Biomedical subjects

B Galán

Publications and source records attributed to B Galán.

5 recordsLinked to original sources

PubMed2004

Discriminative capacity of calcaneal quantitative ultrasound and of osteoporosis and fracture risk factors in postmenopausal women with osteoporotic fractures.

Bone fragility fractures constitute the principal complication of osteoporosis. The identification of individuals at high risk of sustaining osteoporotic fractures is important for implementing preventive measures. The purpose of this study is to analyze the discriminative capacity of a series of osteoporosis and fracture risk factors, and of calcaneal quantitative ultrasound (QUS), in a population of postmenopausal women with a history of osteoporotic fracture. A cross-sectional analysis was made of a cohort of 5195 women aged 65 or older (mean +/- SD: 72.3 +/- 5.4 years) seen in 58 primary care centers in Spain. A total of 1042 women (20.1%) presented with a history of osteoporotic fracture. Most fractures (93%) were non-vertebral. Age-adjusted odds ratios corresponding to each decrease in one standard deviation of the different QUS parameters ranged from 1.47 to 1.55 (P < 0.001) for fractures. The age-adjusted multivariate analysis yielded the following risk factors independently associated with a history of osteoporotic fracture: number of fertile years, a family history of fracture, falls in the previous year, a history of chronic obstructive airway disease, the use of antiarrhythmic drugs, and a low value for any of the QUS parameters. The area under the receiver operating characteristic curve of the best model was 0.656. In summary, a series of easily assessable osteoporotic fracture risk factors has been identified. QUS was shown to discriminate between women with and without a history of fracture, and constitutes a useful tool for assessing fracture risk. Various of the vertebral and hip fracture risk factors frequently cited in North American and British populations showed no discriminative capacity in our series--thus suggesting that such factors may not be fully applicable to our population and/or to the predominant type of fractures included in the present study.

Aged↗

PubMed2000

Enhancing desulphurization by engineering a flavin reductase-encoding gene cassette in recombinant biocatalysts.

Biological desulphurization of petroleum feedstocks and products may offer an attractive alternative to reduce sulphur oxide emissions that cause serious environmental pollution. Dibenzothiophene (DBT) desulphurization via the Dsz pathway of Rhodococcus erythropolis IGTS8 is an energetically expensive process that consumes reducing equivalents. We have shown in this work that the HpaC oxidoreductase from Escherichia coli W is able to supply the required FMNH2 to the Dsz monooxygenases. The cloning and expression of the hpaC gene in Pseudomonas strains bearing the dszABC gene cluster significantly enhanced DBT desulphurization efficacy of the recombinant biocatalysts in a resting-cell process, thus indicating that overexpression of a heterologous flavin reductase in the host cell is critical for a high rate of sulphur removal in vivo. The hpaC and dszABC genes have been engineered as a single transcription unit under control of broadhost-range regulatory signals in a mobilizable DNA cassette that can be used to confer a DBT desulphurization phenotype to a wide variety of bacteria regardless of the expression of putative housekeeping flavin reductases within the host cells. This cassette will be very useful in exploring the biotechnological potential of novel biocatalysts for developing an efficient desulphurization process.

Air Pollutants↗

PubMed2000

Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: a prototype of a new Flavin:NAD(P)H reductase subfamily.

Escherichia coli W uses the aromatic compound 4-hydroxyphenylacetate (4-HPA) as a sole source of carbon and energy for growth. The monooxygenase which converts 4-HPA into 3,4-dihydroxyphenylacetate, the first intermediate of the pathway, consists of two components, HpaB (58.7 kDa) and HpaC (18.6 kDa), encoded by the hpaB and hpaC genes, respectively, that form a single transcription unit. Overproduction of the small HpaC component in E. coli K-12 cells has facilitated the purification of the protein, which was revealed to be a homodimer that catalyzes the reduction of free flavins by NADH in preference to NADPH. Subsequently, the reduced flavins diffuse to the large HpaB component or to other electron acceptors such as cytochrome c and ferric ion. Amino acid sequence comparisons revealed that the HpaC reductase could be considered the prototype of a new subfamily of flavin:NAD(P)H reductases. The construction of a fusion protein between the large HpaB oxygenase component and the choline-binding domain of the major autolysin of Streptococcus pneumoniae allowed us to develop a rapid method to efficiently purify this highly unstable enzyme as a chimeric CH-HpaB protein, which exhibited a 4-HPA hydroxylating activity only when it was supplemented with the HpaC reductase. These results suggest the 4-HPA 3-monooxygenase of E. coli W as a representative member of a novel two-component flavin-diffusible monooxygenase (TC-FDM) family. Relevant features on the evolution and structure-function relationships of these TC-FDM proteins are discussed.

Amino Acid Sequence↗

PubMed1999

News & notes: production, purification, and properties of an endo-1, 3-beta-glucanase from the basidiomycete Agaricus bisporus.

Agaricus bisporus H 25 produced extracellular endo-1, 3-beta-glucanase when grown in a static culture at 25 degrees C in a minimal synthetic medium supplemented with A. bisporus cell walls plus fructose. Endo-1,3-beta-glucanase was purified 17.85-fold from 20-day-old culture filtrates by precipitation at 80% ammonium sulfate saturation, Sephadex G-75 gel filtration, and preparative PAGE followed by electroelution. The purified enzyme yielded a single band in both native and SDS-polyacrylamide gels with a molecular mass of 32 kDa (SDS-PAGE) and 33.7 kDa (MALDI-MS), showing an isoelectric point of 3.7. The enzyme was active against beta-1,3- linkages and, to a lesser extent, against beta-1,6-, exhibiting an endohydrolytic mode of action and a glycoprotein nature. Significant activities of the endo-glucanase against laminarin and pustulan were observed between pH 4 and 5.5, and between 40 degrees and 50 degrees C for laminarin, and between 30 degrees and 50 degrees C for pustulan. The optimum pH and temperature were 4.5 and 45 degrees C for both substrates.

Agaricus↗

PubMedDate not supplied

[Natural "dopaminotrophic" cell transplant: a new concept in antiparkinsonian therapy].

AIM AND METHOD: Parkinson s disease is caused by the degeneration of dopaminergic neurons of substantia nigra projecting to striatum. Cellular substitution represents a potentially treatment once beneficial levodopa effects wear off. A promising therapeutic approach is grafting cells or other vectors which release neuroprotective molecules that stimulate regeneration in the damaged nigrostriatal system or, in other words, that exert a dopaminotrophic action. We have tested the suitability of intrastriatal grafts of extra adrenal chromaffin cells taken from the Zuckerkandl s organ. This paraganglion contains chromaffin cells that express and release glial cell line derived neurotrophic factor (GDNF) and transforming growth factor b1 (TGF b1), both known to protect dopamine cells in vitro and in vivo. Grafts induced a functional recovery of parkinsonian rats which developed over months. The beneficial effects of grafts of the Zuckerkandl s organ were related to long survival of grafted cells, striatal reinnervation, enhancement of dopamine levels in the host striatum, and the cell delivery into the host striatum of GDNF and TGF b1. CONCLUSION: Our result should stimulate research on the clinical applicability of transplants of the Zuckerkandl s organ in Parkinson s disease

Animals↗