Depletion of glutathione attenuates response of bone marrow stem cells to stromal cell-derived factor -1 [2007](IR91)

Depletion of glutathione attenuates response of bone marrow stem cells to stromal cell-derived factor -1 [2007](IR91)BK

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Depletion of glutathione attenuates response of bone marrow stem cells to stromal cell-derived factor -1

http://www.fasebj.org/cgi/content/meeting_abstract/21/6/A737-b
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FASEB J.
April 2007
21 (Meeting Abstract Supplement) A737

(The FASEB Journal. 2007;21:702.12)
© 2007 FASEB
702.12
Depletion of glutathione attenuates response of bone marrow stem cells to stromal cell-derived factor -1
Smita Swaminathan Iyer1, Jianguo Xu2, Dean P Jones2, Kenneth Brigham2 and Mauricio Rojas2
1 Nutrition and Health Sciences Program, Emory University, 615,Michael Street, 215 Whitehead Bldg, Emory University, Atlanta, GA, 30322,
2 Division of Pulmonary Allergy and Critical Care Medicine, Department of Medicine, Emory University, 615,Michael Street, 205,Whitehead Bldg, Emory University, Atlanta, GA, 30322

ABSTRACT

In adult organisms, stem cells, found primarily in the bone marrow and in low numbers in other organs, are mobilized to the injured tissue where they participate in the repair process. Stromal cell-derived factor -1a (SDF-1a) is critical for stem cell trafficking during injury. Very little is known about how nutrition affects this process. Our objectives were to determine how Glutathione (GSH) depletion, observed with aging and in numerous chronic disease states, affects the functional response of bone marrow cells to SDF-1a.

Bone marrow stem cells (BMSC) from 8 week old C57BL/6J mice were isolated, and were cultured for 24 hours in buthionine sulfoximine (BSO), an inhibitor of GSH synthesis. SDF-1a (120 ng/ml) dependent chemotaxis was determined in viable cells, over 3 hours, using a modified Boyden chamber method. We found a 5 fold decline in migration, in cells depleted of GSH compared to control.

Our data show that GSH is important in the directional migration of BMSC to SDF-1a and indicate that signal transduction pathways initiated by SDF-1a may be redox sensitive. Therefore, in states of chronic oxidative imbalance, stem cell response to SDF-1a may be attenuated slowing tissue regeneration and repair. As nutrition can impact levels of GSH, dietary control of antioxidant status may provide an opportunity to enhance repair and improve recovery in patients with injury.

Classifications
Cellular Mechanisms of Nutritional Modulation in Immunity
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The role of glutathione in radiation and drug induced cytotoxicity. [1987](IR91){These studies demonstrate that GSH modulation may have a major impact on the cytotoxicity of redox active drugs}.png

December 23, 2010; 06:11:10 p.m. Taipei Time

The role of glutathione in radiation and drug induced cytotoxicity. [1987](IR91).png

The role of glutathione in radiation and drug induced cytotoxicity. [1987](IR91){Diagrammatic representation of the inter-relationship of GSH with other cellular systems.}.png

The role of glutathione in radiation and drug induced cytotoxicity. [1987](IR91){These studies demonstrate that GSH modulation may have a major impact on the cytotoxicity of redox active drugs}.png

Keywords:

Clock, Watch, GSH, glutathione, interaction, mechanism, intricacy, 錯綜複雜的事物（或細節）

Glutathione Transport Is a Unique Function of the ATP-binding Cassette Protein ABCG2 [2010[(IR91)

Glutathione Transport Is a Unique Function of the ATP-binding Cassette Protein ABCG2 [2010[(IR91)

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Glutathione Transport Is a Unique Function of the ATP-binding Cassette Protein ABCG2

http://www.jbc.org/content/285/22/16582
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First Published on March 23, 2010, doi: 10.1074/jbc.M109.090506
May 28, 2010 The Journal of Biological Chemistry, 285, 16582-16587.

Glutathione Transport Is a Unique Function of the ATP-binding Cassette Protein ABCG2 *
Heather M. Brechbuhl‡, Neal Gould§, Remy Kachadourian¶, Wayne R. Riekhof¶, Dennis R. Voelker¶ and Brian J. Day§¶‖**,1
- Author Affiliations

From the Departments of ‖Medicine,
**Immunology, and
§Pharmaceutical Sciences, University of Colorado Denver Health Sciences Center, Aurora, Colorado 80045 and
the Departments of ¶Medicine and
‡Pediatrics, National Jewish Health, Denver, Colorado 80206
1 To whom correspondence should be addressed: National Jewish Health, 1400 Jackson St., Denver, CO 80206. Tel.: 303-398-1121; Fax: 303-270-2263; E-mail: dayb@njhealth.org.
Abstract

Glutathione (GSH) transport is vital for maintenance of intracellular and extracellular redox balance. Only a few human proteins have been identified as transporters of GSH, glutathione disulfide (GSSG) and/or GSH conjugates (GS-X). Human epithelial MDA1586, A549, H1975, H460, HN4, and H157 cell lines were exposed to 2′,5′-dihydroxychalcone, which induces a GSH efflux response. A real-time gene superarray for 84 proteins found in families that have a known role in GSH, GSSG, and/or GS-X transport was employed to help identify potential GSH transporters. ABCG2 was identified as the only gene in the array that closely corresponded with the magnitude of 2′,5′-dihydroxychalcone (2′,5′-DHC)-induced GSH efflux. The role of human ABCG2 as a novel GSH transporter was verified in a Saccharomyces cerevisiae galactose-inducible gene expression system. Yeast expressing human ABCG2 had 2.5-fold more extracellular GSH compared with those not expressing ABCG2. GSH efflux in ABCG2-expressing yeast was abolished by the ABCG2 substrate methotrexate (10 μM), indicating competitive inhibition. In contrast, 2′,5′-DHC treatment of ABCG2-expressing yeast increased extracellular GSH levels in a dose-dependent manner with a maximum 3.5-fold increase in GSH after 24 h. In addition, suppression of ABCG2 with short hairpin RNA or ABCG2 overexpression in human epithelial cells decreased or increased extracellular GSH levels, respectively. Our data indicate that ABCG2 is a novel GSH transporter.

ABC Transporter Antioxidant Membrane Proteins Transport Amino Acids Yeast Glutathione
Footnotes

↵* This work was supported, in whole or in part, by National Institutes of Health Grants R01 HL084469 (to B. J. D.), R01 HL075523 (to B. J. D), R01 ES0175825, R37-GM32453 (to D. R. V), and 1F32-GM076798 (to W. R. R.). This work was also supported by American Cancer Society Great-West Division Postdoctoral Fellowship Award PF-06-288-01-CSM (to W. R. R.).

↵ The on-line version of this article (available at http://www.jbc.org) contains supplemental Experimental Procedures and additional references, Figs. 1–5, and Table 1.

Received December 2, 2009.
Revision received March 23, 2010.
© 2010 by The American Society for Biochemistry and Molecular Biology, Inc.
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ABCG2: structure, function and role in drug response. [2008](IR91)

ABCG2: structure, function and role in drug response. [2008](IR91)

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(Memo Item created on December 16, 2010 10:48 PM)
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ABCG2: structure, function and role in drug response.

http://www.ncbi.nlm.nih.gov/pubmed/18370855
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Expert Opin Drug Metab Toxicol. 2008 Jan;4(1):1-15.
ABCG2: structure, function and role in drug response.
Polgar O, Robey RW, Bates SE.
National Cancer Institute, Medical Oncology Branch, Center for Cancer Research, NIH, 9000 Rockville Pike, Building 10, Room 13N240, Bethesda, MD 20892, USA.

Abstract
ABCG2 was discovered in multi-drug-resistant cancer cells, with the identification of chemotherapeutic agents, such as mitoxantrone, flavopiridol, methotrexate and irinotecan as substrates. Later, drugs from other therapeutic groups were also described as substrates, including antibiotics, antivirals, HMG-CoA reductase inhibitors and flavonoids. An expanding list of compounds inhibiting ABCG2 has also been generated. The wide variety of drugs transported by ABCG2 and its normal tissue distribution with highest levels in the placenta (胎盤), intestine and liver, suggest a role in protection against xenobiotics. ABCG2 also has an important role in the pharmacokinetics (藥物動力學) of its substrates. Single nucleotide polymorphisms of the gene were shown to alter either plasma concentrations of substrate drugs or levels of resistance against chemotherapeutic agents in cell lines. ABCG2 was also described as the determinant of the side population of stem cells. All these aspects of the transporter warrant further research aimed at understanding ABCG2's structure, function and regulation of expression.

PMID: 18370855 [PubMed - indexed for MEDLINE]
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(Memo Item created on December 16, 2010 10:51 PM)
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Common added by WeiJin Tang (湯偉晉)
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Known GSH transporter
Glutathione Transport Is a Unique Function of the ATP-binding Cassette Protein ABCG2

ABCG2 is a GSH transporter

Source; URL of the source or Name of the professional paper:
Glutathione Transport Is a Unique Function of the ATP-binding Cassette Protein ABCG2 [2010[(IR91)
http://www.jbc.org/content/285/22/16582
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(Memo Item created on December 16, 2010 10:56 PM)
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Auxiliary info for understanding this paper
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Pharmacokinetics
藥物動力學
pharmacokinetics (藥物動力學)

The branch of pharmacology concerned with the movement of drugs within the body.

The study of the action of drugs in the body: method and rate of excretion; duration of effect; etc.
Source:
wordnetweb.princeton.edu/perl/webwn

large intestine
大腸
small intestine
小腸
intestine
腸子

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Element (元素) – selenium (Se)(【化】硒) with 1s, 2s, 2p, 3s, 3p, 4s, 3d, 4p electron orbital (電子軌域)[2010-12-15]

Element (元素) – selenium (Se)(【化】硒) with 1s, 2s, 2p, 3s, 3p, 4s, 3d, 4p electron orbital (電子軌域) [2010-11-02] 01.png

Element (元素) – selenium (Se)(【化】硒) with 1s, 2s, 2p, 3s, 3p, 4s, 3d, 4p electron orbital (電子軌域) [2010-11-02] 02.png

Element (元素) – selenium (Se)(【化】硒) with 1s, 2s, 2p, 3s, 3p, 4s, 3d, 4p electron orbital (電子軌域) [2010-11-02] 03.png

Element (元素) – selenium (Se)(【化】硒) with 1s, 2s, 2p, 3s, 3p, 4s, 3d, 4p electron orbital (電子軌域) [2010-11-02] 04.png

Element (元素) – selenium (Se)(【化】硒) with 1s, 2s, 2p, 3s, 3p, 4s, 3d, 4p electron orbital (電子軌域) [2010-11-02] 05.png

Element (元素) – selenium (Se)(【化】硒) with 1s, 2s, 2p, 3s, 3p, 4s, 3d, 4p electron orbital (電子軌域) [2010-11-02] 06.png

Element (元素) – selenium (Se)(【化】硒) with 1s, 2s, 2p, 3s, 3p, 4s, 3d, 4p electron orbital (電子軌域) [2010-11-02] 07.png

Element (元素) – selenium (Se)(【化】硒) with 1s, 2s, 2p, 3s, 3p, 4s, 3d, 4p electron orbital (電子軌域) [2010-11-02] 08.png

Electron orbitals [2010-12-15]

Electron orbitals - 1s orbital [2010-05-16].GIF

Electron orbitals - 2s orbital [2010-05-16].GIF

Electron orbitals - p orbital [2010-05-16].GIF

Electron orbitals - The p orbitals at the second energy level are called 2px, 2py and 2pz [2010-05-16].GIF

Electron configuration of element B, C, N [2010-05-17].png

Electron configuration of element H [2010-05-17].png

Electron configuration of element K, Ca [2010-05-17].png

Electron configuration of element Mg, S, Ar [2010-05-17].png

Electron configuration of element Mn, Fe, Co, Ni, Cu, Zn [2010-05-17].png

Electron configuration of element O, F, Ne [2010-05-17].png

d-block elements in periodic table [2010-05-17].png

Electron orbitals and their associated energy level diagram (Note; energy not to scale) [2010-05-16](IR91) [2010-05-16].png

Filling of electrons in d-orbital [2010-05-17].png

Most popular pictures of the atom are wrong [2010-05-16].png

s- and p-block elements in periodic table [2010-05-17].png

Mass-spectrometric approaches to identify proteins and sequence peptides; Source#nih.gov (IR90)[2010-12-15]

Mass-spectrometric approaches to identify proteins and sequence peptides; Source#nih.gov (IR90)[2010-12-15] 01.png

United States Patent 7,557,182 [2009]{Molecules for transporting a compound across the blood-brain barrier}(IR91)

United States Patent 7,557,182 [2009]{Molecules for transporting a compound across the blood-brain barrier}(IR91)

FIELD OF THE INVENTION

The present invention relates to improvements in the field of drug delivery. More particularly, the invention relates to polypeptide, conjugates and pharmaceutical compositions comprising the polypeptides of the present invention and their use for transporting a compound or drug across the blood-brain barrier of an individual and in the treatment and diagnosis of neurological diseases.

BACKGROUND OF THE INVENTION

In the development of a new therapy for brain pathologies, the blood-brain barrier (BBB) is considered as a major obstacle for the potential use of drugs for treating disorders of the central nervous system (CNS). The global market for CNS drugs was $33 billion in 1998, which was roughly half that of global market for cardiovascular drugs, even though in the United States, nearly twice as many people suffer from CNS disorders as from cardiovascular diseases. The reason for this lopsidedness is that more than 98% of all potential CNS drugs do not cross the blood-brain barrier. In addition, more than 99% of worldwide CNS drug development is devoted solely to CNS drug discovery, and less than 1% is directed to CNS drug delivery. This ratio could explain why no efficient treatment is currently available for the major neurological diseases such as brain tumors, Alzheimer's and stroke.

The brain is shielded against potentially toxic substances by the presence of two barrier systems: the blood-brain barrier (BBB) and the blood-cerebrospinal fluid barrier (BCSFB). The BBB is considered to be the major route for the uptake of serum ligands since its surface area is approximately 5000-fold greater than that of BCSFB. The brain endothelium (內皮), which constitutes the BBB, represents the major obstacle for the use of potential drugs against many disorders of the CNS. As a general rule, only lipophilic molecules smaller than about 500 Daltons may pass across the BBB, i.e., from blood to brain. However, the size of many drugs that show promising results in animal studies for treating CNS disorders is considerably bigger. Thus, peptide and protein therapeutics are generally excluded from transport from blood to brain, owing to the negligible permeability of the brain capillary endothelial wall to these drugs. Brain capillary endothelial cells (BCECs) are closely sealed by tight junctions, possess few fenestrae and few endocytic vesicles as compared to capillaries of other organs. BCECs are surrounded by extracellular matrix, astrocytes, pericytes and microglial cells. The close association of endothelial cells with the astrocyte foot processes and the basement membrane of capillaries are important for the development and maintenance of the BBB properties that permit tight control of blood-brain exchange.

International publication WO2004/060403 discloses an invention made by the inventors relating to molecules for transporting a drug across the blood brain barrier. Otherwise, to date, there is no efficient drug delivery approach available for the brain. Methods under investigation for peptide and protein drug delivery to the brain may be divided in three principal strategies. Firstly, invasive procedures include the direct intraventricular administration of drugs by means of surgery, and the temporary disruption of the BBB via intracarotid infusion of hyperosmolar solutions. Secondly, the pharmacologically-based strategy consists in facilitating the passage through the BBB by increasing the lipid solubility of peptides or proteins. Thirdly, physiologic-based strategies exploit the various carrier mechanisms at the BBB, which have been characterized in the recent years. In this approach, drugs are attached to a protein vector that performs like receptors-targeted delivery vehicle on the BBB. This approach is highly specific and presents high efficacy with an extreme flexibility for clinical indications with unlimited targets. The latter approach has been, and is still, investigated by the inventors, who came up with the molecules described in the afore-mentioned publication and those of the present invention.

U.S. Pat. No. 5,807,980 describes Bovine Pancreatic Trypsin Inhibitor (aprotinin)-derived inhibitors as well as a method for their preparation and therapeutic use. These peptides are used for the treatment of a condition characterized by an abnormal appearance or amount of tissue factor and/or factor Villa such as abnormal thrombosis.

U.S. Pat. No. 5,780,265 describes serine protease inhibitors that are capable of inhibiting plasma kallikrein.

U.S. Pat. No. 5,118,668 describes Bovine Pancreatic Trypsin Inhibitor variants.

It would be highly desirable to be provided with improved molecules that can act as carriers or vectors for transporting a compound or drug across the BBB of an individual.

Choroid plexus protects cerebrospinal fluid against toxic metals [1991](IR91); The choroid plexus is the principal site of formation of the cerebrospinal fluid (CSF) which bathes the brain.

 

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Choroid plexus protects cerebrospinal fluid against toxic metals

http://www.fasebj.org/content/5/8/2188.abstract
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The FASEB Journal, Vol 5, 2188-2193, Copyright © 1991 by The Federation of American Societies for Experimental Biology

--------------------------------------------------------------------------------

RESEARCH COMMUNICATIONS

Choroid plexus protects cerebrospinal fluid against toxic metals
W Zheng, DF Perry, DL Nelson and HV Aposhian
Department of Pharmacology and Toxicology, University of Arizona, Tucson 86721.

Although heavy metal ions are known to be toxic to the central nervous system (CNS), the mechanisms by which the CNS may protect itself from initial challenges of such toxic ions is unknown. The choroid plexus is the principal site of formation of the cerebrospinal fluid (CSF) which bathes the brain. We have determined in rats and rabbits that after intraperitoneal administration of lead, cadmium, mercury, and arsenic compounds, these toxic metal ions accumulated in the lateral choroid plexus at concentrations of Pb, Hg, and As that were 70-, 95-, and 40- fold higher, respectively, than those found in the CSF. Cd was not detected in the CSF. In addition, concentrations of these heavy metal ions were found to be many fold greater in the choroid plexus than in the brain or blood. The accumulation of Pb in the choroid plexus was dose-dependent and time-related. When the choroid plexus was preincubated, in vitro, with ouabain (1.5 mM), the uptake of Cd from the CSF side of the choroid plexus was inhibited 57%. Cadmium metallothionein was not found in the choroid plexus. Whereas the concentration of reduced glutathione in the choroid plexus was less than that in the brain cortex, the concentration of cystine was fourfold greater. The lateral choroid plexus sequesters (使隔絕; 隔離) Pb, Cd, As, and Hg. It appears to be one of the important mechanisms that protects the CSF and the brain from the fluxes of toxic heavy metals in the blood.

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Normal alveolar epithelial lining fluid contains high levels of glutathione [1987](IR92)

Normal alveolar epithelial lining fluid contains high levels of glutathione [1987](IR92)

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(Memo Item created on November 15, 2010 11:01 AM)
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Normal alveolar epithelial lining fluid contains high levels of glutathione

http://jap.physiology.org/cgi/content/short/63/1/152
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J Appl Physiol 63: 152-157, 1987; 8750-7587/87 $5.00

Journal of Applied Physiology, Vol 63, Issue 1 152-157, Copyright © 1987 by American Physiological Society

ARTICLES

Normal alveolar epithelial lining fluid contains high levels of glutathione

A. M. Cantin, S. L. North, R. C. Hubbard and R. G. Crystal

The epithelial cells on the alveolar surface of the human lower respiratory tract are vulnerable to toxic oxidants derived from inhaled pollutants or inflammatory cells. Although these lung cells have intracellular antioxidants, these defenses may be insufficient to protect the epithelial surface against oxidants present at the alveolar surface. This study demonstrates that the epithelial lining fluid (ELF) of the lower respiratory tract contains large amounts of the sulfhydryl-containing antioxidant glutathione (GSH). The total glutathione (the reduced form GSH and the disulfide GSSG) concentration of normal ELF was 140-fold higher than that in plasma of the same individuals, and 96% of the glutathione in ELF was in the reduced form. Compared with nonsmokers, cigarette smokers had 80% higher levels of ELF total glutathione, 98% of which was in the reduced form. Studies of cultured lung epithelial cells and fibroblasts demonstrated that these concentrations of reduced glutathione were sufficient to protect these cells against the burden of H2O2 in the range released by alveolar macrophages removed from the lower respiratory tract of nonsmokers and smokers, respectively, suggesting that the glutathione present in the alveolar ELF of normal individuals likely contributes to the protective screen against oxidants in the extracellular milieu of the lower respiratory tract.

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Proceedings of the ATS, November 1, 2006; 3(8): 703 - 708. [Abstract] [Full Text] [PDF] T. Sato, K. Seyama, Y. Sato, H. Mori, S. Souma, T. Akiyoshi, Y. Kodama, T. Mori, S. Goto, K. Takahashi, et al.
Senescence Marker Protein-30 Protects Mice Lungs from Oxidative Stress, Aging, and Smoking
Am. J. Respir. Crit. Care Med., September 1, 2006; 174(5): 530 - 537. [Abstract] [Full Text] [PDF] I. Rahman and I. M. Adcock
Oxidative stress and redox regulation of lung inflammation in COPD.
Eur. Respir. J., July 1, 2006; 28(1): 219 - 242. [Abstract] [Full Text] [PDF] K Nagai, T Betsuyaku, T Kondo, Y Nasuhara, and M Nishimura
Long term smoking with age builds up excessive oxidative stress in bronchoalveolar lavage fluid
Thorax, June 1, 2006; 61(6): 496 - 502. [Abstract] [Full Text] [PDF] A. M. Cantin, J. W. Hanrahan, G. Bilodeau, L. Ellis, A. Dupuis, J. Liao, J. Zielenski, and P. Durie
Cystic Fibrosis Transmembrane Conductance Regulator Function Is Suppressed in Cigarette Smokers
Am. J. Respir. Crit. Care Med., May 15, 2006; 173(10): 1139 - 1144. [Abstract] [Full Text] [PDF] A. Papi, F. Luppi, F. Franco, and L. M. Fabbri
Pathophysiology of Exacerbations of Chronic Obstructive Pulmonary Disease
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Abnormalities in the Pulmonary Innate Immune System in Cystic Fibrosis
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Tomato juice prevents senescence-accelerated mouse P1 strain from developing emphysema induced by chronic exposure to tobacco smoke
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Oxidant stress suppresses CFTR expression
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Treatment of stable COPD: antioxidants
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Deletion of the Anaerobic Regulator HlyX Causes Reduced Colonization and Persistence of Actinobacillus pleuropneumoniae in the Porcine Respiratory Tract
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Focus on antioxidant enzymes and antioxidant strategies in smoking related airway diseases
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Role of Glutathione in Reproductive Tract Secretions on Mouse Preimplantation Embryo Development
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The Association of Acetaminophen, Aspirin, and Ibuprofen with Respiratory Disease and Lung Function
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Inflammatory markers in bronchoalveolar lavage fluid from human volunteers 2 hours after hydrogen fluoride exposure
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Glutathione: A Radical Treatment for Cystic Fibrosis Lung Disease?
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A Pilot Study of the Effect of Inhaled Buffered Reduced Glutathione on the Clinical Status of Patients With Cystic Fibrosis
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Alveolar antioxidant status in patients with acute respiratory distress syndrome
Eur. Respir. J., December 1, 2004; 24(6): 994 - 999. [Abstract] [Full Text] [PDF] A. Shukla, T. Flanders, K. M. Lounsbury, and B. T. Mossman
The {gamma}-Glutamylcysteine Synthetase and Glutathione Regulate Asbestos-induced Expression of Activator Protein-1 Family Members and Activity
Cancer Res., November 1, 2004; 64(21): 7780 - 7786. [Abstract] [Full Text] [PDF] K. M. Beeh, J. Beier, N. Koppenhoefer, and R. Buhl
Increased Glutathione Disulfide and Nitrosothiols in Sputum Supernatant of Patients With Stable COPD
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Impact of 30-Day Oral Dosing with N-acetyl-L-cysteine on Sprague-Dawley Rat Physiology
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Nitric Oxide in Health and Disease of the Respiratory System
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Antioxidant properties of N-acetylcysteine: their relevance in relation to chronic obstructive pulmonary disease
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Role for Cystic Fibrosis Transmembrane Conductance Regulator Protein in a Glutathione Response to Bronchopulmonary Pseudomonas Infection
Infect. Immun., April 1, 2004; 72(4): 2045 - 2051. [Abstract] [Full Text] [PDF] M. Griese, J. Ramakers, A. Krasselt, V. Starosta, S. van Koningsbruggen, R. Fischer, F. Ratjen, B. Mullinger, R. M. Huber, K. Maier, et al.
Improvement of Alveolar Glutathione and Lung Function but Not Oxidative State in Cystic Fibrosis
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Hypochlorous acid alters bronchial epithelial cell membrane properties and prevention by extracellular glutathione
J Appl Physiol, December 1, 2003; 95(6): 2444 - 2452. [Abstract] [Full Text] J. D. Crapo
Redox Active Agents in Inflammatory Lung Injury
Am. J. Respir. Crit. Care Med., November 1, 2003; 168(9): 1027 - 1028. [Full Text] J. A. Wickenden, M. C. H. Clarke, A. G. Rossi, I. Rahman, S. P. Faux, K. Donaldson, and W. MacNee
Cigarette Smoke Prevents Apoptosis through Inhibition of Caspase Activation and Induces Necrosis
Am. J. Respir. Cell Mol. Biol., November 1, 2003; 29(5): 562 - 570. [Abstract] [Full Text] N. R. Hackett, A. Heguy, B.-G. Harvey, T. P. O'Connor, K. Luettich, D. B. Flieder, R. Kaplan, and R. G. Crystal
Variability of Antioxidant-Related Gene Expression in the Airway Epithelium of Cigarette Smokers
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Glutamate-cysteine ligase modulatory subunit in BAL alveolar macrophages of healthy smokers
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Superoxide Dismutases in the Lung and Human Lung Diseases
Am. J. Respir. Crit. Care Med., June 15, 2003; 167(12): 1600 - 1619. [Abstract] [Full Text] [PDF] C. E. Healy, L. D. Kier, F. Broeckaert, and M. A. Martens
A Review of the Genotoxicity of Triallate
International Journal of Toxicology, May 1, 2003; 22(3): 233 - 251. [Abstract] [PDF] F.J. Kelly, C. Dunster, and I. Mudway
Air pollution and the elderly: oxidant/antioxidant issues worth consideration
Eur. Respir. J., May 1, 2003; 21(40_suppl): 70S - 75s. [Abstract] [Full Text] [PDF] S.-J. Yong, Z. Vuk-Pavlovic, J. E. Standing, E. C. Crouch, and A. H. Limper
Surfactant Protein D-Mediated Aggregation of Pneumocystis carinii Impairs Phagocytosis by Alveolar Macrophages
Infect. Immun., April 1, 2003; 71(4): 1662 - 1671. [Abstract] [Full Text] [PDF] T. H. Stenson, A. K. Patton, and A. A. Weiss
Reduced Glutathione Is Required for Pertussis Toxin Secretion by Bordetella pertussis
Infect. Immun., March 1, 2003; 71(3): 1316 - 1320. [Abstract] [Full Text] [PDF] H Kanazawa, S Shiraishi, K Hirata, and J Yoshikawa
Imbalance between levels of nitrogen oxides and peroxynitrite inhibitory activity in chronic obstructive pulmonary disease
Thorax, February 1, 2003; 58(2): 106 - 109. [Abstract] [Full Text] [PDF] S. El-Chemaly, M. Salathe, S. Baier, G. E. Conner, and R. Forteza
Hydrogen Peroxide-Scavenging Properties of Normal Human Airway Secretions
Am. J. Respir. Crit. Care Med., February 1, 2003; 167(3): 425 - 430. [Abstract] [Full Text] [PDF] E. M. Leslie, R. G. Deeley, and S. P. C. Cole
Bioflavonoid Stimulation of Glutathione Transport by the 190-kDa Multidrug Resistance Protein 1 (MRP1)
Drug Metab. Dispos., January 1, 2003; 31(1): 11 - 15. [Abstract] [Full Text] [PDF] K. J Lenton, A. T Sane, H. Therriault, A. M Cantin, H. Payette, and J R. Wagner
Vitamin C augments lymphocyte glutathione in subjects with ascorbate deficiency
Am J Clin Nutr, January 1, 2003; 77(1): 189 - 195. [Abstract] [Full Text] [PDF] I. Y. Haddad
Idiopathic Pneumonia after Marrow Transplantation: When Are Antioxidants Effective?
Am. J. Respir. Crit. Care Med., December 15, 2002; 166(12): 1532 - 1534. [Full Text] [PDF] K. S. Bhalla and R. J. Folz
Idiopathic Pneumonia Syndrome after Syngeneic Bone Marrow Transplant in Mice
Am. J. Respir. Crit. Care Med., December 15, 2002; 166(12): 1579 - 1589. [Abstract] [Full Text] [PDF] I L C Chapple, G Brock, C Eftimiadi, and J B Matthews
Glutathione in gingival crevicular fluid and its relation to local antioxidant capacity in periodontal health and disease
Mol. Pathol., December 1, 2002; 55(6): 367 - 373. [Abstract] [Full Text] [PDF] W. R. Henderson Jr., E. Y. Chi, J.-L. Teo, C. Nguyen, and M. Kahn
A Small Molecule Inhibitor of Redox-Regulated NF-{kappa}B and Activator Protein-1 Transcription Blocks Allergic Airway Inflammation in a Mouse Asthma Model
J. Immunol., November 1, 2002; 169(9): 5294 - 5299. [Abstract] [Full Text] [PDF] J. C. Jean, Y. Liu, L. A. Brown, R. E. Marc, E. Klings, and M. Joyce-Brady
gamma -Glutamyl transferase deficiency results in lung oxidant stress in normoxia
Am J Physiol Lung Cell Mol Physiol, October 1, 2002; 283(4): L766 - L776. [Abstract] [Full Text] [PDF] P. S. Hiemstra
The Adaptive Response of Smokers to Oxidative Stress: Moving from Culture to Tissue
Am. J. Respir. Crit. Care Med., September 1, 2002; 166(5): 635 - 636. [Full Text] [PDF] T. Harju, R. Kaarteenaho-Wiik, Y. Soini, R. Sormunen, and V. L. Kinnula
Diminished Immunoreactivity of {gamma}-Glutamylcysteine Synthetase in the Airways of Smokers' Lung
Am. J. Respir. Crit. Care Med., September 1, 2002; 166(5): 754 - 759. [Abstract] [Full Text] [PDF] S. A. A. Comhair and S. C. Erzurum
Antioxidant responses to oxidant-mediated lung diseases
Am J Physiol Lung Cell Mol Physiol, August 1, 2002; 283(2): L246 - L255. [Abstract] [Full Text] [PDF] A. M. Abushamaa, T. A. Sporn, and R. J. Folz
Oxidative stress and inflammation contribute to lung toxicity after a common breast cancer chemotherapy regimen
Am J Physiol Lung Cell Mol Physiol, August 1, 2002; 283(2): L336 - L345. [Abstract] [Full Text] [PDF] J. Kloek, I. van Ark, N. Bloksma, F. De Clerck, F. P. Nijkamp, and G. Folkerts
Glutathione and other low-molecular-weight thiols relax guinea pig trachea ex vivo: interactions with nitric oxide?
Am J Physiol Lung Cell Mol Physiol, August 1, 2002; 283(2): L403 - L408. [Abstract] [Full Text] [PDF] H. J. Kim, X. Liu, H. Wang, T. Kohyama, T. Kobayashi, F.-Q. Wen, D. J. Romberger, S. Abe, W. MacNee, I. Rahman, et al.
Glutathione prevents inhibition of fibroblast-mediated collagen gel contraction by cigarette smoke
Am J Physiol Lung Cell Mol Physiol, August 1, 2002; 283(2): L409 - L417. [Abstract] [Full Text] [PDF] S. W. Griffiths, J. King, and C. L. Cooney
The Reactivity and Oxidation Pathway of Cysteine 232 in Recombinant Human alpha 1-Antitrypsin
J. Biol. Chem., July 5, 2002; 277(28): 25486 - 25492. [Abstract] [Full Text] [PDF] H. Jardine, W. MacNee, K. Donaldson, and I. Rahman
Molecular Mechanism of Transforming Growth Factor (TGF)-beta 1-induced Glutathione Depletion in Alveolar Epithelial Cells. INVOLVEMENT OF AP-1/ARE AND Fra-1
J. Biol. Chem., June 7, 2002; 277(24): 21158 - 21166. [Abstract] [Full Text] [PDF] B. Gaston and J. F. Hunt
How Acidopneic Is My Patient? A New Question in the Pulmonary Laboratory
Am. J. Respir. Crit. Care Med., May 15, 2002; 165(10): 1349 - 1350. [Full Text] [PDF] S. Hammerschmidt, N. Buchler, and H. Wahn
Tissue Lipid Peroxidation and Reduced Glutathione Depletion in Hypochlorite-Induced Lung Injury
Chest, February 1, 2002; 121(2): 573 - 581. [Abstract] [Full Text] [PDF] V L Kinnula, S Lehtonen, R Kaarteenaho-Wiik, E Lakari, P Paakko, S W Kang, S G Rhee, and Y Soini
Cell specific expression of peroxiredoxins in human lung and pulmonary sarcoidosis
Thorax, February 1, 2002; 57(2): 157 - 164. [Abstract] [Full Text] [PDF] G. Sun, K. Crissman, J. Norwood, J. Richards, R. Slade, and G. E. Hatch
Oxidative interactions of synthetic lung epithelial lining fluid with metal-containing particulate matter
Am J Physiol Lung Cell Mol Physiol, October 1, 2001; 281(4): L807 - L815. [Abstract] [Full Text] [PDF] S. Yang, V. A. Porter, D. N. Cornfield, C. Milla, A. Panoskaltsis-Mortari, B. R. Blazar, and I. Y. Haddad
Effects of oxidant stress on inflammation and survival of iNOS knockout mice after marrow transplantation
Am J Physiol Lung Cell Mol Physiol, October 1, 2001; 281(4): L922 - L930. [Abstract] [Full Text] [PDF] J. H. Roum, A. S. Aledia, L. A. Carungcong, K.-J. Kim, and Z. Borok
Extracellular glutathione inhibits oxygen-induced permeability changes in alveolar epithelial monolayers
J Appl Physiol, August 1, 2001; 91(2): 748 - 754. [Abstract] [Full Text] [PDF] E. Cavarra, M. Lucattelli, F. Gambelli, B. Bartalesi, S. Fineschi, A. Szarka, F. Giannerini, P. A. Martorana, and G. Lungarella
Human SLPI inactivation after cigarette smoke exposure in a new in vivo model of pulmonary oxidative stress
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Synthetic chloride channel restores glutathione secretion in cystic fibrosis airway epithelia
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Antioxidant imbalance in the lungs of cystic fibrosis transmembrane conductance regulator protein mutant mice
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Interstitial lung disease induced by exogenous agents: factors governing susceptibility
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Glutathione in induced sputum of healthy individuals and patients with asthma
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Selectivity properties of a Na-dependent amino acid cotransport system in adult alveolar epithelial cells
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Effect of Cigarette Smoke on the Permeability and IL-1beta and sICAM-1 Release from Cultured Human Bronchial Epithelial Cells of Never-Smokers, Smokers, and Patients with Chronic Obstructive Pulmonary Disease
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Ozone, But Not Nitrogen Dioxide, Exposure Decreases Glutathione Peroxidases in Epithelial Lining Fluid of Human Lung
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Albumin-mediated Regulation of Cellular Glutathione and Nuclear Factor Kappa B Activation
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S-nitrosoglutathione breakdown prevents airway smooth muscle relaxation in the guinea pig
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Less than additive interaction between cigarette smoke and chromium(VI) in inducing clastogenic damage in rodents
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Pulmonary Glutathione Levels in Acute Episodes of Farmer's Lung
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Oxidants/Antioxidants and COPD
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Threshold mechanisms and site specificity in chromium(VI) carcinogenesis
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Frequent paracetamol use and asthma in adults
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Treatment of Obstructive Airway Disease With a Cysteine Donor Protein Supplement: A Case Report
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The Effects of Chronic Alcohol Abuse on Pulmonary Glutathione Homeostasis
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The structure of ATP synthase, the universal protein that manufactures ATP; Photo courtesy of Professor George Oster; Department of Molecular and Cell Biology, University of California, Berkeley [2000](IR92)

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(Memo Item created on November 3, 2010 08:54 PM)
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The structure of ATP synthase, the universal protein that manufactures ATP; Photo courtesy of Professor George Oster; Department of Molecular and Cell Biology, University of California, Berkeley [2000](IR92)

http://mcb.berkeley.edu/gallery2/main.php?g2_itemId=99
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The structure of ATP synthase, the universal protein that manufactures ATP; Photo courtesy of Professor George Oster; Department of Molecular and Cell Biology, University of California, Berkeley [2000](IR92)

The structure of ATP synthase, the universal protein that manufactures ATP.

The structure of ATP synthase consists of two rotary motors, labeled F1 and Fo, that are connected by a flexible shaft. Under normal operation, the Fo motor uses the energy stored in a transmembrane ion gradient to drive the F1 motor in reverse so that ATP is synthesized from ADP and phosphate. In bacteria, anerobic conditions wipe out the ion gradient whereupon the F1 part becomes a motor, using the energy of ATP hydrolysis to turn the Fo part in reverse so that it functions as an ion pump.

Oster, G., and Wang, H. (2000). Reverse engineering a protein: The mechanochemistry of ATP synthase. Biochimica et Biophysica Acta 1458, 482-510.
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Microtubule-driven self-assembly (自我組裝的) of the Dam1 kinetochore ring. [2010-11-03](IR92)

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(Memo Item created on November 3, 2010 08:59 PM)
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Microtubule-driven self-assembly of the Dam1 kinetochore ring.
Microtubule-driven self-assembly (自我組裝的) of the Dam1 kinetochore ring. [2010-11-03](IR92)

http://mcb.berkeley.edu/gallery2/main.php?g2_itemId=172
Department of Molecular and Cell Biology, University of California, Berkeley
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Microtubule-driven self-assembly of the Dam1 kinetochore ring.

The yeast kinetochore complex Dam1 self-assembles around microtubules forming rings that can diffuse on the microtubule lattice and harvest the energy of microtubule disassembly to move processively towards the poles during anaphase.

(These studies are being carried out as a collaboration of three MCB faculty members: Georjana Barnes, David Drubin and Eva Nogales)

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