Thus, these residues are predicted to be critical for MFS-wide functions such as inter-helical interactions but are not involved directly in drug-proton antiport function of CaMdr1p. As an exception, our criteria of CRES also picked up two residues D235 and F277, which were earlier reported to be familywide function-specific. This could probably be because our program does not discriminate between the nature of amino acid present in DHA1 and SP families at a given alignment position. Some positions that are scored using this method may be actually excluded using our knowledge of amino acid similarity. For example, at position 235 of CaMdr1p, an aspartate is present. However, a glutamate occurs with same frequency at the respective alignment position in the SP family. It is composed of two major compartments, the endocrine pancreas and the exocrine pancreas. The endocrine pancreas, which regulates metabolism and glucose homeostasis, consists of five hormone-expressing cell types – a, b, d, e, and pp cells – that produce glucagon, insulin, somatostatin, ghrelin, and pancreatic polypeptide, respectively. Endocrine cells are arranged in clusters, called the islets of Langerhans, and most of the cells in each islet are b cells. Rafts are putative membrane entities that are proposed to have important physiological functions, such as signal transduction, and their molecular composition can be determined by analyzing detergent-resistant membrane fractions. While the functions of rafts in erythrocytes have not been definitively elucidated, some raft-associated GPI-anchored proteins have been implicated in immune-mediated clearance of erythrocytes. While the structure of rafts and their contribution to the physical properties of live cell membranes continue to be clarified, analyses of DRM fractions are useful in comparing AA and CC erythrocyte membranes for differences in lipid packing conditions and lateral protein distributions. Significant modifications of rafts, together with membraneassociated hemichromes and plasma protein aggregates, would be predicted to change the whole-cell net charge of CC erythrocytes. This can be determined by comparing ZP measurements of AA and CC erythrocytes. The ZP of a cell is a measure of the electrochemical potential of its membrane, as determined by the LDK378 amount and sign of associated ions. Among numerous chargebearing molecules in the erythrocyte membrane, sialic acid contributes substantially to the high net negative charge on the surface of erythrocyte membranes, and removal of sialic acid by neuraminidase treatment results in erythrocyte aggregation. Unlike Ecadherin, p120ctn, a-catenin, and b-catenin, PLEKHA7 is absent from the ”puncta adherentia” along lateral walls of epithelial cells, where a mobile pool of E-cadherin associates with many AJ plaque proteins.