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Article: Making Connections: Desmoplakin as an Intermediate Filament-Binding Protein.

Kowalczyk, Andrew P / Kottke, Margaret D

The Journal of investigative dermatology

2007 Volume 127 Suppl 3, Page(s) E8–9

Language	English
Publishing date	2007-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	80136-7
ISSN	1523-1747 ; 0022-202X
ISSN (online)	1523-1747
ISSN	0022-202X
DOI	10.1038/sj.skinbio.6250008
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Article: Making connections: desmoplakin as an intermediate filament-binding protein.

Kowalczyk, Andrew P / Kottke, Margaret D

The Journal of investigative dermatology

2007 Volume 127, Issue E1, Page(s) E8–9

MeSH term(s)	Cytoskeletal Proteins/metabolism ; Desmoplakins/metabolism ; Intermediate Filament Proteins/metabolism ; Intermediate Filaments/metabolism ; Protein Binding ; Proteins/metabolism
Chemical Substances	Cytoskeletal Proteins ; Desmoplakins ; Intermediate Filament Proteins ; Proteins
Language	English
Publishing date	2007-01-30
Publishing country	United States
Document type	Journal Article
ZDB-ID	80136-7
ISSN	1523-1747 ; 0022-202X
ISSN (online)	1523-1747
ISSN	0022-202X
DOI	10.1038/sj.skinbio.6250008
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Article: The desmosome: cell science lessons from human diseases.

Kottke, Margaret D / Delva, Emmanuella / Kowalczyk, Andrew P

Journal of cell science

2006 Volume 119, Issue Pt 5, Page(s) 797–806

Abstract: Human skin diseases have revealed fundamental mechanisms by which cytoskeletal proteins contribute to tissue architecture and function. In particular, the analysis of epidermal blistering disorders and the role of keratin gene mutations in these diseases ...

Abstract	Human skin diseases have revealed fundamental mechanisms by which cytoskeletal proteins contribute to tissue architecture and function. In particular, the analysis of epidermal blistering disorders and the role of keratin gene mutations in these diseases has led to significant increases in our understanding of intermediate filament biology. The major cell-surface attachment site for intermediate filament networks is the desmosome, an adhesive intercellular junction prominent in the epidermis and the heart. During the past decade, substantial progress has been made in understanding the molecular basis of a variety of epidermal autoimmune diseases, skin fragility syndromes, and disorders that involve a combination of heart and skin defects caused by perturbations in desmosome structure and function. These human diseases reveal key roles for desmosomes in maintaining tissue integrity, but also suggest functions for desmosomal components in signal transduction pathways and epidermal organization.
MeSH term(s)	Cytoskeletal Proteins/immunology ; Cytoskeletal Proteins/metabolism ; Desmosomal Cadherins/immunology ; Desmosomal Cadherins/metabolism ; Desmosomes/chemistry ; Desmosomes/immunology ; Desmosomes/pathology ; Humans ; Skin Diseases/immunology ; Skin Diseases/pathology
Chemical Substances	Cytoskeletal Proteins ; Desmosomal Cadherins
Language	English
Publishing date	2006-03-01
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.02888
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Article ; Online: Intravenous cidofovir-induced resolution of disfiguring cutaneous human papillomavirus infection.

Kottke, Margaret D / Parker, Sareeta R S

Journal of the American Academy of Dermatology

2006 Volume 55, Issue 3, Page(s) 533–536

Abstract: Human papillomavirus infection is one of the most common and most distressing cutaneous diseases in patients with HIV infection. It is also a common, and often therapeutically challenging, infection in individuals who are immunologically competent. A ... ...

Abstract	Human papillomavirus infection is one of the most common and most distressing cutaneous diseases in patients with HIV infection. It is also a common, and often therapeutically challenging, infection in individuals who are immunologically competent. A wide range of therapeutic options exists for treating cutaneous human papillomavirus infections, but none is uniformly effective. In this report we describe a man with HIV-1 infection and disfiguring facial verruca vulgaris who demonstrated complete clinical response to intravenous cidofovir. Our report provides further support for the use of intravenous cidofovir as therapy for treatment-resistant and/or widespread cutaneous human papillomavirus infection.
MeSH term(s)	Adult ; Antiviral Agents/administration & dosage ; Antiviral Agents/therapeutic use ; Cytosine/administration & dosage ; Cytosine/analogs & derivatives ; Cytosine/therapeutic use ; Humans ; Injections, Intravenous ; Male ; Organophosphonates/administration & dosage ; Organophosphonates/therapeutic use ; Papillomavirus Infections/drug therapy ; Papillomavirus Infections/pathology ; Skin Diseases, Viral/drug therapy ; Skin Diseases, Viral/pathology ; Treatment Outcome
Chemical Substances	Antiviral Agents ; Organophosphonates ; Cytosine (8J337D1HZY) ; cidofovir (JIL713Q00N)
Language	English
Publishing date	2006-09
Publishing country	United States
Document type	Case Reports ; Journal Article
ZDB-ID	603641-7
ISSN	1097-6787 ; 0190-9622
ISSN (online)	1097-6787
ISSN	0190-9622
DOI	10.1016/j.jaad.2006.01.007
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Article: The desmosome: cell science lessons from human diseases

Kottke, Margaret D / Delva, Emmanuella / Kowalczyk, Andrew P

Journal of cell science. 2006 Mar. 1, v. 119, no. 5

2006

Abstract	Human skin diseases have revealed fundamental mechanisms by which cytoskeletal proteins contribute to tissue architecture and function. In particular, the analysis of epidermal blistering disorders and the role of keratin gene mutations in these diseases has led to significant increases in our understanding of intermediate filament biology. The major cell-surface attachment site for intermediate filament networks is the desmosome, an adhesive intercellular junction prominent in the epidermis and the heart. During the past decade, substantial progress has been made in understanding the molecular basis of a variety of epidermal autoimmune diseases, skin fragility syndromes, and disorders that involve a combination of heart and skin defects caused by perturbations in desmosome structure and function. These human diseases reveal key roles for desmosomes in maintaining tissue integrity, but also suggest functions for desmosomal components in signal transduction pathways and epidermal organization.
Language	English
Dates of publication	2006-0301
Size	p. 797-806.
Publishing place	The Company of Biologists Limited
Document type	Article
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
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Article: Pemphigus vulgaris IgG-induced desmoglein-3 endocytosis and desmosomal disassembly are mediated by a clathrin- and dynamin-independent mechanism.

Delva, Emmanuella / Jennings, Jean Marie / Calkins, Cathárine C / Kottke, Margaret D / Faundez, Victor / Kowalczyk, Andrew P

The Journal of biological chemistry

2008 Volume 283, Issue 26, Page(s) 18303–18313

Abstract: Pemphigus vulgaris (PV) is a life-threatening autoimmune disease characterized by oral mucosal erosions and epidermal blistering. The autoantibodies generated target the desmosomal cadherin desmoglein-3 (Dsg3). Previous studies demonstrate that upon PV ... ...

Abstract	Pemphigus vulgaris (PV) is a life-threatening autoimmune disease characterized by oral mucosal erosions and epidermal blistering. The autoantibodies generated target the desmosomal cadherin desmoglein-3 (Dsg3). Previous studies demonstrate that upon PV IgG binding, Dsg3 is internalized and enters an endo-lysosomal pathway where it is degraded. To define the endocytic machinery involved in PV IgG-induced Dsg3 internalization, human keratinocytes were incubated with PV IgG, and various tools were used to perturb distinct endocytic pathways. The PV IgG.Dsg3 complex failed to colocalize with clathrin, and inhibitors of clathrin- and dynamin-dependent pathways had little or no effect on Dsg3 internalization. In contrast, cholesterol binding agents such as filipin and nystatin and the tyrosine kinase inhibitor genistein dramatically inhibited Dsg3 internalization. Furthermore, the Dsg3 cytoplasmic tail specified sensitivity to these inhibitors. Moreover, inhibition of Dsg3 endocytosis with genistein prevented disruption of desmosomes and loss of adhesion in the presence of PV IgG. Altogether, these results suggest that PV IgG-induced Dsg3 internalization is mediated through a clathrin- and dynamin-independent pathway and that Dsg3 endocytosis is tightly coupled to the pathogenic activity of PV IgG.
MeSH term(s)	Cell Adhesion ; Cells, Cultured ; Clathrin/chemistry ; Cytoplasm/metabolism ; Desmoglein 3/chemistry ; Dynamins/chemistry ; Endocytosis ; Gene Expression Regulation ; Genistein/pharmacology ; Humans ; Immunoglobulin G/chemistry ; Keratinocytes/cytology ; Keratinocytes/metabolism ; Pemphigus/immunology ; Protein Binding ; Protein-Tyrosine Kinases/metabolism
Chemical Substances	Clathrin ; Desmoglein 3 ; Immunoglobulin G ; Genistein (DH2M523P0H) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; Dynamins (EC 3.6.5.5)
Language	English
Publishing date	2008-04-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M710046200
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Article ; Online: Desmosome disassembly in response to pemphigus vulgaris IgG occurs in distinct phases and can be reversed by expression of exogenous Dsg3.

Jennings, Jean M / Tucker, Dana K / Kottke, Margaret D / Saito, Masataka / Delva, Emmanuella / Hanakawa, Yasushi / Amagai, Masayuki / Kowalczyk, Andrew P

The Journal of investigative dermatology

2010 Volume 131, Issue 3, Page(s) 706–718

Abstract: Pemphigus vulgaris (PV) is an epidermal blistering disorder caused by antibodies directed against the desmosomal cadherin desmoglein-3 (Dsg3). The mechanism by which PV IgG disrupts adhesion is not fully understood. To address this issue, primary human ... ...

Abstract	Pemphigus vulgaris (PV) is an epidermal blistering disorder caused by antibodies directed against the desmosomal cadherin desmoglein-3 (Dsg3). The mechanism by which PV IgG disrupts adhesion is not fully understood. To address this issue, primary human keratinocytes (KCs) and patient IgG were used to define the morphological, biochemical, and functional changes triggered by PV IgG. Three phases of desmosome disassembly were distinguished. Analysis of fixed and living KCs demonstrated that PV IgG cause rapid Dsg3 internalization, which likely originates from a non-junctional pool of Dsg3. Subsequently, Dsg3 and other desmosomal components rearrange into linear arrays that run perpendicular to cell contacts. Dsg3 complexes localized at the cell surface are transported in a retrograde manner along with these arrays before being released into cytoplasmic vesicular compartments. These changes in Dsg3 distribution are followed by depletion of detergent-insoluble Dsg3 pools and by the loss of cell adhesion strength. Importantly, this process of disassembly can be prevented by expressing exogenous Dsg3, thereby driving Dsg3 biosynthesis and desmosome assembly. These data support a model in which PV IgG cause the loss of cell adhesion by altering the dynamics of Dsg3 assembly into desmosomes and the turnover of cell surface pools of Dsg3 through endocytic pathways.
MeSH term(s)	Antibodies/blood ; Antibodies/pharmacology ; Cell Adhesion/drug effects ; Cells, Cultured ; Desmoglein 3/metabolism ; Desmoglein 3/pharmacology ; Desmosomes/drug effects ; Desmosomes/metabolism ; Desmosomes/ultrastructure ; Endocytosis/drug effects ; Humans ; Immunoglobulin G/metabolism ; Immunoglobulin G/pharmacology ; Keratinocytes/cytology ; Keratinocytes/drug effects ; Keratinocytes/metabolism ; Male ; Microscopy, Immunoelectron ; Pemphigus/blood ; Pemphigus/immunology
Chemical Substances	Antibodies ; DSG3 protein, human ; Desmoglein 3 ; Immunoglobulin G
Language	English
Publishing date	2010-12-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80136-7
ISSN	1523-1747 ; 0022-202X
ISSN (online)	1523-1747
ISSN	0022-202X
DOI	10.1038/jid.2010.389
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Article ; Online: A Framework for Outpatient Infusion of Antispike Monoclonal Antibodies to High-Risk Patients with Mild-to-Moderate Coronavirus Disease-19: The Mayo Clinic Model.

Razonable, Raymund R / Aloia, Nicole C E / Anderson, Ryan J / Anil, Gokhan / Arndt, Lori L / Arndt, Richard F / Ausman, Sara E / Bell, Sarah J / Bierle, Dennis M / Billings, Marcie L / Bishop, Rachel K / Cramer, Carl H / Culbertson, Tracy L / Dababneh, Ala S / Derr, Amber N / Epps, Kevin / Flaker, Susan M / Ganesh, Ravindra / Gilmer, Mary A /

Urena, Eric Gomez / Gulden, Christopher R / Haack, Tamara L / Hanson, Sara N / Herzog, Jenna R / Heyliger, Alexander / Hokanson, Lex D / Hopkins, Laura H / Horecki, Richard J / Krishna, Bipinchandra Hirisave / Huskins, W Charles / Jackson, Tammy A / Johnson, Ryan R / Jorgenson, Betty / Kudrna, Cory / Kennedy, Brian D / Klingsporn, Mary K / Kottke, Brian / Larsen, Jennifer J / Lessard, Sarah R / Lutwick, Larry I / Malone, Edward J / Matoush, Jennifer A / Micallef, Ivana N / Moehnke, Darcie E / Mohamed, Muhanad / Ness, Colleena N / Olson, Shelly M / Orenstein, Robert / Palraj, Raj / Patel, Janki / Paulson, Damian J / Phelan, David / Peinovich, Margaret T / Ramsey, Wilford L / Rau-Kane, Taunya J / Reid, Kevin I / Reinschmidt, Karen J / Seville, Maria Teresa / Skold, Erin C / Smith, Jill M / Speicher, Leigh L / Spielman, Laurie A / Springer, Donna J / Sweeten, Perry W / Tempelis, Jennifer M / Tulledge-Scheitel, Sidna / Vergidis, Paschalis / Whipple, Daniel C / Wilker, Caroline G / Destro Borgen, Molly J

Mayo Clinic proceedings

2021 Volume 96, Issue 5, Page(s) 1250–1261

Abstract: The administration of spike monoclonal antibody treatment to patients with mild to moderate COVID-19 is very challenging. This article summarizes essential components and processes in establishing an effective spike monoclonal antibody infusion program. ... ...

Abstract	The administration of spike monoclonal antibody treatment to patients with mild to moderate COVID-19 is very challenging. This article summarizes essential components and processes in establishing an effective spike monoclonal antibody infusion program. Rapid identification of a dedicated physical infrastructure was essential to circumvent the logistical challenges of caring for infectious patients while maintaining compliance with regulations and ensuring the safety of our personnel and other patients. Our partnerships and collaborations among multiple different specialties and disciplines enabled contributions from personnel with specific expertise in medicine, nursing, pharmacy, infection prevention and control, electronic health record (EHR) informatics, compliance, legal, medical ethics, engineering, administration, and other critical areas. Clear communication and a culture in which all roles are welcomed at the planning and operational tables are critical to the rapid development and refinement needed to adapt and thrive in providing this time-sensitive beneficial therapy. Our partnerships with leaders and providers outside our institutions, including those who care for underserved populations, have promoted equity in the access of monoclonal antibodies in our regions. Strong support from institutional leadership facilitated expedited action when needed, from a physical, personnel, and system infrastructure standpoint. Our ongoing real-time assessment and monitoring of our clinical program allowed us to improve and optimize our processes to ensure that the needs of our patients with COVID-19 in the outpatient setting are met.
MeSH term(s)	Antibodies, Monoclonal/administration & dosage ; Antiviral Agents/administration & dosage ; COVID-19/epidemiology ; COVID-19/therapy ; Clinical Protocols ; Critical Pathways/organization & administration ; Critical Pathways/trends ; Efficiency, Organizational ; Home Infusion Therapy/methods ; Home Infusion Therapy/standards ; Humans ; Intersectoral Collaboration ; Organizational Culture ; Program Development/methods ; SARS-CoV-2/immunology ; SARS-CoV-2/isolation & purification ; Severity of Illness Index ; Spike Glycoprotein, Coronavirus/antagonists & inhibitors ; Spike Glycoprotein, Coronavirus/immunology ; United States/epidemiology
Chemical Substances	Antibodies, Monoclonal ; Antiviral Agents ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
Language	English
Publishing date	2021-03-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	124027-4
ISSN	1942-5546 ; 0025-6196
ISSN (online)	1942-5546
ISSN	0025-6196
DOI	10.1016/j.mayocp.2021.03.010
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Article: Pemphigus Vulgaris IgG-induced Desmoglein-3 Endocytosis and Desmosomal Disassembly Are Mediated by a Clathrin- and Dynamin-independent Mechanism

Delva, Emmanuella / Jennings, Jean Marie / Calkins, Cathárine C / Kottke, Margaret D / Faundez, Victor / Kowalczyk, Andrew P

Journal of biological chemistry. 2008 June 27, v. 283, no. 26

2008

Abstract	Pemphigus vulgaris (PV) is a life-threatening autoimmune disease characterized by oral mucosal erosions and epidermal blistering. The autoantibodies generated target the desmosomal cadherin desmoglein-3 (Dsg3). Previous studies demonstrate that upon PV IgG binding, Dsg3 is internalized and enters an endo-lysosomal pathway where it is degraded. To define the endocytic machinery involved in PV IgG-induced Dsg3 internalization, human keratinocytes were incubated with PV IgG, and various tools were used to perturb distinct endocytic pathways. The PV IgG ·Dsg3 complex failed to colocalize with clathrin, and inhibitors of clathrin- and dynamin-dependent pathways had little or no effect on Dsg3 internalization. In contrast, cholesterol binding agents such as filipin and nystatin and the tyrosine kinase inhibitor genistein dramatically inhibited Dsg3 internalization. Furthermore, the Dsg3 cytoplasmic tail specified sensitivity to these inhibitors. Moreover, inhibition of Dsg3 endocytosis with genistein prevented disruption of desmosomes and loss of adhesion in the presence of PV IgG. Altogether, these results suggest that PV IgG-induced Dsg3 internalization is mediated through a clathrin- and dynamin-independent pathway and that Dsg3 endocytosis is tightly coupled to the pathogenic activity of PV IgG.
Language	English
Dates of publication	2008-0627
Size	p. 18303-18313.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
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Article: Cellular levels of p120 catenin function as a set point for cadherin expression levels in microvascular endothelial cells.

Xiao, Kanyan / Allison, David F / Buckley, Kathleen M / Kottke, Margaret D / Vincent, Peter A / Faundez, Victor / Kowalczyk, Andrew P

The Journal of cell biology

2003 Volume 163, Issue 3, Page(s) 535–545

Abstract: The mechanisms by which catenins regulate cadherin function are not fully understood, and the precise function of p120 catenin (p120ctn) has remained particularly elusive. In microvascular endothelial cells, p120ctn colocalized extensively with cell ... ...

Abstract	The mechanisms by which catenins regulate cadherin function are not fully understood, and the precise function of p120 catenin (p120ctn) has remained particularly elusive. In microvascular endothelial cells, p120ctn colocalized extensively with cell surface VE-cadherin, but failed to colocalize with VE-cadherin that had entered intracellular degradative compartments. To test the possibility that p120ctn binding to VE-cadherin regulates VE-cadherin internalization, a series of approaches were undertaken to manipulate p120ctn availability to endogenous VE-cadherin. Expression of VE-cadherin mutants that competed for p120ctn binding triggered the degradation of endogenous VE-cadherin. Similarly, reducing levels of p120ctn using siRNA caused a dramatic and dose-related reduction in cellular levels of VE-cadherin. In contrast, overexpression of p120ctn increased VE-cadherin cell surface levels and inhibited entry of cell surface VE-cadherin into degradative compartments. These results demonstrate that cellular levels of p120ctn function as a set point mechanism that regulates cadherin expression levels, and that a major function of p120ctn is to control cadherin internalization and degradation.
MeSH term(s)	Antigens, CD ; Cadherins/genetics ; Cadherins/metabolism ; Catenins ; Cell Adhesion/genetics ; Cell Adhesion Molecules/antagonists & inhibitors ; Cell Adhesion Molecules/genetics ; Cell Adhesion Molecules/metabolism ; Cell Line ; Endocytosis/genetics ; Endothelium, Vascular/metabolism ; Feedback, Physiological/genetics ; Humans ; Mutation/genetics ; Phosphoproteins/antagonists & inhibitors ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Protein Binding/drug effects ; Protein Binding/genetics ; Protein Transport/genetics ; RNA, Small Interfering/pharmacology
Chemical Substances	Antigens, CD ; Cadherins ; Catenins ; Cell Adhesion Molecules ; Phosphoproteins ; RNA, Small Interfering ; cadherin 5 ; delta catenin
Language	English
Publishing date	2003-11-10
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	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.200306001
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