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1.
Chemosphere ; 100: 83-8, 2014 Apr.
Article in English | MEDLINE | ID: mdl-24411836

ABSTRACT

Cd bioaccumulation pattern was investigated in Mediterranean spider crab (Maya squinado, Herbst, 1788) collected from the northern Adriatic Sea. Specimens were caught in the framework of a monitoring plan in order to quantify the Cd distribution into different organs and tissues of crab. For this purpose, Cd level was studied in appendages, cephalothorax, abdomen as well as gonads. Cd concentrations were found largely below the Maximum Level (ML) established at the European Union (EU) level for muscle from crab appendages (found mean 0.011 mg kg(-1)) and approximately amounted to 2% of the EU ML (0.50 mg kg(-1)). The higher Cd concentrations were found in organs and tissues included in crab body such as abdomen, chephalotorax and gonads with respect to appendages. Chephalotorax showed the highest metal concentration (mean value of 1.19 mg kg(-1)). The possible differences in Cd bioaccumulation rate among crab organs and tissues were also investigated applying a parametric linear regression. A major Cd bioaccumulation rate was revealed in chephalotorax with respect to other analyzed organs and tissues. Furthermore, the evaluation of health risk related to human consumption of the Mediterranean spider crab has been studied for median of total population, median and 95th percentile of consumers of Italy. The observed results highlighted that the consumption of organs and tissues included in crab body such as abdomen, gonads and, in particular, chephalotorax substantially increased the Cd intake reaching also alarming Estimated Weekly Intake (EWI) values especially for median and 95th percentile of Italian consumers.


Subject(s)
Brachyura/metabolism , Cadmium/metabolism , Cadmium/toxicity , Eating , Environmental Exposure/adverse effects , Health , Shellfish/analysis , Animals , Environmental Pollutants/metabolism , Environmental Pollutants/toxicity , Humans , Italy
2.
Ann Ist Super Sanita ; 43(1): 77-82, 2007.
Article in English | MEDLINE | ID: mdl-17536157

ABSTRACT

To verify whether a diabetes family history might be a risk factor for the development, in adult age, of metabolic disorders, leptin, anthropometric and endocrine parameters were analysed in 95 babies with grandparents affected by type 2 diabetes (DF) and in 95 matched babies without diabetes family history (NDF). A sexual dimorphism for leptin was present in the NDF group (males: 6.7+/-4.1 ng/ml; females: 12.3+/-6.5; p < 0.0001) but not in the DF group (males: 9.0+/-5.5; females: 10.8+/-6.4), due to the significant increase in DF male leptin level, compared to that of NDF males (p < 0.05). In DF males only, leptin was positively correlated with body length, PI, C-peptide, IGF-1 and IGF1BP3. These results suggest that the increase in DF male leptin could be a compensatory mechanism for reduced insulin sensitivity in a pre-clinical alteration of glucose metabolism.


Subject(s)
Birth Weight , Body Height , Diabetes Mellitus, Type 2/genetics , Fetal Blood/chemistry , Leptin/blood , C-Peptide/analysis , Case-Control Studies , Diabetes Mellitus, Type 2/epidemiology , Female , Genetic Predisposition to Disease , Humans , Infant, Newborn , Insulin/blood , Insulin Resistance/genetics , Insulin-Like Growth Factor Binding Protein 3/blood , Insulin-Like Growth Factor I/analysis , Italy/epidemiology , Male , Sex Characteristics
3.
Ann Ist Super Sanita ; 38(4): 393-9, 2002.
Article in English | MEDLINE | ID: mdl-12760336

ABSTRACT

Advanced glycosylation end products (AGE) which are probably involved in the pathogenesis of diabetic complications, comprise a series of related chemical structures. Thus different antisera might recognize particular AGE epitopes rather than the complete range of epitopes. To test this hypothesis, two antisera were raised using different immunization techniques and different AGE-carrier proteins as immunogens. The antisera reactivity towards different AGE-proteins under various experimental conditions was compared. Both antisera recognized all AGE-proteins, although with different binding curves. Following pre-incubation with carboxymethyllysine-BSA (CML-BSA) (an oxidation-derived AGE) one antiserum partially retained its reactivity, suggesting recognition of non-oxidation-derived AGE. This result was confirmed both in the cross-reactivity and the preincubation experiments and when the reactivity of the antisera was tested against antigens incubated under oxidative and non-oxidative conditions. These results confirmed the hypothesis that differently produced antisera may not share the recognition of epitopes of different nature and suggest the necessity to adopt a standardized methodology for the production of antisera for an accurate and reproductible determination of the in vivo AGE concentration.


Subject(s)
Epitopes/analysis , Glycation End Products, Advanced/analysis , Animals , Antioxidants/pharmacology , Epitopes/immunology , Glycation End Products, Advanced/immunology , Hemocyanins/chemistry , Humans , Immunochemistry , Isoelectric Focusing , Rabbits/immunology , Ribonucleases/chemistry , Serum Albumin, Bovine/chemistry , Serum Albumin, Bovine/immunology
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