The metabolic consequences of obesity are well-documented in Western populations. However, limited data are available on the association between body mass index (BMI) and cardiovascular risk factors in developing countries. The authors therefore examined the association between BMI and cardiovascular risk factors in a very lean population in China. A total of 2,542 subjects aged 20-70 years from a rural area of Anqing, China, participated in a cross-sectional survey, and 1,610 provided blood samples in 1993. Mean BMI (kg/m2) was 20.7 for men and 20.9 for women. After adjustment for age, sex, education level, occupation, current alcohol use, and cigarette smoking, BMI was significantly associated with systolic and diastolic blood pressures (p < 0.0001). The adjusted odds ratio for hypertension (systolic pressure > or =140 mmHg or diastolic pressure > or = 90 mmHg) across quintiles of BMI (quintile medians: 18.0, 19.4, 20.6, 21.8, and 24.0) were 1.0, 1.34, 2.46, 2.61, and 4.90 (95% confidence interval: 3.20, 7.50). A higher BMI was directly associated with higher levels of serum total cholesterol, triglycerides, and fasting glucose and lower levels of high density lipoprotein cholesterol. These data from a very lean Chinese population confirm independent relations between body mass and cardiovascular risk factors observed in predominantly overweight Western populations and extend the range of associations to lower BMI levels than do previous studies.
Almost all proteins contain charged amino acids. While the function in catalysis or binding of individual charges in the active site can often be identified, it is less clear how to assign function to charges beyond this region. Are they necessary for solubility? For reasons other than solubility? Can manipulating these charges change the properties of proteins? A combination of capillary electrophoresis (CE) and protein charge ladders makes it possible to study the roles of charged residues on the surface of proteins outside the active site. This method involves chemical modification of those residues to generate a large number of derivatives of the protein that differ in charge. CE separates those derivatives into groups with the same number of modified charged groups. By studying the influence of charge on the properties of proteins using charge ladders, it is possible to estimate the net charge and hydrodynamic radius and to infer the role of charged residues in ligand binding and protein folding.