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Book: Toxicology of metals

Ballatori, Nazzareno / Goyer, Robert A.

biochemical aspects

(Handbook of experimental pharmacology ; 115)

1995

Author's details	contributors N. Ballatori ... Ed. Robert A. Goyer
Series title	Handbook of experimental pharmacology ; 115
Collection
Keywords	Metals / toxicity ; Maximum Permissible Exposure Level ; Metall ; Toxikologie ; Physiologische Chemie
Subject	Chemische Physiologie ; Biochemische Medizin ; Medizinische Biochemie ; Giftkunde ; Klinische Toxikologie ; Metalle
Language	English
Size	XXII, 467 S. : graph. Darst.
Publisher	Springer
Publishing place	Berlin u.a.
Document type	Book
HBZ-ID	HT006488859
ISBN	3-540-58281-9 ; 0-387-58281-9 ; 978-3-540-58281-6 ; 978-0-387-58281-8
Database	Catalogue ZB MED Medicine, Health

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Article ; Online: Pleiotropic functions of the organic solute transporter Ostα-Ostβ.

Ballatori, Nazzareno

Digestive diseases (Basel, Switzerland)

2011 Volume 29, Issue 1, Page(s) 13–17

Abstract: The heteromeric organic solute transporter alpha-beta (Ostα-Ostβ) is expressed at relatively high levels on the basolateral membrane of enterocytes, where it plays a critical role in the intestinal absorption of bile acids and the enterohepatic ... ...

Abstract	The heteromeric organic solute transporter alpha-beta (Ostα-Ostβ) is expressed at relatively high levels on the basolateral membrane of enterocytes, where it plays a critical role in the intestinal absorption of bile acids and the enterohepatic circulation. However, this transporter is also expressed in nearly all human tissues, including those that are not normally thought to be involved in bile acid homeostasis, indicating that Ostα-Ostβ may have additional roles beyond bile acid transport in these other tissues, or that bile acids and their derivatives are more pervasive than currently envisioned. Emerging data from different laboratories provide support for both of these hypotheses. In particular, recent studies indicate that tissues such as brain and ovary have the capacity to synthesize bile acids or bile acid precursors. In addition, studies examining Ostα-Ostβ substrate specificity have revealed that this transporter can also accept conjugated steroids, including some neurosteroids, and that the transporter is selectively expressed in steroidogenic cells of the brain and adrenal gland, suggesting a novel function for Ostα-Ostβ. The broad tissue expression of Ostα-Ostβ is also consistent with the emerging concept that bile acids and their derivatives act as signaling molecules in diverse tissues. Bile acids activate nuclear receptors such as the farnesoid X receptor (FXR/NR1H4), the pregnane X receptor and the vitamin D receptor, are ligands for a G-protein-coupled bile acid receptor (GPBAR1/TGR5), and can also activate protein kinases A and C as well as mitogen-activated protein kinase pathways. These signaling pathways are present in many tissues and regulate processes such as triglyceride, glucose and energy homeostasis. Note that although FXR and TGR5 are thought to function primarily as bile acid receptors, they are modulated by some other sterols and select lipid metabolites, and are also widely expressed in tissues, indicating a complex interplay among diverse regulatory networks that impact critical cell and organ functions. The present report summarizes the evidence for a pleiotropic role of Ostα-Ostβ in different tissues.
MeSH term(s)	Animals ; Bile Acids and Salts/metabolism ; Humans ; Membrane Transport Proteins/metabolism ; Organ Specificity ; Receptors, Cytoplasmic and Nuclear/metabolism ; Sterols/metabolism
Chemical Substances	Bile Acids and Salts ; Membrane Transport Proteins ; Receptors, Cytoplasmic and Nuclear ; Sterols
Language	English
Publishing date	2011-06-17
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	632798-9
ISSN	1421-9875 ; 0257-2753
ISSN (online)	1421-9875
ISSN	0257-2753
DOI	10.1159/000324123
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Article: Biology of a novel organic solute and steroid transporter, OSTalpha-OSTbeta.

Ballatori, Nazzareno

Experimental biology and medicine (Maywood, N.J.)

2005 Volume 230, Issue 10, Page(s) 689–698

Abstract: Using a comparative approach, recent studies have identified and functionally characterized a new type of organic solute and steroid transporter (OST) from skate, mouse, rat, and human genomes. In contrast to all other organic anion transporters ... ...

Abstract	Using a comparative approach, recent studies have identified and functionally characterized a new type of organic solute and steroid transporter (OST) from skate, mouse, rat, and human genomes. In contrast to all other organic anion transporters identified to date, transport activity requires the coexpression of two distinct gene products, a predicted 340-amino acid, seven-transmembrane (TM) domain protein (OSTalpha) and a putative 128-amino acid, single-TM domain ancillary polypeptide (OSTbeta). When OSTalpha and OSTbeta are coexpressed in Xenopus oocytes, they are able to mediate transport of estrone 3-sulfate, dehydroepiandrosterone 3- sulfate, taurocholate, digoxin, and prostaglandin E2, indicating a role in the disposition of key cellular metabolites or signaling molecules. OSTalpha and OSTbeta are expressed at relatively high levels in intestine, kidney, and liver, but they are also expressed at lower levels in many human tissues. Indirect immunofluorescence microscopy revealed that intestinal OSTalpha and OSTbeta proteins are localized to the baso-lateral membrane of mouse enterocytes. In MDCK cells, mouse Ostalpha-Ostbeta mediated the vectorial movement of taurocholate from the apical to the basolateral membrane, but not in the opposite direction, indicating basolateral efflux of bile acids. Overall, these findings indicate that OSTalpha-OSTbeta is a heteromeric transporter that is localized to the basolateral membrane of specific epithelial tissues and serves to regulate the export and disposition of bile acids and structurally related compounds from the cell. If confirmed, this model would have important implications for the body's handling of various steroid-derived molecules and may provide a new pharmacologic target for altering sterol homeostasis.
MeSH term(s)	Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Biological Transport ; Cell Membrane/metabolism ; Humans ; Models, Molecular ; Molecular Sequence Data ; Organic Anion Transporters/chemistry ; Organic Anion Transporters/genetics ; Organic Anion Transporters/isolation & purification ; Organic Anion Transporters/physiology ; Phylogeny ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid ; Steroids/metabolism ; Tissue Distribution
Chemical Substances	Organic Anion Transporters ; Steroids
Language	English
Publishing date	2005-10-12
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, P.H.S. ; Review
ISSN	1535-3702
ISSN	1535-3702
DOI	10.1177/153537020523001001
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Article ; Online: Measurement of hepatobiliary transport.

Ballatori, Nazzareno

Current protocols in toxicology

2004 Volume Chapter 14, Page(s) Unit14.5

Abstract: A major hepatic function involves the removal of xenobiotics from portal blood and their subsequent storage, metabolism, and excretion into bile, or delivery of various products back into the bloodstream. Transport across the liver cell basolateral (or ... ...

Abstract	A major hepatic function involves the removal of xenobiotics from portal blood and their subsequent storage, metabolism, and excretion into bile, or delivery of various products back into the bloodstream. Transport across the liver cell basolateral (or sinusoidal) plasma membrane is a key step in the overall metabolism of many compounds, whereas transport across the apical (or canalicular) plasma membrane into bile is often the principal pathway for their elimination. Although significant progress has been made in the molecular identification of the transport proteins that mediate these processes, much remains to be learned about regulation and physiological integration. The critical limiting factor in studying biliary excretion is that the bile canaliculus is very small (~1 µm in diameter) and is generally inaccessible to sampling by conventional approaches. The bile canalicular membrane is a specialized part of the hepatocellular plasma membrane, such that bile is separated from blood plasma only by the tight junctions that encircle each hepatocyte. Because hepatocyte polarity is rapidly lost during cell isolation, most cell culture models provide only limited information on mechanisms of biliary excretion. Thus, biliary secretion has been studied using four major experimental models: canalicular plasma membrane vesicles, cultured hepatocyte couplets, perfused liver, and in vivo (bile duct-cannulated animals). This unit describes basic methods for collecting bile from anesthetized mice and rats, for carrying out isolated perfused rat liver studies, and for the simultaneous isolation of plasma membrane vesicles derived from the basolateral and canalicular domains of rat liver.
MeSH term(s)	Animals ; Bile/metabolism ; Biliary Tract/metabolism ; In Vitro Techniques ; Liver/metabolism ; Male ; Mice ; Rats ; Rats, Sprague-Dawley
Language	English
Publishing date	2004-05
Publishing country	United States
Document type	Journal Article
ISSN	1934-9262
ISSN (online)	1934-9262
DOI	10.1002/0471140856.tx1405s19
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Article: Transport of toxic metals by molecular mimicry.

Ballatori, Nazzareno

Environmental health perspectives

2002 Volume 110 Suppl 5, Page(s) 689–694

Abstract: Intracellular concentrations of essential metals are normally maintained within a narrow range, whereas the nonessential metals generally lack homeostatic controls. Some of the factors that contribute to metal homeostasis have recently been identified at ...

Abstract	Intracellular concentrations of essential metals are normally maintained within a narrow range, whereas the nonessential metals generally lack homeostatic controls. Some of the factors that contribute to metal homeostasis have recently been identified at the molecular level and include proteins that mediate import of essential metals from the extracellular environment, those that regulate delivery to specific intracellular proteins or compartments, and those that mediate metal export from the cell. Some of these proteins appear highly selective for a given essential metal; however, others are less specific and interact with multiple metals, including toxic metals. For example, DCT1 (divalent cation transporter-1; also known as NRAMP2 or DMT1) is considered to be a major cellular uptake mechanism for Fe(2+) and other essential divalent metals, but this protein also mediates uptake of Cd(2+), Pb(2+), and possibly of other toxic divalent metals. The ability of nonessential metals to interact with binding sites for essential metals is critical for their ability to gain access to specific cellular compartments and for their ability to disrupt normal biochemical or physiological functions. Another major mechanism by which metals traverse cell membranes and produce cell injury is by forming complexes whose overall structures mimic those of endogenous molecules. For example, it has long been known that arsenate and vanadate can compete with phosphate for transport and metabolism, thereby disrupting normal cellular functions. Similarly, cromate and molybdate can mimic sulfate in biological systems. Studies in our laboratory have focused on the transport and toxicity of methylmercury (MeHg) and inorganic mercury. Mercury has a high affinity for reduced sulfhydryl groups, including those of cysteine and glutathione (GSH). MeHg-l-cysteine is structurally similar to the amino acid methionine, and this complex is a substrate for transport systems that carry methionine across cell membranes. Once MeHg has entered the cell, some of it binds to GSH, and the resulting MeHg-glutathione complex appears to be a substrate for proteins that mediate cellular export of glutathione S-conjugates, including the apically located MRP2 (multidrug resistance-associated protein 2) transporter, a member of the adenosine triphosphate-binding cassette protein superfamily. Because other toxic metals also form complexes with endogenous molecules, comparable mechanisms may be involved in their membrane transport and disposition.
MeSH term(s)	Animals ; Biological Transport ; Cell Membrane ; Glutathione/chemistry ; Humans ; Mercury/chemistry ; Mercury/pharmacokinetics ; Mercury/toxicity ; Metals/chemistry ; Metals/pharmacokinetics ; Metals/toxicity ; Methylmercury Compounds/chemistry ; Methylmercury Compounds/pharmacokinetics ; Methylmercury Compounds/toxicity ; Structure-Activity Relationship
Chemical Substances	Metals ; Methylmercury Compounds ; Mercury (FXS1BY2PGL) ; Glutathione (GAN16C9B8O)
Language	English
Publishing date	2002-10
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	195189-0
ISSN	1552-9924 ; 0091-6765 ; 1078-0475
ISSN (online)	1552-9924
ISSN	0091-6765 ; 1078-0475
DOI	10.1289/ehp.02110s5689
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Article: The iron transporter ferroportin can also function as a manganese exporter.

Madejczyk, Michael S / Ballatori, Nazzareno

Biochimica et biophysica acta

2011 Volume 1818, Issue 3, Page(s) 651–657

Abstract: The present study examined the hypothesis that the iron exporter ferroportin (FPN1/SLC40A1) can also mediate cellular export of the essential trace element manganese, using Xenopus laevis oocytes expressing human FPN1. When compared to oocytes expressing ...

Abstract	The present study examined the hypothesis that the iron exporter ferroportin (FPN1/SLC40A1) can also mediate cellular export of the essential trace element manganese, using Xenopus laevis oocytes expressing human FPN1. When compared to oocytes expressing only the divalent metal transporter-1 (DMT1/NRAMP2), (54)Mn accumulation was lower in oocytes also expressing FPN1. FPN1-expressing oocytes exported more (54)Mn than control oocytes (26.6±0.6% versus 7.1±0.5%, respectively, over 4h at pH 7.4 when preloaded with approximately 16μM (54)Mn); however, there was no difference in (54)Mn uptake between control and FPN1-expressing oocytes. FPN1-mediated Mn export was concentration dependent and could be partially cis-inhibited by 100μM Fe, Co, and Ni, but not by Rb. In addition, Mn export ability was significantly reduced when the extracellular pH was reduced from 7.4 to 5.5, and when Na(+) was substituted with K(+) in the incubation media. These results indicate that Mn is a substrate for FPN1, and that this export process is inhibited by a low extracellular pH and by incubation in a high K(+) medium, indicating the involvement of transmembrane ion gradients in FPN1-mediated transport.
MeSH term(s)	Animals ; Cation Transport Proteins/genetics ; Cation Transport Proteins/metabolism ; Gene Expression ; Hep G2 Cells ; Humans ; Ion Transport/physiology ; Manganese/metabolism ; Oocytes/cytology ; Oocytes/metabolism ; Xenopus laevis
Chemical Substances	Cation Transport Proteins ; metal transporting protein 1 ; solute carrier family 11- (proton-coupled divalent metal ion transporters), member 2 ; Manganese (42Z2K6ZL8P)
Language	English
Publishing date	2011-12-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamem.2011.12.002
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Article: Ostα-/- mice are not protected from western diet-induced weight gain.

Hammond, Christine L / Wheeler, Sadie G / Ballatori, Nazzareno / Hinkle, Patricia M

Physiological reports

2015 Volume 3, Issue 1

Abstract: Organic solute transporterα-OSTβ is a bile acid transporter important for bile acid recycling in the enterohepatic circulation. In comparison to wild-type mice, Ostα(-/-) mice have a lower bile acid pool and increased fecal lipids and they are relatively ...

Abstract	Organic solute transporterα-OSTβ is a bile acid transporter important for bile acid recycling in the enterohepatic circulation. In comparison to wild-type mice, Ostα(-/-) mice have a lower bile acid pool and increased fecal lipids and they are relatively resistant to age-related weight gain and insulin resistance. These studies tested whether Ostα(-/-) mice are also protected from weight gain, lipid changes, and insulin resistance which are normally observed with a western-style diet high in both fat and cholesterol (WD). Wild-type and Ostα(-/-) mice were fed a WD, a control defined low-fat diet (LF) or standard laboratory chow (CH). Surprisingly, although the Ostα(-/-) mice remained lighter on LF and CH diets, they weighed the same as wild-type mice after 12 weeks on the WD even though bile acid pool levels remained low and fecal lipid excretion remained elevated. Mice of both genotypes excreted relatively less lipid when switched from CH to LF or WD. WD caused slightly greater changes in expression of genes involved in lipid transport in the small intestines of Ostα(-/-) mice than wild-type, but the largest differences were between CH and defined diets. After WD feeding, Ostα(-/-) mice had lower serum cholesterol and hepatic lipids, but Ostα(-/-) and wild-type mice had equivalent levels of muscle lipids and similar responses in glucose and insulin tolerance tests. Taken together, the results show that Ostα(-/-) mice are able to adapt to a western-style diet despite low bile acid levels.
Language	English
Publishing date	2015-01-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	2724325-4
ISSN	2051-817X
ISSN	2051-817X
DOI	10.14814/phy2.12263
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Article: Transport of Toxic Metals by Molecular Mimicry

Ballatori, Nazzareno

2002 , Page(s) S. 689–694

Abstract: Several metal transport mechanisms have recently been identified at the molecular level, and investigators are beginning to examine their structure, function, and regulation. Many of these transporters have thus far been identified only at the cDNA level, ...

Abstract	Several metal transport mechanisms have recently been identified at the molecular level, and investigators are beginning to examine their structure, function, and regulation. Many of these transporters have thus far been identified only at the cDNA level, and there is comparatively little information on their cellular and subcellular localization, their functional orientation in the membrane (uptake or efflux), driving force, substrate selectivity, or regulation under physiological and pathophysiological conditions. It is likely that additional families of metal-specific transporters will be identified in the near future and that many new members of existing families will be described.
Keywords	Toxische Metalle ; Mimikry ; Schadstoffausbreitung ; Membran ; Protein ; Zelle ; Leber ; Blut ; Zink ; Kupfer ; Sulfat ; Phosphat ; Stofftransport ; Biochemie ; Physiologie ; Blutplasma ; Zellmembran ; Komplexverbindung ; Mensch
Language	English
Document type	Article
Database	OPAC and Environmental database (ULIDAT) of The Federal Environment Agency (UBA)

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Article ; Online: The heteromeric organic solute transporter, OSTα-OSTβ/SLC51: a transporter for steroid-derived molecules.

Ballatori, Nazzareno / Christian, Whitney V / Wheeler, Sadie G / Hammond, Christine L

Molecular aspects of medicine

2013 Volume 34, Issue 2-3, Page(s) 683–692

Abstract: The organic solute transporter alpha-beta (OSTα-OSTβ) is one of the newest members of the solute carrier family, designated as SLC51, and arguably one of the most unique. The transporter is composed of two gene products encoded by SLC51A and SLC51B that ... ...

Abstract	The organic solute transporter alpha-beta (OSTα-OSTβ) is one of the newest members of the solute carrier family, designated as SLC51, and arguably one of the most unique. The transporter is composed of two gene products encoded by SLC51A and SLC51B that heterodimerize to form the functional transporter complex. SLC51A encodes OSTα, a predicted 340-amino acid, 7-transmembrane (TM) domain protein, whereas SLC51B encodes OSTβ, a putative 128-amino acid, single-TM domain polypeptide. Heterodimerization of the two subunits increases the stability of the individual proteins, facilitates their post-translational modification, and is required for delivery of the functional transporter complex to the plasma membrane. There are no paralogues for SLC51A or SLC51B in any genome that has been examined. The transporter functions via a facilitated diffusion mechanism, and can mediate either efflux or uptake depending on the electrochemical gradient of its substrates. Overall, characterization of the transporter's substrate specificity, transport mechanism, tissue distribution, subcellular localization, and transcriptional regulation as well as the phenotype of the recently generated Slc51a-deficient mice have revealed that OSTα-OSTβ plays a central role in the transport of bile acids, conjugated steroids, and structurally-related molecules across the basolateral membrane of many epithelial cells. In particular, OSTα-OSTβ appears to be essential for intestinal bile acid absorption, and thus for dietary lipid absorption.
MeSH term(s)	Amino Acid Sequence ; Base Sequence ; Bile Acids and Salts/metabolism ; Computational Biology ; Dimerization ; Enterocytes/metabolism ; Gonadal Steroid Hormones/metabolism ; Humans ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Membrane Transport Proteins/physiology ; Models, Biological ; Molecular Sequence Data ; Multigene Family ; Phylogeny ; Sequence Analysis, DNA
Chemical Substances	Bile Acids and Salts ; Gonadal Steroid Hormones ; Membrane Transport Proteins ; organic solute transporter alpha, human ; SLC51B protein, human
Language	English
Publishing date	2013-03-18
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	197640-0
ISSN	1872-9452 ; 0098-2997
ISSN (online)	1872-9452
ISSN	0098-2997
DOI	10.1016/j.mam.2012.11.005
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Article ; Online: Organic solute transporter, OSTalpha-OSTbeta: its role in bile acid transport and cholestasis.

Soroka, Carol J / Ballatori, Nazzareno / Boyer, James L

Seminars in liver disease

2010 Volume 30, Issue 2, Page(s) 178–185

Abstract: Organic solute transporter alpha-beta (OSTalpha-OSTbeta) is a unique heteromeric transporter localized to the basolateral membrane of epithelial cells involved in sterol transport. It is believed to be the primary bile acid efflux transporter in the ... ...

Abstract	Organic solute transporter alpha-beta (OSTalpha-OSTbeta) is a unique heteromeric transporter localized to the basolateral membrane of epithelial cells involved in sterol transport. It is believed to be the primary bile acid efflux transporter in the intestine of mammals and is therefore essential to bile acid homeostasis and the enterohepatic circulation. First described in the evolutionarily primitive small skate, LEUCORAJA ERINACEA, this facilitated transporter requires expression of both subunits for its function. It can transport a variety of bile acids, as well as estrone 3-sulfate, dehydroepiandrosterone 3-sulfate, digoxin, and prostaglandin E (2). Expression of both subunits is variable between species and tissues; in humans high expression is noted in the liver, small intestine, kidney, testis, and adrenal gland. OSTalpha-OSTbeta is directly regulated by the bile acid sensing nuclear receptor, farnesoid X receptor (FXR). Furthermore, it is part of the complex regulatory pathway that controls bile acid synthesis and homeostasis. Hepatic OSTalpha-OSTbeta is upregulated in cholestasis in both humans and rodents, where it appears to play a protective role. Additional studies are necessary to determine its role in liver injury, bile acid malabsorption, and lipid and glucose metabolism, as well as a potential protective role for kidney OSTalpha-OSTbeta in cholestasis.
MeSH term(s)	ATP Binding Cassette Transporter, Subfamily B/physiology ; Adaptation, Physiological/physiology ; Animals ; Bile Acids and Salts/metabolism ; Cholestasis/physiopathology ; Enterohepatic Circulation/physiology ; Homeostasis/physiology ; Humans ; Kidney/physiopathology ; Liver/physiopathology ; Membrane Transport Proteins/metabolism ; Membrane Transport Proteins/physiology ; Mice ; Substrate Specificity/physiology
Chemical Substances	ATP Binding Cassette Transporter, Subfamily B ; Bile Acids and Salts ; Membrane Transport Proteins ; organic solute transporter alpha, human ; organic solute transporter alpha, mouse ; SLC51B protein, human ; organic solute transporter beta, mouse
Language	English
Publishing date	2010-04-26
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	603177-8
ISSN	1098-8971 ; 0272-8087
ISSN (online)	1098-8971
ISSN	0272-8087
DOI	10.1055/s-0030-1253226
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