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3.  Dietary reduction of serum cholesterol concentration: time to think again. 
BMJ : British Medical Journal  1991;303(6808):953-957.
OBJECTIVE--To evaluate the long term efficacy of diets in lowering serum cholesterol concentration. DESIGN--Descriptive overview of 16 published controlled trials of six months' duration or longer. SETTING--Trials had been conducted in hospital clinics (6), industry (3), mental hospitals or institutions (3), and in general populations (4). PATIENTS--Trials had been conducted in high risk subjects (5), in unselected healthy subjects (6), or for secondary prevention in patients with coronary heart disease (5). Women were included in only four trials. INTERVENTIONS--Diets equivalent to the step 1 diet were employed in eight trials, with individual intervention by dietitians (3) or occupational physicians (2) or with population advice (3). Intensive diets which were more rigorous than the step 2 diet were employed in eight trials. MAIN OUTCOME MEASURES--Net change in serum total cholesterol concentration in subjects receiving treatment with diet compared with values in control subjects after six months to 10 years. RESULTS--In five trials with the step 1 diet as individual intervention the net reduction in serum cholesterol concentration ranged from 0% to 4.0% over six months to six years. In trials with population education reductions in cholesterol concentrations were 0.6-2.0% over five to 10 years. When population and individual dietary advice were combined changes in cholesterol concentration ranged from a fall of 2.1% to a rise of 1.0% over four to 10 years. Diets more intensive than the step 2 diet reduced serum cholesterol concentration by 13% over five years in selected high risk men in the population; by 6.5-15.1% over two to five years in hospital outpatients; and by 12.8-15.5% over one to four and a half years in patients in institutions. CONCLUSIONS--The response to a step 1 diet is too small to have any value in the clinical management of adults with serum cholesterol concentrations above 6.5 mmol/l. Current guidelines recommend screening of serum cholesterol concentration in healthy subjects, followed by treatment with a step 1 diet. The guidelines should be reviewed to provide a more realistic estimate of the effect of a step 1 diet and of the likely need for lipid lowering drugs.
PMCID: PMC1671346  PMID: 1954418
5.  Developmental expression of Sp1 in the mouse. 
Molecular and Cellular Biology  1991;11(4):2189-2199.
The expression of the trans-acting transcription factor Sp1 in mice was defined by a combination of RNA analysis and immunohistochemical localization of the Sp1 protein. Although ubiquitously expressed, there was an unexpected difference of at least 100-fold in the amount of Sp1 message in different cell types. Sp1 protein levels showed corresponding marked differences. Substantial variations in Sp1 expression were also found in some cell types at different stages of development. Sp1 levels appeared to be highest in developing hematopoietic cells, fetal cells, and spermatids, suggesting that an elevated Sp1 level is associated with the differentiation process. These results indicate that Sp1 has a regulatory function in addition to its general role in the transcription of housekeeping genes.
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PMCID: PMC359911  PMID: 2005904
6.  Activation of phosphatidylinositol 3-kinase in cells expressing abl oncogene variants. 
Molecular and Cellular Biology  1991;11(2):1107-1113.
A phosphoinositide kinase specific for the D-3 position of the inositol ring, phosphatidylinositol (PI) 3-kinase, associates with activated receptors for platelet-derived growth factor, insulin, and colony-stimulating factor 1, with products of the oncogenes src, fms, yes, crk, and with polyomavirus middle T antigen. Efficient fibroblast transformation by proteins of the abl and src oncogene families requires activation of their protein-tyrosine kinase activity and membrane association via an amino-terminal myristoylation. We have demonstrated that the PI 3-kinase directly associates with autophosphorylated, activated protein-tyrosine kinase variants of the abl protein. In vivo, this association leads to accumulation of the highly phosphorylated products of PI 3-kinase, PI-3,4-bisphosphate and PI-3,4,5-trisphosphate, only in myristoylated, transforming abl protein variants. Myristoylation thus appears to be required to recruit PI 3-kinase activity to the plasma membrane for in vivo activation and correlates with the mitogenicity of the abl protein variants.
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PMCID: PMC359788  PMID: 1846663

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