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Sci Total Environ. 2002 Apr 22;289(1-3):255-60.
Blood lead concentrations and iron deficiency in Canadian aboriginal infants.

Willows ND, Gray-Donald K.

Canadian Institutes of Health Research Postdoctoral Fellow, Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton.

Aboriginal Cree infants living in northern Quebec who were 9 months of age were screened for anemia, iron deficiency and elevated blood lead concentrations. Of the 314 infants who were eligible to participate, 274 (87.3%) were screened for anemia, 186 had blood lead concentration measured and 141 of the latter group had iron status determined. The median blood lead concentration was 0.08 micromol/l (range 0.01-1.00 micromol/l). The 25, 50 and 75 percentiles for blood lead concentration were 0.05, 0.08 and 0.12 micromol/l, respectively. The prevalence of elevated blood lead concentrations (> 0.48 micromol/l) was 2.7% (95% Cl 0.36-5.0). Among infants who had blood lead measured, the prevalence of anemia (hemoglobin < 110 g/l) was 25.0% and 7.9% of infants had iron-deficiency anemia (hemoglobin < 110 g/l and serum ferritin < 10 microg/l). Anemic infants had a higher mean geometric blood lead concentration than did babies without anemia (0.11 micromol/l vs. 0.07 micromol/l, P = 0.003). Likewise, infants with iron-deficiency anemia had a significantly higher mean geometric blood lead concentration than infants without iron deficiency anemia (0.16 micromol/l vs. 0.07 micromol/l, P = 0.001). There was a significant negative correlation between blood lead and hemoglobin concentrations (r = -0.203, P = 0.006) and between blood lead and serum ferritin concentrations (r = -0.245, P = 0.003). Infants who were fed traditional food (fish, fowl and game) did not have a significantly different mean geometric blood lead concentration, hemoglobin concentration or serum ferritin concentration than infants who did not eat traditional food. Few infants (5.3%) ate traditional food daily.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12049403&dopt=Abstract

Biochim Biophys Acta. 2002 Jun 6;1571(2):124-30.
Generation of carbon monoxide and iron from hemeproteins in the presence of 7,8-dihydroneopterin.

Horejsi R, Jung C, Moller R, Tafeit E, Reibnegger G.

Institute for Medical Chemistry and Pregl Laboratory, University Graz, Harrachgasse 21/II, Austria. renate.horejsfunigraz.ac.at

7,8-Dihydroneopterin and neopterin are secreted by human and primate macrophages after activation by interferon-gamma in a ratio of 2:1. 7,8-Dihydroneopterin is known to suppress radical-mediated processes, but it is also able in the presence of iron ions to generate superoxide radical anion and hydroxyl radicals from molecular oxygen. Effects of 7,8-dihydroneopterin were investigated on (met)myoglobin and (met)hemoglobin. Addition of 7,8-dihydroneopterin to heme proteins in air-saturated solution resulted in dose-dependent cleavage of the porphyrin moiety. The liberation of non-heme iron and carbon monoxide originating from the cleaved porphyrin was quantified. Both were generated at equimolar concentrations with a linear correlation coefficient of 0.9. Addition of ferrous iron significantly accelerated the pteridine-mediated cleaving of the porphyrin. However, the total yield of porphyrin cleaved was controlled by the pterin rather than by the ferrous ion concentration. 7,8-Dihydroneopterin is assumed to reduce the heme iron in intact protein molecules, thereby preparing the conditions for binding of oxygen and carbon monoxide as ligands. Beyond that, it is concluded that hydroxyl radicals might be generated via reduction of molecular oxygen to superoxide anion in the autoxidation process and dismutation to hydrogen peroxide and subsequent Fenton reaction.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12049792&dopt=Abstract

Biophys Chem. 2002 Jun 19;97(2-3):129-38.
Structural electrochemical study of hemoglobin by in situ circular dichroism thin layer spectroelectrochemistry.

Zhu Y, Cheng G, Dong S.

State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022, PR China.

Secondary and tertiary or quaternary structural changes in hemoglobin (HB) during an electroreduction process were studied by in situ circular dichroism (CD) spectroelectrochemistry with a long optical path thin-layer cell. By means of singular value decomposition least-squares analysis, CD spectra in the far-UV region give two similar alpha components with different CD intensity, indicating slight denaturation in the secondary structures due to the electric field effect. CD spectra in the Soret band show a R-->T transition of two quaternary structural components induced by electroreduction of the heme, which changes the redox states of the center ion from Fe3+ to Fe2+ and the co-ordination number from 6 to 5. The double logarithmic analysis shows that electroreduction of hemoglobin follows a chemical reaction with R-->T transition. Some parameters in the electrochemical process were obtained: formal potential, E0'=-0.167 V; electrochemical kinetic overpotential, deltaE0=-0.32 V; standard electrochemical reaction rate constant, k0=1.79 x 10(-5) cm s(-1); product of electron transfer coefficient and electron number, alphan=0.14; and the equilibrium constant of R-->T transition, Kc=9.0.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12050005&dopt=Abstract

Biophys Chem. 2002 Jun 19;97(2-3):139-57.
Fluorescence properties of tryptophan residues in the monomeric d-chain of Glossoscolex paulistus hemoglobin: an interpretation based on a comparative molecular model.

Bosch Cabral C, Imasato H, Rosa JC, Laure HJ, da Silva CH, Tabak M, Garratt RC, Greene LJ.

Instituto de Quimica de Sao Carlos, Universidade de Sao Paulo, P.O. Box 780, Sao Carlos, SP, Brazil.

The primary structure of the 142 residue Glossoscolex paulistus d-chain hemoglobin has been determined from Edman degradation data of 11 endo-Glu-C peptides and 11 endo-Lys-C peptides, plus the results of Edman degradation of the intact globin. Tryptophan occupies positions 15, 33 and 129. Homology modeling allowed us to assign the positions of these Trp residues relative to the heme and its environment. The reference coordinates of the indole rings (average coordinates of the C(varepsilon2) and C(delta2) atoms) for W15 and W129 were 16.8 and 18.5 A, respectively, from the geometric center of the heme, and W33 was located in close proximity to the heme group at a distance which was approximately half of that for W15 and W129. It was possible to identify three rotamers of W33 on the basis of electrostatic and Van der Waals energy criteria. The calculated distances from the center of the heme were 8.3, 8.4 and 9.1 A for Rot1, Rot2 and Rot3, respectively. Radiationless energy transfer from the excited indole to the heme was calculated on the basis of Forster theory. For W33, the distance was more important than the orientation factor, kappa(2), due to its proximity to the heme. However, based on kappa(2), Rot2 (kappa(2)=0.945) was more favorable for the energy transfer than Rot1 (kappa(2)=0.433) or Rot3 (kappa(2)=0.125). In contrast, despite its greater distance from the heme, the kappa(2) of W129 (2.903) established it as a candidate to be more efficiently quenched by the heme than W15 (kappa(2)=0.191). Although the Forster approach is powerful for the evaluation of the relative efficiency of quenching, it can only explain pico- and sub-nanosecond lifetimes. With the average lifetime, <tau>=3 ns, measured for the apomonomer as the reference, the lifetimes calculated for each emitter were: W33-1 (1 ps), W33-2 (2 ps), W33-3 (18 ps), W129 (100 ps), and W15 (600 ps). Experimentally, there are four components for oxymonomers at pH 7: two long ones of 4.6 and 2.1 ns, which contribute approximately 90% of the total fluorescence, one of 300 ps (4%), and the last one of 33 ps (7.4%). It is clear that the equilibrium structure resulting from homology modeling explains the sub-nanosecond fluorescence lifetimes, while the nanosecond range lifetimes require more information about the protein in solution, since there is a significant contribution of lifetimes that resemble the apo molecule.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12050006&dopt=Abstract

J Clin Endocrinol Metab. 2002 Jun;87(6):2784-91.
Effect of pioglitazone on abdominal fat distribution and insulin sensitivity in type 2 diabetic patients.

Miyazaki Y, Mahankali A, Matsuda M, Mahankali S, Hardies J, Cusi K, Mandarino LJ, DeFronzo RA.

University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78229, USA.

We examined the effect of pioglitazone on abdominal fat distribution to elucidate the mechanisms via which pioglitazone improves insulin resistance in patients with type 2 diabetes mellitus. Thirteen type 2 diabetic patients (nine men and four women; age, 52 +/- 3 yr; body mass index, 29.0 +/- 1.1 kg/m(2)), who were being treated with a stable dose of sulfonylurea (n = 7) or with diet alone (n = 6), received pioglitazone (45 mg/d) for 16 wk. Before and after pioglitazone treatment, subjects underwent a 75-g oral glucose tolerance test (OGTT) and two-step euglycemic insulin clamp (insulin infusion rates, 40 and 160 mU/m(2).min) with [(3)H]glucose. Abdominal fat distribution was evaluated using magnetic resonance imaging at L4-5. After 16 wk of pioglitazone treatment, fasting plasma glucose (179 +/- 10 to 140 +/- 10 mg/dl; P < 0.01), mean plasma glucose during OGTT (295 +/- 13 to 233 +/- 14 mg/dl; P < 0.01), and hemoglobin A(1c) (8.6 +/- 0.4% to 7.2 +/- 0.5%; P < 0.01) decreased without a change in fasting or post-OGTT insulin levels. Fasting plasma FFA (674 +/- 38 to 569 +/- 31 microEq/liter; P < 0.05) and mean plasma FFA (539 +/- 20 to 396 +/- 29 microEq/liter; P < 0.01) during OGTT decreased after pioglitazone. In the postabsorptive state, hepatic insulin resistance [basal endogenous glucose production (EGP) x basal plasma insulin concentration] decreased from 41 +/- 7 to 25 +/- 3 mg/kg fat-free mass (FFM).min x microU/ml; P < 0.05) and suppression of EGP during the first insulin clamp step (1.1 +/- 0.1 to 0.6 +/- 0.2 mg/kg FFM.min; P < 0.05) improved after pioglitazone treatment. The total body glucose MCR during the first and second insulin clamp steps increased after pioglitazone treatment [first MCR, 3.5 +/- 0.5 to 4.4 +/- 0.4 ml/kg FFM.min (P < 0.05); second MCR, 8.7 +/- 1.0 to 11.3 +/- 1.1 ml/kg FFM(.)min (P < 0.01)]. The improvement in hepatic and peripheral tissue insulin sensitivity occurred despite increases in body weight (82 +/- 4 to 85 +/- 4 kg; P < 0.05) and fat mass (27 +/- 2 to 30 +/- 3 kg; P < 0.05). After pioglitazone treatment, sc fat area at L4-5 (301 +/- 44 to 342 +/- 44 cm(2); P < 0.01) increased, whereas visceral fat area at L4-5 (144 +/- 13 to 131 +/- 16 cm(2); P < 0.05) and the ratio of visceral to sc fat (0.59 +/- 0.08 to 0.44 +/- 0.06; P < 0.01) decreased. In the postabsorptive state hepatic insulin resistance (basal EGP x basal immunoreactive insulin) correlated positively with visceral fat area (r = 0.55; P < 0.01). The glucose MCRs during the first (r = -0.45; P < 0.05) and second (r = -0.44; P < 0.05) insulin clamp steps were negatively correlated with the visceral fat area. These results demonstrate that a shift of fat distribution from visceral to sc adipose depots after pioglitazone treatment is associated with improvements in hepatic and peripheral tissue sensitivity to insulin.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12050251&dopt=Abstract

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