• Archives of Pharmacal Research
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• v.22 no.4
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• pp.329-334
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• 1999

Insulin stimulates glucose uptake in muscle and adipose cells primarily by recruiting GLUT4 from an intracellular storage pool to the plasma membrane. Dysfunction of this process known as insulin resistance causes hyperglycemia, a hallmark of diabetes and obesity. Thus the understanding of the mechanisms underlying this process at the molecular level may give an insight into the prevention and treatment of these health problems. GLUT4 in rat adipocytes, for example, constantly recycles between the cells surface and an intracellular pool by endocytosis and exocytosis, each of which is regulated by an insulin-sensitive and GLUT4-selective sorting mechanism. Our working hypothesis has been that this sorting mechanism includes a specific interaction of a cytosolic protein with the GLUT4 cytoplasmic domain. Indeed, a synthetic peptide of the C-terminal cytoplasmic domain of GLUT4 induces an insulin-like GLUT4 recruitment when introduced in rat adipocytes. Relevance of these observations to a novel euglycemic drug design is discussed.

• Applied Microscopy
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• v.28 no.4
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• pp.577-590
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• 1998

Puromycin aminonucleoside (PAN) nephropathy was induced in a group of Sprague-Dawley rat by a single dose of intraperitoneal Injection to study an ultrastructural change of glomerulus. The experimental rats developed proteinuria three days after PAN injection. Electron microscopic studies of glomeruli showed the loss of epithelial foot processes, formation of cytoplasmic vacuoles, microvillous formation and increased numbers of lysosomes in the cytoplasm of podocytes. It is strongly suggested that proteinuria in PAN nephrosis may be primarily due to a glomerular epithelial lesion, leading to focal disarray of anionic sites or focal defects in the epithelial covering of the basement membrane. The loss of anionic sites in the basement membrane nay be caused by the foot process fusion and the epithelial detachment from the basement membrane.

• Proceedings of the Korean Biophysical Society Conference
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• 2003.06a
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• pp.30-30
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• 2003

Without a definitive resolution of stoichiometry of cardiac Na$^{+}$-Ca$^{2+}$exchange (NCX), we cannot proceed to any quantitative analysis of exchange function as well as cardiac excitation-contraction coupling. The stoichiometry of cardiac NCX, however, is presently in doubt because reversal potentials determined by various groups range between those expected for a 3-to-1 and a 4-to-1 flux coupling. For a new perspective on this problem, we have used ion-selective microelectrodes to quantify directly exchanger-mediated fluxes of $Ca^{2+}$and Na$^{+}$in giant membrane patches. $Ca^{2+}$- and Na$^{+}$-selective microelectrodes, fabricated from quartz capillaries, are placed inside of the patch pipettes to detect extracellular ion transients associated with exchange activity. Ion changes are monitored at various distances from the membrane, and the absolute ion fluxes through NCX are determined via simulations of ion diffusion and compared with standard ion fluxes (Ca$^{2+}$ fluxes mediated by $Ca^{2+}$ ionophore, and Na$^{+}$ fluxes through gramicidin channels and Na$^{+}$/K$^{+}$pumps). Both guinea pig myocytes and NCX1-expressing BHK cells were employed, and for both systems the calculated stoichiometries for inward and outward exchange currents range between 3.2- and 3.4-to-1. The coupling ratios do not change significantly when currents are varied by changing cytoplasmic [Ca$^{2+}$] or by adding cytoplasmic Na$^{+}$. The exchanger reversal potentials, measured in both systems under several ionic conditions, range from 3.1- to 3.3-to-1. Taken together, a clear discrepancy from a NCX stoichiometry of 3-to-1 was obtained. Further definitive experiments are required to acquire a fixed number, and the present working hypothesis is that NCX current has an extra current via ‘conduction mode’.ent via ‘conduction mode’.

• Microbiology and Biotechnology Letters
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• v.17 no.5
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• pp.412-420
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• 1989

To know how the ribosomes involved in secretory protein synthesis were attached to the cytoplasmic membrane in Bacillus amyloliquefaciens, the cells were treated with puromycin combinated with magnesium at the logarithmic phase, and the variation of cell-bound and extracellular $\alpha$-amylase activity was assayed for determining the $\alpha$-amylase translocation blocking through the cytoplasmic membrane. In the abnormal $\alpha$-amylase producing mutant in which the C-terminal of the $\alpha$-amylase structure was deleted, B. umytotiquefaciens CH10-2, the $\alpha$-amylase was translocated normally through the cytoplasmic membranes, and the translocation blocking by puromycin was revealed to have a similar pattern as that in the wild type. This means that the C-terminal part of the enzyme structure may not have a signal for secretion. The cell death of the logarithmic phase cells in both strains was not affected much under 20$\mu\textrm{g}$/$m\ell$ of puromycin, however, the $\alpha$-amylase translocation was blocked markedly under less than 10$\mu\textrm{g}$/$m\ell$ of the puromycin concentration. The blocking of the enzyme secretion by puromycin may be due to the detachment of the ribosomes from cytoplasmic membranes by disturbing the nascent polypeptide synthesis. Further evidence for confirming this was that the detachment was increased in 50 mM of magnesium ion because the extracellular $\alpha$-amylase activity was decreased more under this condition. If the cells were treated with trypsin combinated with Iysozyme, the extracellular $\alpha$-amylase activity from the cultured medium was reduced markedly, however, the activity from the cells treated with trypsin only was not reduced. This means that the nascent polypeptides protruding from the cytoplasmic membrane were sensitive to the trypsin digestion, whereas the matured ones were not. Therefore, the protruding polypeptides from the cytoplasmic membranes may be truncated by trypsin before forming their final tertiary structures by folding in the cell wall layer.

• Applied Microscopy
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• v.23 no.1
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• pp.1-14
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• 1993

The present study was carried out to analyze the evidence of membrane recycling, and the regulation of cellular transport by dynamic changes in apical membrane area that functionally interacts with the number of cytoplasmic vesicles. Under scanning electron micrographs, turtle bladder mucosa contain three main type of cells; granular cells and carbonic anhydrase (CA)-rich cells, deviding into a and b type of epithelial cell. The granular cell is the majority cell type of the mucosa comprising 80% of the total cell number. The remaining 20% of the cells are characteristically rich in carbonic anhydrase. Uptake of HRP was detected in the most vacuoles or tubulovesicles in both type of CA-rich cells in the turtle bladder, indicating that the part of plasma membrane was internalized in the apical cytoplasmic vacuoles. It seems quite likely that CA-rich cells possess intracellular vesicles carrying proton pumps which are recycling back to the apical plasma membrane. In turtle bladder, the granular cells actively secrete large quantities of mucin and other proteins by an exocytotic mechanism in an apparently constitutive fashion. The possibility that bladder epithelial cells secrete mucin via a regulated secretory pathway has not been rigorously examined and much is still to be determined about these issues from this cell type.

• Journal of Microbiology and Biotechnology
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• v.17 no.11
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• pp.1797-1804
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• 2007

Lycopene, an acyclic carotenoid found in tomatoes (Lycopersicon esculentum) and a number off fruits, has shown various biological properties, but its antifungal effects remain poorly understood. The current study investigated the antifungal activity of lycopene and its mode of action. Lycopene showed potent antifungal effects toward pathogenic fungi, tested in an energy-independent manner, with low hemolytic effects against human erythrocytes. To confirm the antifungal effects of lycopene, its effects on the dimorphism of Candida albicans induced by fetal bovine serum (FBS), which plays a key role in the pathogenesis of a host invasion, were investigated. The results showed that lycopene exerted potent antifungal activity on the serum-induced mycelia of C. albicans. To understand the antifungal mode of action of lycopene, the action of lycopene against fungal cell membranes was examined by FACScan analysis and glucose and trehalose-release test. The results indicated that lycopene caused significant membrane damage and inhibited the normal budding process, resulting from the destruction of membrane integrity. The present study indicates that lycopene has considerable antifungal activity, deserving further investigation for clinical applications.

• Journal of Nutrition and Health
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• v.30 no.6
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• pp.658-668
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• 1997

Path of a small hydrophobic molecule through the aqueous cytoplasma is not linear. Partition may favor membrane binding by several orders of magnitude : thus significant membrane association will markedly decrease the cytosolic transport rate. The presence of high concentration of soluble binding proteins for these hydrophobic molecules would compete with membrane association and thereby increase transport rate. For long chain fatty acid molecules, a family of cytosolic binding proteins collectively known as the fatty acid binding proteins(FABP), are thought to act as intracellular transport proteins. This paper examines the mechanism of transfer of fluorescent antyroyloxy-labeled fatty acids(AOFA) from purified FABPs to phosholipid membranes. With the exception of the liver FABP, AOFA is transferred from FABP by collisional interaction of the protein with a acceptor membrane. The rate of transfer increased markedly when membranes contain anionic phospholipids. This suggests that positively charged residues on the surface of the FABP may interact with the membranes. Neutralization of the surface lysine residues of adipocyte FABP decreased fatty acid transfer rate, and transfer was found to proceed via aqueous diffusion rather than collisional interaction. Site specific mutagenesis has further shown that the helix-turn-helix domain of the FABP is critical for interaction with anionic acceptor membranes. Thus cytosolic FABP may function in intracellular transport of fatty acid to decrease their membranes association as well as to target fatty acid to specific subcellular sites of utilization.

• Journal of Oral Medicine and Pain
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• v.3 no.1
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• pp.23-27
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• 1977

The author thought that the results of cytologic tests could be changed according to the fixative methods. So the author has studied several methods of fixing exfolaiative cells collected from normal adult cheek mucosa with a solution of equal parts of ether and 95% ethylalcohol, 95 ethylalcohol and Isoprophyl alcohol, and compared the results with each other. The results were as follows : The effects of fixation, and staining efficiency of nucleus and protoplasm are similar in each method, but the staining efficiency of cytoplasm and the conversation of cytoplasmic membrane were best in 95% ethylalcohol.

• Proceedings of the Korean Society of Life Science Conference
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• 2001.09a
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• pp.46-46
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• 2001

• Genomics & Informatics
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• v.16 no.1
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• pp.2-9
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• 2018

Olfactory receptors (ORs) in mammals are generally considered to function as chemosensors in the olfactory organs of animals. They are membrane proteins that traverse the cytoplasmic membrane seven times and work generally by coupling to heterotrimeric G protein. The OR is a G protein-coupled receptor that binds the guanine nucleotide-binding $G{\alpha}_{olf}$ subunit and the $G{\beta}{\gamma}$ dimer to recognize a wide spectrum of organic compounds in accordance with its cognate ligand. Mammalian ORs were originally identified from the olfactory epithelium of rat. However, it has been recently reported that the expression of ORs is not limited to the olfactory organ. In recent decades, they have been found to be expressed in diverse organs or tissues and even tumors in mammals. In this review, the expression and expected function of olfactory receptors that exist throughout an organism's system are discussed.