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Article: Cell-cell adhesion in lung endothelium.

Shasby, D Michael

American journal of physiology. Lung cellular and molecular physiology

2006 Volume 292, Issue 3, Page(s) L593–607

Abstract: Homotypic cell-cell adhesion is essential for tissue and organ development, remodeling, regeneration, and physiological function. Whereas a significant number of homotypic cell-cell adhesion molecules have been identified, much more is known about those ... ...

Abstract	Homotypic cell-cell adhesion is essential for tissue and organ development, remodeling, regeneration, and physiological function. Whereas a significant number of homotypic cell-cell adhesion molecules have been identified, much more is known about those concentrated in epithelia than in endothelia. Among the endothelial cell-cell adhesion molecules, very little is known that is specific to endothelium in the pulmonary and bronchial circulations. This review focuses primarily on homotypic cell-cell adhesion molecules that are or are likely to be important in lung endothelium.
MeSH term(s)	Animals ; Cell Adhesion/physiology ; Cell Adhesion Molecules/metabolism ; Endothelium, Vascular/cytology ; Endothelium, Vascular/physiology ; Humans ; Lung/cytology ; Lung Diseases/pathology
Chemical Substances	Cell Adhesion Molecules
Language	English
Publishing date	2006-11-03
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1013184-x
ISSN	1522-1504 ; 1040-0605
ISSN (online)	1522-1504
ISSN	1040-0605
DOI	10.1152/ajplung.00386.2006
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Article: H1 and PAR2 receptors enhance delivery of immune-competent cells and molecules by interrupting E-cadherin adhesion in epithelia.

Shasby, D Michael / Winter, Michael C

Transactions of the American Clinical and Climatological Association

2011 Volume 122, Page(s) 217–228

Abstract: The lung's epithelial surface is at the same time vitally exchanging gas with the environment and acting as a barrier that protects the organism from the environment. We hypothesized that activation of epithelial-cell G-protein-coupled receptors for ... ...

Abstract	The lung's epithelial surface is at the same time vitally exchanging gas with the environment and acting as a barrier that protects the organism from the environment. We hypothesized that activation of epithelial-cell G-protein-coupled receptors for immune-defense molecules would temporarily interrupt cadherin-dependent cell-cell adhesion of epithelial cells and thereby focally and temporarily compromise the epithelial barrier to facilitate delivery of other immune molecules and cells to challenged sites. Activation of type 1 histamine or type 2 PAR receptors on the basolateral surface of primary airway epithelial cells or L-cells expressing E-cadherin interrupted cadherin adhesion and caused approximately a 50% decrease in the epithelial barrier for 2-3 minutes. Given basic biochemical observations of others, we further hypothesized that activation of the receptors altered the barrier by phosphorylating tyrosines on an essential cadherin-complex component, beta-catenin. Y-F mutations in beta-catenin completely blocked the effects of activating the same receptors on cadherin-dependent adhesion and on the epithelial barrier. Hence, G-protein-coupled receptors responding to immune-defense molecules temporarily and focally interrupt the lung epithelial barrier by compromising cadherin-based adhesion.
MeSH term(s)	Animals ; Antigens, CD ; Cadherins/metabolism ; Cell Adhesion ; Cell Line ; Dogs ; Electric Impedance ; Epithelial Cells/drug effects ; Epithelial Cells/immunology ; Epithelial Cells/metabolism ; Humans ; Immunity, Mucosal/drug effects ; Kidney/immunology ; Kidney/metabolism ; Mutation ; Oligopeptides/pharmacology ; Permeability ; Phosphorylation ; Receptor, PAR-2/agonists ; Receptor, PAR-2/metabolism ; Receptors, Histamine H1/metabolism ; Respiratory Mucosa/drug effects ; Respiratory Mucosa/immunology ; Respiratory Mucosa/metabolism ; Signal Transduction ; Time Factors ; Transfection ; Tyrosine ; beta Catenin/genetics ; beta Catenin/metabolism
Chemical Substances	Antigens, CD ; CDH1 protein, human ; CTNNB1 protein, human ; Cadherins ; Oligopeptides ; Receptor, PAR-2 ; Receptors, Histamine H1 ; beta Catenin ; seryl-leucyl-isoleucyl-glycyl-arginyl-leucine ; Tyrosine (42HK56048U)
Language	English
Publishing date	2011-05-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	603823-2
ISSN	0065-7778
ISSN	0065-7778
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Article: System N in eNdothelium.

Shasby, D Michael

American journal of physiology. Lung cellular and molecular physiology

2002 Volume 282, Issue 6, Page(s) L1190–1

MeSH term(s)	Amino Acid Transport Systems/metabolism ; Amino Acid Transport Systems, Neutral/metabolism ; Animals ; Endothelium, Vascular/metabolism ; Histidine/metabolism ; Lung/blood supply ; Lung/metabolism ; Rats
Chemical Substances	Amino Acid Transport Systems ; Amino Acid Transport Systems, Neutral ; Histidine (4QD397987E)
Language	English
Publishing date	2002-03-19
Publishing country	United States
Document type	Comment ; Editorial
ZDB-ID	1013184-x
ISSN	1522-1504 ; 1040-0605
ISSN (online)	1522-1504
ISSN	1040-0605
DOI	10.1152/ajplung.00046.2002
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Article: Compromised E-cadherin adhesion and epithelial barrier function with activation of G protein-coupled receptors is rescued by Y-to-F mutations in beta-catenin.

Winter, Michael C / Shasby, Sandra / Shasby, D Michael

American journal of physiology. Lung cellular and molecular physiology

2007 Volume 294, Issue 3, Page(s) L442–8

Abstract: Activation of the type 1 histamine (H1) or the type 2 protease-activated (PAR-2) G protein-coupled receptors interrupts E-cadherin adhesion and decreases the transepithelial resistance (TER) of epithelium. Several reports suggest that cadherin adhesive ... ...

Abstract	Activation of the type 1 histamine (H1) or the type 2 protease-activated (PAR-2) G protein-coupled receptors interrupts E-cadherin adhesion and decreases the transepithelial resistance (TER) of epithelium. Several reports suggest that cadherin adhesive function depends on the association of cadherin with beta-catenin and that this association is regulated by phosphorylation of tyrosines in beta-catenin. We tested the hypothesis that loss of cadherin adhesion and compromise of TER on activation of the H1 or PAR-2 receptor is due to phosphorylation of tyrosines in beta-catenin. L cells were stably transfected to express E-cadherin (L-E-cad cells) and H1 (L-H1-E-cad cells). L cells and Madin-Darby canine kidney (MDCK) cells constitutively express PAR-2. Stably transfected L-E-cad, L-H1-E-cad, and MDCK cells were also stably transfected with FLAG-tagged wild-type (WT) or mutant beta-catenin, converting tyrosine 142, 489, or 654 to the nonphosphorylatable mimetic, phenylalanine (WT, Y142F, Y489F, or Y654F). Activation of H1 or PAR-2 interrupted adhesion to an immobilized E-cadherin-Fc fusion protein of L-H1-E-cad, L-E-cad, and MDCK cells expressing WT or Y142F beta-catenin but did not interrupt adhesion of L-H1-E-cad, L-E-cad, and MDCK cells expressing the Y489F or Y654F mutant beta-catenins. PAR-2 activation decreased the TER of monolayers of MDCK cells expressing WT or Y142F beta-catenin 40-45%. However, PAR-2 activation did not decrease the TER of monolayers of MDCK cells expressing Y489F or Y654F beta-catenin. The protein tyrosine phosphatase PTP1B binds to the cadherin cytoplasmic domain and dephosphorylates beta-catenin. Inhibition of PTP1B interrupted adhesion to E-cadherin-Fc of MDCK cells expressing WT beta-catenin but did not affect the adhesion of MDCK cells expressing Y489F or Y654F beta-catenin. Similarly, inhibition of PTP1B compromised the TER of MDCK cells expressing WT beta-catenin but did not affect the TER of MDCK cells expressing Y489F or Y654F beta-catenin. We conclude that phosphorylation of tyrosines 489 and 654 in beta-catenin is a necessary step in the process by which G protein-coupled H1 and PAR-2 receptors interrupt E-cadherin adhesion. We also conclude that activation of PAR-2 has no effect on the TER without first interrupting E-cadherin adhesion.
MeSH term(s)	Amino Acid Substitution ; Animals ; Cadherins/physiology ; Cell Adhesion/drug effects ; Cell Adhesion/physiology ; Dogs ; Electric Impedance ; Epithelial Cells/drug effects ; Epithelial Cells/physiology ; Histamine/pharmacology ; Humans ; L Cells ; Mice ; Mutation ; Oligopeptides/pharmacology ; Phenylalanine/physiology ; Protein Tyrosine Phosphatase, Non-Receptor Type 1/metabolism ; Receptor, PAR-2/agonists ; Receptor, PAR-2/physiology ; Receptors, Histamine H1/physiology ; Transfection ; Tyrosine/genetics ; Tyrosine/physiology ; beta Catenin/genetics
Chemical Substances	Cadherins ; Oligopeptides ; Receptor, PAR-2 ; Receptors, Histamine H1 ; beta Catenin ; Tyrosine (42HK56048U) ; Phenylalanine (47E5O17Y3R) ; Histamine (820484N8I3) ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 (EC 3.1.3.48)
Language	English
Publishing date	2007-12-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1013184-x
ISSN	1522-1504 ; 1040-0605
ISSN (online)	1522-1504
ISSN	1040-0605
DOI	10.1152/ajplung.00404.2007
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Article: PAR2 activation interrupts E-cadherin adhesion and compromises the airway epithelial barrier: protective effect of beta-agonists.

Winter, Michael C / Shasby, Sandra S / Ries, Dana R / Shasby, D Michael

American journal of physiology. Lung cellular and molecular physiology

2006 Volume 291, Issue 4, Page(s) L628–35

Abstract: The airway epithelium is an important barrier between the environment and subepithelial tissues. The epithelium is also divided into functionally restricted apical and basolateral domains, and this restriction is dependent on the elements of the barrier. ...

Abstract	The airway epithelium is an important barrier between the environment and subepithelial tissues. The epithelium is also divided into functionally restricted apical and basolateral domains, and this restriction is dependent on the elements of the barrier. The protease-activated receptor-2 (PAR2) receptor is expressed in airway epithelium, and its activation initiates multiple effects including enhanced airway inflammation and reactivity. We hypothesized that activation of PAR2 would interrupt E-cadherin adhesion and compromise the airway epithelial barrier. The PAR2-activating peptide (PAR2-AP, SLIGRL) caused an immediate approximately 50% decrease in the transepithelial resistance of primary human airway epithelium that persisted for 6-10 min. The decrease in resistance was accompanied by an increase in mannitol flux across the epithelium and occurred in cystic fibrosis transmembrane conductance receptor (CFTR) epithelium pretreated with amiloride to block Na and Cl conductances, confirming that the decrease in resistance represented an increase in paracellular conductance. In parallel experiments, activation of PAR2 interrupted the adhesion of E-cadherin-expressing L cells and of primary airway epithelial cells to an immobilized E-cadherin extracellular domain, confirming the hypothesis that activation of PAR2 interrupts E-cadherin adhesion. Selective interruption of E-cadherin adhesion with antibody to E-cadherin decreased the transepithelial resistance of primary airway epithelium by >80%. Pretreatment of airway epithelium or the E-cadherin-expressing L cells with the long-acting beta-agonist salmeterol prevented PAR2 activation from interrupting E-cadherin adhesion and compromising the airway epithelial barrier. Activation of PAR2 interrupts E-cadherin adhesion and compromises the airway epithelial barrier.
MeSH term(s)	Adrenergic beta-Agonists/pharmacology ; Albuterol/analogs & derivatives ; Albuterol/pharmacology ; Bronchi/drug effects ; Bronchi/metabolism ; Bronchi/physiology ; Cadherins/metabolism ; Cell Adhesion/drug effects ; Cell Adhesion/physiology ; Cells, Cultured ; Cyclic AMP/analogs & derivatives ; Cyclic AMP/pharmacology ; Electric Impedance ; Epithelial Cells/drug effects ; Epithelial Cells/metabolism ; Epithelial Cells/physiology ; Humans ; In Vitro Techniques ; Permeability/drug effects ; Receptor, PAR-2/metabolism ; Receptor, PAR-2/physiology ; Receptors, Histamine H1/metabolism ; Receptors, Histamine H1/physiology ; Salmeterol Xinafoate ; Thionucleotides/pharmacology
Chemical Substances	Adrenergic beta-Agonists ; Cadherins ; Receptor, PAR-2 ; Receptors, Histamine H1 ; Thionucleotides ; 8-((4-chlorophenyl)thio)cyclic-3',5'-AMP (41941-66-6) ; Salmeterol Xinafoate (6EW8Q962A5) ; Cyclic AMP (E0399OZS9N) ; Albuterol (QF8SVZ843E)
Language	English
Publishing date	2006-05-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1013184-x
ISSN	1522-1504 ; 1040-0605
ISSN (online)	1522-1504
ISSN	1040-0605
DOI	10.1152/ajplung.00046.2006
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Article: Histamine selectively interrupts VE-cadherin adhesion independently of capacitive calcium entry.

Winter, Michael C / Shasby, Sandra S / Ries, Dana R / Shasby, D Michael

American journal of physiology. Lung cellular and molecular physiology

2004 Volume 287, Issue 4, Page(s) L816–23

Abstract: Histamine is an important agent of innate immunity, transiently increasing the flux of immune-competent molecules from the vascular space to the tissues and then allowing rapid restoration of the integrity of the endothelial barrier. In previous work we ... ...

Abstract	Histamine is an important agent of innate immunity, transiently increasing the flux of immune-competent molecules from the vascular space to the tissues and then allowing rapid restoration of the integrity of the endothelial barrier. In previous work we found that histamine alters the endothelial barrier by disrupting cell-cell adhesion and identified VE-cadherin as an essential participant in this process. The previous work did not determine whether histamine directly interrupted VE-cadherin adhesion, whether the effects of histamine were selective for cadherin adhesion, or whether capacitive calcium flux across the cell membrane was necessary for the effects of histamine on cell-cell adhesion. In the current work we found that histamine directly interrupts adhesion of L cells expressing the type 1 histamine (H1) receptor and VE-cadherin to a VE-cadherin-Fc fusion protein. In contrast, integrin-mediated adhesion to fibronectin of the same L cells expressing the H1 receptor was not affected by histamine, demonstrating that the effects of histamine are selective for cadherin adhesion. Some of the effects of many edemagenic agonists on endothelium are dependent on the capacitive flux of calcium across the endothelial cell membrane. Blocking capacitive calcium flux with LaCl3 did not prevent histamine from interrupting VE-cadherin adhesion of transfected L cells, nor did it prevent histamine from interrupting cell-cell adhesion of human umbilical vein endothelial cells. These data support the contentions that histamine directly and selectively interrupts cadherin adhesion and this effect on cadherin adhesion is independent of capacitive calcium flux.
MeSH term(s)	Animals ; Antigens, CD ; Base Sequence ; Cadherins/genetics ; Cadherins/physiology ; Calcium/physiology ; Cell Adhesion/drug effects ; Cell Adhesion/physiology ; Cells, Cultured ; DNA Primers ; Endothelium, Vascular/drug effects ; Endothelium, Vascular/physiology ; Gene Expression Regulation/drug effects ; Histamine/pharmacology ; Humans ; Kinetics ; L Cells ; Mice ; Recombinant Proteins/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Transfection ; Umbilical Veins
Chemical Substances	Antigens, CD ; Cadherins ; DNA Primers ; Recombinant Proteins ; cadherin 5 ; Histamine (820484N8I3) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2004-06-25
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1013184-x
ISSN	1522-1504 ; 1040-0605
ISSN (online)	1522-1504
ISSN	1040-0605
DOI	10.1152/ajplung.00056.2004
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Article: Histamine stimulates phosphorylation of adherens junction proteins and alters their link to vimentin.

Shasby, D Michael / Ries, Dana R / Shasby, Sandra S / Winter, Michael C

American journal of physiology. Lung cellular and molecular physiology

2002 Volume 282, Issue 6, Page(s) L1330–8

Abstract: Histamine increases microvascular permeability by creating small transitory (100-400 nm) gaps between adjacent endothelial cells at sites of vascular endothelial (VE)-cadherin-based adhesion. We examined the effects of histamine on the proteins within ... ...

Abstract	Histamine increases microvascular permeability by creating small transitory (100-400 nm) gaps between adjacent endothelial cells at sites of vascular endothelial (VE)-cadherin-based adhesion. We examined the effects of histamine on the proteins within the VE-cadherin-based adherens junction in primary human umbilical vein endothelial cells. VE-cadherin is linked not only by beta- and alpha-catenin to cortical actin but also by gamma-catenin to the intermediate filament vimentin. In mature human umbilical vein cultures, the VE-cadherin immunoprecipitate contained equivalent amounts of alpha- and beta-catenin, 130% as much beta- as gamma-catenin, and 50% as much actin as vimentin. Within 60 s, histamine decreased the fraction of VE-cadherin in the insoluble portion of the cell lysate by 35 +/- 1.5%. At the same time, histamine decreased the amount of vimentin that immunoprecipitated with VE-cadherin by 50 +/- 6%. Histamine did not affect the amount of actin or the amount of alpha-, beta-, or gamma-catenin that immunoprecipitated with VE-cadherin. Within 60 s, histamine simulated a doubling in the phosphorylation of VE-cadherin and beta- and gamma-catenin. The VE-cadherin immunoprecipitate contained kinase activity that phosphorylated VE-cadherin and gamma-catenin in vitro.
MeSH term(s)	Actins/metabolism ; Adherens Junctions/drug effects ; Adherens Junctions/metabolism ; Antigens, CD ; Cadherins/metabolism ; Cells, Cultured ; Cytoskeletal Proteins/metabolism ; Cytoskeleton/drug effects ; Cytoskeleton/metabolism ; Desmoplakins ; Endothelium, Vascular/cytology ; Endothelium, Vascular/drug effects ; Endothelium, Vascular/metabolism ; Histamine/pharmacology ; Humans ; Membrane Proteins/metabolism ; Phosphorylation/drug effects ; Precipitin Tests ; Trans-Activators ; Vimentin/metabolism ; alpha Catenin ; beta Catenin ; gamma Catenin
Chemical Substances	Actins ; Antigens, CD ; CTNNA1 protein, human ; CTNNB1 protein, human ; Cadherins ; Cytoskeletal Proteins ; Desmoplakins ; JUP protein, human ; Membrane Proteins ; Trans-Activators ; Vimentin ; alpha Catenin ; beta Catenin ; cadherin 5 ; gamma Catenin ; Histamine (820484N8I3)
Language	English
Publishing date	2002-03-19
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1013184-x
ISSN	1522-1504 ; 1040-0605
ISSN (online)	1522-1504
ISSN	1040-0605
DOI	10.1152/ajplung.00329.2001
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Article: Sepsis and innate immunity.

Shasby, D Michael / McCray, Paul

American journal of respiratory and critical care medicine

2004 Volume 169, Issue 2, Page(s) 144–145

MeSH term(s)	Animals ; Anti-Bacterial Agents/therapeutic use ; Blood Proteins/metabolism ; Blood Proteins/therapeutic use ; Cathelicidins ; Immunity, Innate ; Intestines/immunology ; Rats ; Sheep ; Shock, Septic/etiology ; Shock, Septic/immunology ; Shock, Septic/metabolism ; Shock, Septic/mortality
Chemical Substances	Anti-Bacterial Agents ; Blood Proteins ; Cathelicidins ; SMAP29 protein, Ovis aries
Language	English
Publishing date	2004-01-15
Publishing country	United States
Document type	Comment ; Editorial
ZDB-ID	1180953-x
ISSN	1535-4970 ; 1073-449X ; 0003-0805
ISSN (online)	1535-4970
ISSN	1073-449X ; 0003-0805
DOI	10.1164/rccm.2311003
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Article: Histamine decreases E-cadherin-based adhesion to increase permeability of human airway epithelium.

Zabner, Joseph / Winter, Michael C / Shasby, Sandra / Ries, Dana / Shasby, D Michael

Chest

2002 Volume 123, Issue 3 Suppl, Page(s) 385S

MeSH term(s)	Animals ; Asthma/chemically induced ; Cadherins/adverse effects ; Cadherins/pharmacology ; Cell Membrane Permeability/drug effects ; Disease Models, Animal ; Guinea Pigs ; Histamine/adverse effects ; Histamine/pharmacology ; Humans ; In Vitro Techniques ; Respiratory Mucosa/drug effects ; Tissue Adhesions/chemically induced
Chemical Substances	Cadherins ; Histamine (820484N8I3)
Language	English
Publishing date	2002-10-21
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1032552-9
ISSN	1931-3543 ; 0012-3692
ISSN (online)	1931-3543
ISSN	0012-3692
DOI	10.1378/chest.123.3_suppl.385s
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Article: Histamine alters E-cadherin cell adhesion to increase human airway epithelial permeability.

Zabner, Joseph / Winter, Michael / Excoffon, Katherine J D Ashbourne / Stoltz, David / Ries, Dana / Shasby, Sandra / Shasby, Michael

Journal of applied physiology (Bethesda, Md. : 1985)

2003 Volume 95, Issue 1, Page(s) 394–401

Abstract: During the immediate response to an inhaled allergen, there is an increase in the paracellular permeability of the airway epithelium.1 Histamine is an important agonist released during the immediate response to inhaled allergen. We hypothesized that ... ...

Abstract	During the immediate response to an inhaled allergen, there is an increase in the paracellular permeability of the airway epithelium.1 Histamine is an important agonist released during the immediate response to inhaled allergen. We hypothesized that histamine would increase human airway epithelial paracellular permeability and that it would do this by interrupting E-cadherin-based cell adhesion. Histamine, applied to the basolateral surface, increased the paracellular permeability of cultured human airway epithelia, and this effect of histamine was blocked by the histamine receptor antagonist promethazine. ECV304 cells express a histamine receptor, N-cadherin, and elements of the tight junction, including claudins, but they do not express E-cadherin. Histamine increased the paracellular permeability of ECV304 cells transfected with a vector and expressing E-cadherin but not ECV304 cells expressing lac-Z in the same vector. L cells do not express the histamine receptor, cadherins, or claudins. Histamine decreased adhesion of L cells expressing the human histamine receptor and E-cadherin to an E-cadherin-Fc fusion protein. Histamine did not alter the adhesion to the E-cadherin fusion protein of L cells expressing either the histamine receptor or E-cadherin alone. When applied to the apical surface, adenovirus poorly infects airway epithelial cells because its receptor, CAR, is restricted to the basolateral surface of the cells. When histamine was applied to the basolateral surface of airway epithelial cells, infection of the cells by adenovirus increased by approximately one log. This effect of histamine was also blocked by promethazine. Histamine increases airway paracellular permeability and increases susceptibility of airway epithelial cells to infection by adenovirus by interrupting E-cadherin adhesion.
MeSH term(s)	Adenoviridae/genetics ; Animals ; Cadherins/biosynthesis ; Cadherins/genetics ; Cadherins/physiology ; Cell Adhesion/drug effects ; Cell Differentiation/drug effects ; Cell Line ; Cell Membrane Permeability/drug effects ; DNA, Complementary/biosynthesis ; Dexamethasone/pharmacology ; Epithelial Cells/drug effects ; Green Fluorescent Proteins ; Histamine/pharmacology ; Humans ; In Vitro Techniques ; L Cells (Cell Line) ; Luminescent Proteins/genetics ; Mice ; Plasmids/genetics ; Protein Biosynthesis ; RNA, Messenger/biosynthesis ; RNA, Messenger/genetics ; Receptors, Histamine/genetics ; Receptors, Histamine/metabolism ; Receptors, Virus/genetics ; Respiratory System/cytology ; Respiratory System/drug effects ; Transfection ; beta-Galactosidase/metabolism
Chemical Substances	Cadherins ; DNA, Complementary ; Luminescent Proteins ; RNA, Messenger ; Receptors, Histamine ; Receptors, Virus ; Green Fluorescent Proteins (147336-22-9) ; Dexamethasone (7S5I7G3JQL) ; Histamine (820484N8I3) ; beta-Galactosidase (EC 3.2.1.23)
Language	English
Publishing date	2003-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	219139-8
ISSN	1522-1601 ; 8750-7587 ; 0021-8987 ; 0161-7567
ISSN (online)	1522-1601
ISSN	8750-7587 ; 0021-8987 ; 0161-7567
DOI	10.1152/japplphysiol.01134.2002
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