Summary In this study, we detected multiple var gene transcripts within single, mature trophozoite‐infected red blood cells (iRBCs) bound to chondroitin sulphate A (CSA). Several of the var detected had previously been demonstrated to encode Plasmodium falciparum erythrocyte membrane protein‐1 (PfEMP‐1) variants with domains that mediated iRBC adhesion to receptors other than CSA. Parasites expressing the CSA‐adherent phenotype transcribed far more of one var than of all others, but this gene was different from the two other var previously purported to encode adhesion to CSA. Previous work suggesting that only single var are transcribed by mature trophozoites needs re‐examination in the light of these data from single, infected cells.

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A [meso-tetrakis(4-sulfonatophenyl)porphyrinato]oxovanadium(IV) (VO(tpps)), has been found to have an antidiabetic activity and thus to be effective for treating diabetic animal models. High hypoglycemic effects have been observed not only in streptozotocin (STZ)-induced type 1 diabetic mice but also type 2 diabetic KKAy mice by oral administration of the complex. However, the molecular mechanism for the activities has not yet been examined. The aim of this study was to investigate the molecular mechanism of VO(tpps) in 3T3-L1 adipocytes with respect to insulin signaling pathway. Addition of VO(tpps) was found to phosphorylate the insulin receptor β (IRβ) subunit, insulin receptor substrate 1 (IRS1) and protein kinase B (PKB)/Akt in 3T3-L1 adipocytes, in which all phosphorylations were time dependent. The VO(tpps)-induced Akt phosphorylation was suppressed by a PI3K inhibitor, wortmannin. VO(tpps) also stimulated GLUT4 protein translocation to the plasma membrane. Based on these results, we conclude that VO(tpps) exhibits both insulinomimetic and antidiabetic activities via tyrosine phosphorylations of IRβ and IRS1, which activate the downstream Akt phosphorylation through PI3K, and this signaling cascade finally causes GLUT4 translocation from the cytosol to the plasma membrane.