Search

OBJECTIVES: To explore the association between gender and (1) attendance and (2) compliance with treatment in a population of patients with diabetes who attended outpatient clinics in the island of Trinidad (Trinidad and Tobago). METHODS: A cross-sectional study was conducted with a sample of 360 patients who met the selection criteria. Simple consecutive sampling and a questionnaire were used to interview clinic attendees at two urban clinics in east and south Trinidad. RESULTS: 74.2% (267) of the participants were women. A higher percentage of women than men were unemployed (79.4% vs. 59.1%, P < 0.001). Men were more likely to consume alcohol (26.9% vs. 11.6%, P < 0.001) and smoke cigarettes (20.4% vs. 5.6%, P < 0.001). Women were more compliant than men regarding diet (39.3% vs. 22.6%, P < 0.005) and prescribed medication (71.9% vs. 65.6%, P < 0.04). Women were more satisfied than men with dispensary (81.3% vs. 71.0%, P < 0.04) and clinic conditions (92.1% vs. 84.9%, P < 0.05). CONCLUSIONS: More women attended the clinic, and their compliance with the treatment regimen was better than in men. The latter were more likely to engage in health risk behaviors such as drinking and smoking. Efforts focused on men with diabetes mellitus in Trinidad and Tobago are needed to encourage greater compliance. [ABSTRACT FROM AUTHOR]

Acute allograft rejection is driven by production of cytokines such as interleukin-2 (IL-2) that activate and expand alloreactive T cells by ligating high-affinity IL-2 receptors composed of three subunit chains: α, β, γ. The α chain, expressed only on activated T cells, has become an important therapeutic target. Monoclonal antibodies (mAbs) that bind IL-2Rα chains significantly decrease transplant rejection. We examined the ability of the humanized anti-IL-2Rα antibody daclizumab to block high-affinity IL-2Rs and interrupt T-lymphocyte signaling. Our evaluation focused on a pathway critical for T-cell proliferation, the Jak/STAT pathway. Daclizumab markedly inhibited phosphorylation of the Jak1, Jak3 and STAT5a/b components of the IL-2R-dependent pathway. Suppression by daclizumab was associated with internalization of IL-2Rα but not IL-2Rβγ chains. High IL-2 doses overcame daclizumab-induced blockade of Jak/STAT phosphorylation despite absent cell surface high-affinity IL-2Rs. Under these circumstances, IL-2-mediated Jak/STAT pathway activation might be generated through residual intermediate affinity IL-2Rβγ receptors, and this was demonstrated by complete blockade of signaling when anti-IL-2Rβ monoclonal antibody was added. Humanized antibodies are an important part of strategies to induce alloantigen tolerance. Understanding the molecular events associated with their beneficial clinical effect is critical to design of future immunosuppressive strategies.

Zn2+ binding to canine cardiac calsequestrin was investigated using the Zn2+ specific fluorescence dye salicylcarbohydrazone (SACH), 65Zn2+ overlay and Zn2+-IDA chromatography. Cardiac calsequestrin binds ~200 moles of Zn2+/mole of protein with the K_d=300 µM. Zn2+ binding to calsequestrin was further confirmed by 65Zn2+ overlay and Zn2+-dependent aggregation of the protein. However, calsequestrin did not bind to a Zn2+-IDA-agarose column, indicating that histidine residues may not be involved in Zn2+ binding to the protein. Circular dichroism revealed only minor Zn2+-dependent conformational changes in calsequestrin. We conclude that calsequestrin is a Ca2+- and Zn2+-binding protein and that Zn2+ may modulate the structure and function of the protein.Copyright 1995, 1999 Academic Press, Inc.

Short bamboo fiber reinforced epoxy composites have been developed with varying fiber length. The chemical resistance tests indicate that the composite materials are resistant to acetic acid, hydrochloric acid, nitric acid, sodium hydroxide, sodium carbonate, ammonia, benzene, carbon tetrachloride and toluene. The variation of tensile load at break with fiber length has been studied and the tensile load is found to be maximum for the fiber length of 30 mm.

This study aimed to identify social characteristics associated with higher levels of morbidity from diabetes and their relationship to health care utilization.

The distribution of calsequestrin and calreticulin in smooth muscle and non-muscle tissues was investigated. Immunoblots of endoplasmic reticulum proteins probed with anti-calreticulin and anti-calsequestrin antibodies revealed that only calreticulin is present in the rat liver endoplasmic reticulum. Membrane fractions isolated from uterine smooth muscle, which are enriched in sarcoplasmic reticulum, contain a protein band which is immunoreactive with anti-calreticulin but not with anti-calsequestrin antibodies. The presence of calreticulin in these membrane fractions was further confirmed by 45Ca2+ overlay and “Stains-All” techniques. Calreticulin was also localized to smooth muscle sarcoplasmic reticulum by the indirect immunofluorescence staining of smooth muscle cells with anti-calreticulin antibodies. Furthermore, both liver and uterine smooth muscle were found to contain high levels of mRNA encoding calreticulin, whereas no mRNA encoding calsequestrin was detected. We have employed an ammonium sulfate precipitation followed by Mono Q fast protein liquid chromatography, as a method by which calsequestrin and calreticulin can be isolated from whole tissue homogenates, and by which they can be clearly resolved from one another, even where present in the same tissue. Calreticulin was isolated from rabbit and bovine liver, rabbit brain, rabbit and porcine uterus, and bovine pancreas and was identified by its amino-terminal amino acid sequence. Calsequestrin cannot be detected in preparations from whole liver tissue, and only very small amounts of calsequestrin are detectable in ammonium sulfate extracts of uterine smooth muscle. We conclude that calreticulin, and not calsequestrin, is a major Ca2+ binding protein in liver endoplasmic reticulum and in uterine smooth muscle sarcoplasmic reticulum. Calsequestrin and calreticulin may perform parallel functions in the lumen of the sarcoplasmic and endoplasmic reticulum.