Ethnic differences in total and HDL cholesterol among Turkish, Moroccan and Dutch ethnic groups living in Amsterdam, the Netherlands.

<p>Abstract</p> <p>Background</p> <p>High total cholesterol and low HDL (high-density lipoprotein) cholesterol are important determinants of cardiovascular disease. Little is known about dyslipidemia among Turkish and Moroccan migrants, two of the largest ethnic minority groups in several European countries. This study examines ethnic differences in total and HDL cholesterol levels between Dutch, Turkish and Moroccan ethnic groups.</p> <p>Methods</p> <p>Data were collected in the setting of a general health survey, in Amsterdam, the Netherlands, in 2004. Total response rate was 45% (Dutch: 46%, Turks: 50%, Moroccans: 39%). From 1,220 adults information on history of hypercholesterolemia, lifestyle and demographic background was obtained via health interviews. In a physical examination measurements of anthropometry and blood pressure were performed and blood was collected. Total and HDL cholesterol were determined in serum.</p> <p>Results</p> <p>Total cholesterol levels were lower and hypercholesterolemia was less prevalent among the Moroccan and Turkish than the Dutch ethnic population. HDL cholesterol was also relatively low among these migrant groups. The resulting total/HDL cholesterol ratio was particularly unfavourable among the Turkish ethnic group. Controlling for Body Mass Index and alcohol abstinence substantially attenuated ethnic differences in HDL cholesterol levels and total/HDL cholesterol ratio.</p> <p>Conclusions</p> <p>Total cholesterol levels are relatively low in Turkish and Moroccan migrants. However part of this advantage is off-set by their relatively low levels of HDL cholesterol, resulting in an unfavourable total/HDL cholesterol ratio, particularly in the Turkish population. Important factors in explaining ethnic differences are the relatively high Body Mass Index and level of alcohol abstinence in these migrant groups.</p

Correlating mesophilic counts to the pseudo-CMP content of raw milk

RESUMO A presente comunicação objetivou avaliar a quantificação do caseínomacropeptídeo (CMP), bem como diferenciá-lo (devido à adulteração com soro) do pseudo-CMP (devido à proteólise bacteriana) em amostras de leite cru coletadas nos domicílios do sul do Brasil. Os resultados reforçam a necessidade de práticas higiênicas durante a ordenha e estocagem do leite. As amostras de leite estudadas não estavam adulteradas por adição de soro, mostrando que a análise por cromatografia de exclusão por tamanho deve ser complementada a fim de revelar a identidade do peptídeo (CMP ou pseudo-CMP). A contagem bacteriana total (TBC) também se mostrou útil como indicador da contaminação do leite por micro-organismos proteolíticos, uma vez que uma relação diretamente proporcional entre TBC e pseudo-CMP foi estabelecida

Perfil eletroforético de lombo suíno adicionado de proteínas não cárneas.

A legislação brasileira permite a adição intencional de proteínas não cárneas em alguns produtos cárneos; entretanto, há poucas técnicas adaptadas e próprias para controle desses ingredientes. Na presente pesquisa, empregou-se a técnica de eletroforese em gel de poliacrilamida na presença de dodecil-sulfato de sódio (SDS-PAGE) para comparar amostras de carne suína (lombo), adicionadas de 1,5% de proteínas não cárneas (proteína isolada de soja e concentrado protéico de soro de leite). Mediante a padronização de dois protocolos distintos de extração (uréia 6M e Tris-HCl-SDS-mercaptoetanol) e a utilização de controles positivos e negativos, obtiveram-se perfis eletroforéticos típicos do músculo e das proteínas utilizadas. Ambas as extrações utilizadas foram adequadas para separação das proteínas do soro de leite das proteínas da carne, mas a visualização dos marcadores da soja não foi possível em razão da sobreposição de bandas.Made available in DSpace on 2011-04-09T22:21:22Z (GMT). No. of bitstreams: 1 2010044.pdf: 484836 bytes, checksum: eadebfd0a898fe3459b9e80d5b36f99d (MD5) Previous issue date: 2011-01-14201

Detecção de soja pelo teor de isoflavonas em lombo injetado de suíno.

No presente trabalho, a utilização de 1,5% de proteína isolada de soja em lombo de suíno foi detectada por meio do teor de isoflavonas, utilizando-se cromatografia líquida de alta eficiência. Elegeu-se o pico de genistina para quantificação, construindo-se uma curva-padrão com a proteína isolada de soja utilizada nas salmouras para injeção das carnes. A técnica revelou-se como uma alternativa rápida e eficaz para ser implantada no controle da utilização desse ingrediente em produtos cárneos.Made available in DSpace on 2011-04-09T22:21:14Z (GMT). No. of bitstreams: 1 2010039.pdf: 155783 bytes, checksum: ecaf1b3f614f6dde03ae7ca0ab402843 (MD5) Previous issue date: 2011-01-13201

Genome-wide linkage and association analyses to identify genes influencing adiponectin levels: the GEMS Study.

Adiponectin has a variety of metabolic effects on obesity, insulin sensitivity, and atherosclerosis. To identify genes influencing variation in plasma adiponectin levels, we performed genome-wide linkage and association scans of adiponectin in two cohorts of subjects recruited in the Genetic Epidemiology of Metabolic Syndrome Study. The genome-wide linkage scan was conducted in families of Turkish and southern European (TSE, n = 789) and Northern and Western European (NWE, N = 2,280) origin. A whole genome association (WGA) analysis (500K Affymetrix platform) was carried out in a set of unrelated NWE subjects consisting of approximately 1,000 subjects with dyslipidemia and 1,000 overweight subjects with normal lipids. Peak evidence for linkage occurred at chromosome 8p23 in NWE subjects (lod = 3.10) and at chromosome 3q28 near ADIPOQ, the adiponectin structural gene, in TSE subjects (lod = 1.70). In the WGA analysis, the single-nucleotide polymorphisms (SNPs) most strongly associated with adiponectin were rs3774261 and rs6773957 (P &lt; 10(-7)). These two SNPs were in high linkage disequilibrium (r(2) = 0.98) and located within ADIPOQ. Interestingly, our fourth strongest region of association (P &lt; 2 x 10(-5)) was to an SNP within CDH13, whose protein product is a newly identified receptor for high-molecular-weight species of adiponectin. Through WGA analysis, we confirmed previous studies showing SNPs within ADIPOQ to be strongly associated with variation in adiponectin levels and further observed these to have the strongest effects on adiponectin levels throughout the genome. We additionally identified a second gene (CDH13) possibly influencing variation in adiponectin levels. The impact of these SNPs on health and disease has yet to be determined

A-Imilano apoprotein. Isolation and characterization of a cysteine-containing variant of the A-I apoprotein from human high density lipoproteins.

A recently discovered familial lipoprotein disorder is characterized by reduced plasma levels of high density lipoproteins (HDL) and elevated triglyceride levels. The clinical aspects of this disorder are presented in an accompanying article (Franceschini et al. 1980. J. Clin. Invest. 66: 892-900). The apoprotein content of the HDL isolated from these patients differed markedly from that of normal HDL in that three apoprotein bands not previously described in man were present as major protein components. As determined by sodium dodecyl sulfate (SDS) gel electrophoresis, the relative molecular weights (Mr) of these new apoprotein bands were 55,000, 35,000, and 28,000. Although the Mr 28,000 apoprotein coelectrophoresed with authentic A-I on SDS polyacrylamide gels and showed immunochemical identity with the A-I apoprotein when tested with monospecific apo-A-I antiserum, it contained two amino acid residues, cysteine and isoleucine, which were not present in the amino acid sequence of normal human apo-A-I. This variant form of the A-I apoprotein was designated the A-IMilano apoprotein and denoted A-Icys. By virtue of the presence of cysteine (2 mol/mol A-Icys), the A-Icys apoprotein was capable of forming intermolecular disulfide bonds, and dimer formation of A-Icys produced the Mr 55,000 apoprotein. The Mr 35,000 apoprotein was composed of two different subunits, A-Icys and A-II. By analogy to the apo(E--A-II) complex, which also occurs in human HDL, this mixed disulfide complex was designated as the apo(A-Icys--A-II) complex. The A-IMilano (A-Icys) is the first example of a variation in the primary sequence of a protein of plasma lipoproteins