Papers by Israel Hanukoglu
Current Problems in Dermatology
and abnormal epidermal dlfferentlatlon/ volume editors, Makoto Sel]l, I A Bernstein.-Basel, New Y... more and abnormal epidermal dlfferentlatlon/ volume editors, Makoto Sel]l, I A Bernstein.-Basel, New York: Karger, 1983. (Current problems In dermatology: v. II) I Epidermis-cytology 2 Epidermis-physiology 3 Keratin-biosynthesIs 4. Keratin-physiology 5. Skin-anatomy & histology I. Bernstein, I. A II Sel]l, Makoto Ill. SerIes ISBN 3-8055-3752-2 WI CU804L v. II [WR 101 N842] © UNIVERSITY OF TOKYO PRESS, 1983 UTP 3047-68292-5149 Prin ted in Japan. All rights reserved No part of this pUblication may be translated into other languages, reproduced or ut!lized In any from or by any means, electronic or mechamcal, Including photocopymg, recording, microcopying, or by any informatIOn storage and retrIeval system, without permiSSIOn in wrItmg from the publisher. S. Karger AG, P.O. Box, CH-4009 Basel(Swltzerland)has the sale distribution nghts for all countries, with the exception of Japan.
The FASEB Journal, 2011
This study was designed to evaluate the changes number of cells of the two selected probiotic bac... more This study was designed to evaluate the changes number of cells of the two selected probiotic bacteria, B. longum TISTR2195 and L. plantarum TISTR1465, and yeast S. cerevisiae TISTR8656. The microorganisms were cultured in two types of media, namely selective media and protein base model. Selective media were divided into 4 subgroups: with 2% glucose added as a positive control (i), inulin (ii), fructo-oligosaccharide (FOS) (iii), and without added carbon source as negative control (iv). Protein base media had chicken egg and coconut juice, baker's yeast and potassium chloride (i), with 9% FOS (ii), or inulin (iii), or 7.34% whey protein (iv) to verify growth. All the probiotics were able to utilize inulin and FOS to growth. The numbers of cells increased with incubation time. However, L. plantarum produced an acidic in the selective culture medium significantly. Protein based with FOS and inulin added supported all probiotics growth. In addition, acetic acid content was the highest among short-chain fatty acids (SCFAs) produced. B. longum produced acetic acid very fast within 24 h. L. plantarum cultured in inulin added provided the peak level of acetic acid at 72 h. However, S. cerevisiae tended to decrease the SCFAs with incubation time.
Journal of molecular evolution, 2017
FAD and NAD(P) together represent an ideal pair for coupled redox reactions in their capacity to ... more FAD and NAD(P) together represent an ideal pair for coupled redox reactions in their capacity to accept two electrons and their redox potentials. Enzymes that bind both NAD(P) and FAD represent large superfamilies that fulfill essential roles in numerous metabolic pathways. Adrenodoxin reductase (AdxR) shares Rossmann fold features with some of these superfamilies but remains in a group of its own in the absence of sequence homology. This article documents the phylogenetic distribution of AdxR by examining whole genome databases for Metazoa, Plantae, Fungi, and Protista, and determines the conserved structural features of AdxR. Scanning these databases showed that most organisms have a single gene coding for an AdxR ortholog. The sequence identity between AdxR orthologs is correlated with the phylogenetic distance among metazoan species. The NADP binding site of all AdxR orthologs showed a modified Rossmann fold motif with a GxGxxA consensus instead of the classical GxGxxG at the ed...
Histochemistry and cell biology, Jan 27, 2017
A major function of the skin is the regulation of body temperature by sweat secretions. Sweat gla... more A major function of the skin is the regulation of body temperature by sweat secretions. Sweat glands secrete water and salt, especially NaCl. Excreted water evaporates, cooling the skin surface, and Na(+) ions are reabsorbed by the epithelial sodium channels (ENaC). Mutations in ENaC subunit genes lead to a severe multi-system (systemic) form of pseudohypoaldosteronism (PHA) type I, characterized by salt loss from aldosterone target organs, including sweat glands in the skin. In this study, we mapped the sites of localization of ENaC in the human skin by confocal microscopy using polyclonal antibodies generated against human αENaC. Our results reveal that ENaC is expressed strongly in all epidermal layers except stratum corneum, and also in the sebaceous glands, eccrine glands, arrector pili smooth muscle cells, and intra-dermal adipocytes. In smooth muscle cells and adipocytes, ENaC is co-localized with F-actin. No expression of ENaC was detected in the dermis. CFTR is strongly exp...
Gene, 2016
The epithelial sodium channel (ENaC) is composed of three homologous subunits and allows the flow... more The epithelial sodium channel (ENaC) is composed of three homologous subunits and allows the flow of Na + ions across high resistance epithelia, maintaining body salt and water homeostasis. ENaC dependent reabsorption of Na + in the kidney tubules regulates extracellular fluid (ECF) volume and blood pressure by modulating osmolarity. In multi-ciliated cells, ENaC is located in cilia and plays an essential role in the regulation of epithelial surface liquid volume necessary for cilial transport of mucus and gametes in the respiratory and reproductive tracts respectively. The subunits that form ENaC (named as alpha, beta, gamma and delta, encoded by genes SCNN1A, SCNN1B, SCNN1G, and SCNN1D) are members of the ENaC/Degenerin superfamily. The earliest appearance of ENaC orthologs is in the genomes of the most ancient vertebrate taxon, Cyclostomata (jawless vertebrates) including lampreys, followed by earliest representatives of Gnathostomata (jawed vertebrates) including cartilaginous sharks. Among Euteleostomi (bony vertebrates), Actinopterygii (ray finned-fishes) branch has lost ENaC genes. Yet, most animals in the Sarcopterygii (lobe-finned fish) branch including Tetrapoda, amphibians and amniotes (lizards, crocodiles, birds, and mammals), have four ENaC paralogs. We compared the sequences of ENaC orthologs from 20 species and established criteria for the identification of ENaC orthologs and paralogs, and their distinction from other members of the ENaC/Degenerin superfamily, especially ASIC family. Differences between ENaCs and ASICs are summarized in view of their physiological functions and tissue distributions. Structural motifs that are conserved throughout vertebrate ENaCs are highlighted. We also present a comparative overview of the genotype-phenotype relationships in inherited diseases associated with ENaC mutations, including multisystem pseudohypoaldosteronism (PHA1B), Liddle syndrome, cystic fibrosis-like disease and essential hypertension.
Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology, Jan 20, 2015
The Rossmann fold is one of the most common and widely distributed super-secondary structures. It... more The Rossmann fold is one of the most common and widely distributed super-secondary structures. It is composed of a series of alternating beta strand (β) and alpha helical (α) segments wherein the β-strands are hydrogen bonded forming a β-sheet. The initial beta-alpha-beta (βαβ) fold is the most conserved segment of Rossmann folds. As this segment is in contact with the ADP portion of dinucleotides such as FAD, NAD, and NADP it is also called as an "ADP-binding βαβ fold". The Proteopedia entry on the Rossmann fold (Available at: http://proteopedia.org/w/Rossmann_fold) was generated to illustrate several structural aspects of super families of FAD and NAD(P) binding proteins: (1) The coenzymes FAD and NAD(P) share the basic adenosine diphosphate (ADP) structure. (2) The βαβ fold motif that is common to both FAD and NAD(P) binding enzymes accommodates the common ADP component of these two coenzymes. (3) In both FAD and NAD(P) binding sites, the tight turn between the first β-...
Journal of Cell Biology, 1990
Advances in Molecular and Cell Biology, 1996
IUPHAR/BPS Guide to Pharmacology CITE, 2021
The epithelial sodium channels (ENaC) are located on the apical membrane of epithelial cells in t... more The epithelial sodium channels (ENaC) are located on the apical membrane of epithelial cells in the kidney tubules, lung, respiratory tract, male and female reproductive tracts, sweat and salivary glands, placenta, colon, and some other organs [9, 13, 22, 21, 42]. In these epithelia, Na+ ions flow from the extracellular fluid into the cytoplasm of epithelial cells via ENaC. The Na+ ions are then pumped out of the cytoplasm into the interstitial fluid by the Na+/K+ ATPase located on the basolateral membrane [36]. As Na+ is one of the major electrolytes in the extracellular fluid (ECF), osmolarity change initiated by the Na+ flow is accompanied by a flow of water accompanying Na+ ions [6]. Thus, ENaC has a central role in regulating ECF volume and blood pressure, primarily via its function in the kidney [37]. The expression of ENaC subunits, hence its activity, is regulated by the renin-angiotensin-aldosterone system, and other factors involved in electrolyte homeostasis [37, 30]. In ...
The FEBS Journal, 2016
The acid-sensing ion channels (ASICs) and epithelial sodium channels (ENaC) are members of a supe... more The acid-sensing ion channels (ASICs) and epithelial sodium channels (ENaC) are members of a superfamily of channels that play critical roles in mechanosensation, chemosensation, nociception, and regulation of blood volume and pressure. These channels look and function like a tripartite funnel that directs the flow of Na + ions into the cytoplasm via the channel pore in the membrane. The subunits that form these channels share a common structure with two transmembrane segments (TM1 and TM2) and a large extracellular part. In most vertebrates, there are five paralogous genes that code for ASICs (ASIC1-ASIC5), and four for ENaC subunits alpha, beta, gamma, and delta (a, b, c, and d). While ASICs can form functional channels as a homo-or heterotrimer, ENaC functions as an obligate heterotrimer composed of a-b-c or b-c-d subunits. The structure of ASIC has been determined in several conformations, including desensitized and open states. This review presents a comparison of the structures of these states using easy-to-understand molecular models of the full complex, the central tunnel that includes an outer vestibule, the channel pore, and ion selectivity filter. The differences in the secondary, tertiary, and quaternary structures of the states are summarized to pinpoint the conformational changes responsible for channel opening. Results of site-directed mutagenesis studies of ENaC subunits are examined in light of ASIC1 models. Based on these comparisons, a molecular model for the selectivity filter of ENaC is built by in silico mutagenesis of an ASIC1 structure. These models suggest that Na + ions pass through the filter in a hydrated state.
THE CONCISE GUIDE TO PHARMACOLOGY 2021/22: Ion channels
British Journal of Pharmacology
IUPHAR/BPS Guide to Pharmacology CITE
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Papers by Israel Hanukoglu