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Abstract.Anemia among adolescent girls is one of the major challenges faced by India. The present study was undertaken to assess the prevalence of anemia and status of other hematological parameters among adolescent girls (11 - 18 years) residing in an urban slum of Delhi. A total of 794 adolescent girls were recruited for the study. The prevalence of anemia was estimated using the cyanmethemoglobin method. Serum levels of ferritin, folic acid and vitamin B12were estimated for anemic subjects. The prevalence of anemia was reported as 58.7 %, with 31.6 %, 25.7 % and 1.4 % of subjects being mild, moderate and severely anemic. Hemoglobin levels of subjects who had attained menarche were found to be significantly lower than those who had not attained menarche. The prevalence of serum ferritin, folic acid and vitamin B12deficiency among those who were anemic was reported as 41.1 %, 5.0 % and 63.3 % respectively. A total of 23.5 % anemic subjects had concomitant micronutrient deficiencies of serum vitamin B12and ferritin. The results indicate that supplemental iron and vitamin B12may better address the burden of anemia in adolescent girls in Delhi.

Senile plaques of Alzheimer's disease brain contain, in addition to beta amyloid peptide (Aβ), multiple proteoglycans. Systemic amyloidotic deposits also routinely contain proteoglycan, suggesting that these glycoconjugates are generally involved in amyloid plaque formation and/or persistence. We demonstrate that heparan sulfate proteoglycan (HSPG) and chondroitin sulfate proteoglycan (CSPG) inhibit the proteolytic degradation of fibrillar, but not non-fibrillar, Aβ at physiological pH. In accordance with the proteolysis studies, high affinity binding of proteoglycans to fibrillar Aβ(1-40) and Aβ(1-42) is observed from pH 4 to 9, whereas appreciable binding of HSPG or CSPG to non-fibrillar peptide is only seen at pH < 6. This differing pH dependence of binding suggests that a lysine residue is involved in proteoglycan association with fibrillar Aβ, whereas a protonated histidine appears to be needed for binding of the glycoconjugates to non-fibrillar peptide. Scatchard analysis of fibrillar Aβ association with proteoglycans indicates a single affinity interaction, and the binding of both HSPG and CSPG to fibrillar Aβ is completely inhibited by free glycosaminoglycan chains. This implies that these sulfated carbohydrate moieties are primarily responsible for proteoglycan•Aβ interaction. The ability of proteoglycans to bind fibrillar Aβ and inhibit its proteolytic degradation suggests a possible mechanism of senile plaque accumulation and persistence in Alzheimer's disease.

Senile plaques of Alzheimer's disease brain contain, in addition to beta amyloid peptide (A beta), multiple proteoglycans. Systemic amyloidotic deposits also routinely contain proteoglycan, suggesting that these glycoconjugates are generally involved in amyloid plaque formation and/or persistence. We demonstrate that heparan sulfate proteoglycan (HSPG) and chondroitin sulfate proteoglycan (CSPG) inhibit the proteolytic degradation of fibrillar, but not non-fibrillar, A beta at physiological pH. In accordance with the proteolysis studies, high affinity binding of proteoglycans to fibrillar A beta(1-40) and A beta(1-42) is observed from pH 4 to 9, whereas appreciable binding of HSPG or CSPG to non-fibrillar peptide is only seen at pH < 6. This differing pH dependence of binding suggests that a lysine residue is involved in proteoglycan association with fibrillar A beta, whereas a protonated histidine appears to be needed for binding of the glycoconjugates to non-fibrillar peptide. Scatchard analysis of fibrillar A beta association with proteoglycans indicates a single affinity interaction, and the binding of both HSPG and CSPG to fibrillar A beta is completely inhibited by free glycosaminoglycan chains. This implies that these sulfated carbohydrate moieties are primarily responsible for proteoglycan.A beta interaction. The ability of proteoglycans to bind fibrillar A beta and inhibit its proteolytic degradation suggests a possible mechanism of senile plaque accumulation and persistence in Alzheimer's disease.