Darcy B. Kelley ◽  
Martha L. Tobias ◽  
Mark Ellisman
Keyword(s):  
Xenopus Laevis ◽  
Motor Neurons ◽  
Sexual Differentiation ◽  
Molecular Basis ◽  
Neuromuscular Synapse ◽  
Sexually Dimorphic ◽  
Intracellular Protein ◽  
Developmental Program ◽  
Androgen Action ◽  
Clawed Frog

Brain and muscle are sexually differentiated tissues in which masculinization is controlled by the secretion of androgens from the testes. Sensitivity to androgen is conferred by the expression of an intracellular protein, the androgen receptor. A central problem of sexual differentiation is thus to understand the cellular and molecular basis of androgen action. We do not understand how hormone occupancy of a receptor translates into an alteration in the developmental program of the target cell. Our studies on sexual differentiation of brain and muscle in Xenopus laevis are designed to explore the molecular basis of androgen induced sexual differentiation by examining how this hormone controls the masculinization of brain and muscle targets.Our approach to this problem has focused on a highly androgen sensitive, sexually dimorphic neuromuscular system: laryngeal muscles and motor neurons of the clawed frog, Xenopus laevis. We have been studying sex differences at a synapse, the laryngeal neuromuscular junction, which mediates sexually dimorphic vocal behavior in Xenopus laevis frogs.

A molecular basis for opiate action

1998 ◽  
Vol 33 ◽  
pp. 65-77 ◽  
Author(s):  
Dominique Massotte ◽  
Brigitte L. Kieffer
Keyword(s):  
Molecular Basis

Emerging Nutrition Gaps in a World of Affluence - Micronutrient Intake and Status Globally

2011 ◽  
Vol 81 (4) ◽  
pp. 238-239 ◽  
Author(s):  
Manfred Eggersdorfer ◽  
Paul Walter
Keyword(s):  
Developing Countries ◽  
Human Health ◽  
Old Age ◽  
Molecular Basis ◽  
Health Benefit ◽  
Developed Countries ◽  
Micronutrient Deficiencies ◽  
New Science ◽  
Health And Nutrition ◽  
Micronutrient Intake

Nutrition is important for human health in all stages of life - from conception to old age. Today we know much more about the molecular basis of nutrition. Most importantly, we have learnt that micronutrients, among other factors, interact with genes, and new science is increasingly providing more tools to clarify this interrelation between health and nutrition. Sufficient intake of vitamins is essential to achieve maximum health benefit. It is well established that in developing countries, millions of people still suffer from micronutrient deficiencies. However, it is far less recognized that we face micronutrient insufficiencies also in developed countries.

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