Prevalence and factors associated with hyperglycemia in a rural population of Tanvè and Dékanmey in Benin in 2019.

BACKGROUND: Hyperglycemia leads to serious damage to the body, especially the blood vessels and nerves. This study aimed to determine the prevalence and factors associated with hyperglycemia in a rural population of Tanvè and Dékanmey in Benin in 2019. MATERIALS AND METHODS: This was a cross-sectional, descriptive and analytical study, nested in the Tanvè Health Study (TAHES) cohort. It covered all residents of the villages of Tanvè and Dékanmey, aged 25 years and above, and having given their written consent. Data were collected in the households during the fourth annual monitoring visit in 2019 using the WHO STEPS Wise approach. Hyperglycemia was defined as a fasting capillary blood glucose value ≥ 110 mg/dL. Data were analyzed with R Studio software version 3.5.1. RESULTS: A total of 1331 subjects were included in the study with a 60% female predominance and a sex ratio (male/female) of 0.7. The median age was 40 years (Q1 = 32 years; Q3 = 53 years) with a range of 25 and 98 years. The prevalence of hyperglycemia was 4.6%. In multivariate analysis, advanced age (AOR = 1.03; 95%CI = 1.02-1.73; p = 0.004), male sex (AOR = 2.93; 95%CI = 1.49-5.84; p = 0.023), monthly income> 105,000 FCFA (AOR = 2.63; 95%CI = 1.24-5.63; p = 0.030), abdominal obesity (AOR = 2.80; 95%CI = 1.29-6.16; p = 0.007, and obesity (AOR = 1.68; 95%CI = 0.75-3.59; p = 0.004) were statistically associated with hyperglycemia. CONCLUSION: The prevalence of hyperglycemia is not negligible in rural areas in Benin. Our study found that older age, male gender, high income, abdominal obesity, and obesity are determining factors in its occurrence.

Protein kinase C regulates the phosphorylation and oligomerization of ERM binding phosphoprotein 50.

Ezrin-Radixin-Moesin (ERM) binding phosphoprotein 50 (EBP50, a.k.a. NHERF-1) is a scaffold protein essential for the localization and coordinated activity of apical transporters, enzymes and receptors in epithelial cells. EBP50 acts via multiple protein binding interactions, including oligomerization through interactions of its PSD95-Dlg-ZO1 (PDZ) domains. EBP50 can be phosphorylated on multiple sites and phosphorylation of specific sites modulates the extent of oligomerization. The aim of the present study was to test the capacity of protein kinase C (PKC) to phosphorylate EBP50 and to regulate its oligomerization. In vitro experiments showed that the catalytic subunit of PKC directly phosphorylates EBP50. In HEK-293 cells transfected with rat EBP50 cDNA, a treatment with 12 myristate 13-acetate (PMA) induced a translocation of PKCalpha and beta isoforms to the membrane and increased 32P incorporation into EBP50. In co-transfection/co-precipitation studies, PMA treatment stimulated EBP50 oligomerization. Mass spectrometry analysis of full-length EBP50 and phosphorylation analyses of specific domains, and of mutated or truncated forms of EBP50, indicated that PKC-induced phosphorylation of EBP50 occurred on the Ser337/Ser338 residue within the carboxyl-tail domain of the protein. Truncation of Ser337/Ser338 also diminished PKC-induced oligomerization of EBP50. These results suggest the PKC signaling pathway can impact EBP50-dependent cellular functions by regulating EBP50 oligomerization.

Butyrate-treated colonic Caco-2 cells exhibit defective integrin-mediated signaling together with increased apoptosis and differentiation.

We previously reported that the enterocytic differentiation of human colonic Caco-2 cells correlated with alterations in integrin signaling. We now investigated whether differentiation and apoptosis of Caco-2 cells induced by the short-chain fatty acid butyrate (NaBT) was associated with alterations in the integrin-mediated signaling pathway with special interest in the expression and activity of focal adhesion kinase (FAK), of the downstream phosphatidylinositol 3'-kinase (PI 3-kinase)-Akt pathway and in the role of the nuclear factor kappaB (NF-kappaB). NaBT increased the level of sucrase. It induced apoptosis as shown by: (1) decreased Bcl-2 and Bcl-X(L) proteins and increased Bax protein; (2) activation of caspase-3; and (3) increased shedding of apoptotic cells in the medium. This effect was associated with defective integrin-mediated signaling as shown by: (1) down-regulation of beta1 integrin expression; 2) decreased FAK expression and tyrosine phosphorylation; (3) concerted alterations in cytoskeletal and structural focal adhesions proteins (talin, ezrin); and (4) decreased FAK ability to associate with PI 3-kinase. However, in Caco-2 cells, beta1-mediated signaling failed to be activated downstream of FAK and PI 3-kinase at the level of Akt. Transfection studies show that NaBT treatment of Caco-2 cells promoted a significant activation of the NF-kappaB which was probably involved in the NaBT-induced apoptosis. Our results indicate that the prodifferentiating agent NaBT induced apoptosis of Caco-2 cells probably through NF-kappaB activation together with a defective beta1 integrin-FAK-PI 3-kinase pathways signaling.