In vivo ultrastructural localization of the desmoglein 3 adhesive interface to the desmosome mid-line

Atsushi Shimizu, Akira Ishiko, Takayuki Ota, Hitoshi Saito, Hiroshi Oka, Kazuyuki Tsunoda, Masayuki Amagai, Takeji Nishikawa

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Desmoglein (Dsg) is a cadherin cell-cell adhesion molecule located in desmosomes and its precise mechanism for cell-cell adhesion still remains to be elucidated. Opposing cadherin molecules may adhere to the N-terminal EC1 domains, or the entire length of the extracellular (EC) domains may overlap. To solve this controversy, we performed immunoelectron microscopy to map the Dsg3 epitopes in desmosomes. Three different hybridoma cell lines producing anti-Dsg3 monoclonal antibodies (mAb) were intraperitoneally injected into immunodeficient mice and the precise ultrastructural location of bound IgG between the mucosal epithelial cells in vivo was statistically measured and analyzed. The binding site of the AK23 mAb that recognizes the N-terminal EC1 domain was localized to the electron-dense mid-line of desmosomes. The binding sites of AK7 and AK18, which recognize the C-terminal membrane proximal and middle portions of the EC domains, were localized to the desmosomal region proximal to the membrane and the region between the plasma membrane and the dense mid-line, respectively. These results indicate that the N-terminal regions of Dsg3 from opposing cells interact at the dense mid-line of desmosomes where EC1 overlaps.

Original languageEnglish
Pages (from-to)984-989
Number of pages6
JournalJournal of Investigative Dermatology
Volume124
Issue number5
DOIs
Publication statusPublished - 2005 May

Fingerprint

Desmoglein 3
Desmosomes
Cadherins
Adhesives
Desmogleins
Binding Sites
Monoclonal Antibodies
Membranes
Cell adhesion
Cell Adhesion Molecules
Cell membranes
Epitopes
Microscopic examination
Immunoglobulin G
Cells
Molecules
Immunoelectron Microscopy
Electrons
Hybridomas
Cell Adhesion

Keywords

  • Adhesion molecule
  • Cadherin
  • Immunoelectron microscopy
  • Pemphigus vulgaris

ASJC Scopus subject areas

  • Dermatology

Cite this

In vivo ultrastructural localization of the desmoglein 3 adhesive interface to the desmosome mid-line. / Shimizu, Atsushi; Ishiko, Akira; Ota, Takayuki; Saito, Hitoshi; Oka, Hiroshi; Tsunoda, Kazuyuki; Amagai, Masayuki; Nishikawa, Takeji.

In: Journal of Investigative Dermatology, Vol. 124, No. 5, 05.2005, p. 984-989.

Research output: Contribution to journalArticle

Shimizu, Atsushi ; Ishiko, Akira ; Ota, Takayuki ; Saito, Hitoshi ; Oka, Hiroshi ; Tsunoda, Kazuyuki ; Amagai, Masayuki ; Nishikawa, Takeji. / In vivo ultrastructural localization of the desmoglein 3 adhesive interface to the desmosome mid-line. In: Journal of Investigative Dermatology. 2005 ; Vol. 124, No. 5. pp. 984-989.
@article{225906524d8c4345bb224d2343808af3,
title = "In vivo ultrastructural localization of the desmoglein 3 adhesive interface to the desmosome mid-line",
abstract = "Desmoglein (Dsg) is a cadherin cell-cell adhesion molecule located in desmosomes and its precise mechanism for cell-cell adhesion still remains to be elucidated. Opposing cadherin molecules may adhere to the N-terminal EC1 domains, or the entire length of the extracellular (EC) domains may overlap. To solve this controversy, we performed immunoelectron microscopy to map the Dsg3 epitopes in desmosomes. Three different hybridoma cell lines producing anti-Dsg3 monoclonal antibodies (mAb) were intraperitoneally injected into immunodeficient mice and the precise ultrastructural location of bound IgG between the mucosal epithelial cells in vivo was statistically measured and analyzed. The binding site of the AK23 mAb that recognizes the N-terminal EC1 domain was localized to the electron-dense mid-line of desmosomes. The binding sites of AK7 and AK18, which recognize the C-terminal membrane proximal and middle portions of the EC domains, were localized to the desmosomal region proximal to the membrane and the region between the plasma membrane and the dense mid-line, respectively. These results indicate that the N-terminal regions of Dsg3 from opposing cells interact at the dense mid-line of desmosomes where EC1 overlaps.",
keywords = "Adhesion molecule, Cadherin, Immunoelectron microscopy, Pemphigus vulgaris",
author = "Atsushi Shimizu and Akira Ishiko and Takayuki Ota and Hitoshi Saito and Hiroshi Oka and Kazuyuki Tsunoda and Masayuki Amagai and Takeji Nishikawa",
year = "2005",
month = "5",
doi = "10.1111/j.0022-202X.2005.23706.x",
language = "English",
volume = "124",
pages = "984--989",
journal = "Journal of Investigative Dermatology",
issn = "0022-202X",
publisher = "Nature Publishing Group",
number = "5",

}

TY - JOUR

T1 - In vivo ultrastructural localization of the desmoglein 3 adhesive interface to the desmosome mid-line

AU - Shimizu, Atsushi

AU - Ishiko, Akira

AU - Ota, Takayuki

AU - Saito, Hitoshi

AU - Oka, Hiroshi

AU - Tsunoda, Kazuyuki

AU - Amagai, Masayuki

AU - Nishikawa, Takeji

PY - 2005/5

Y1 - 2005/5

N2 - Desmoglein (Dsg) is a cadherin cell-cell adhesion molecule located in desmosomes and its precise mechanism for cell-cell adhesion still remains to be elucidated. Opposing cadherin molecules may adhere to the N-terminal EC1 domains, or the entire length of the extracellular (EC) domains may overlap. To solve this controversy, we performed immunoelectron microscopy to map the Dsg3 epitopes in desmosomes. Three different hybridoma cell lines producing anti-Dsg3 monoclonal antibodies (mAb) were intraperitoneally injected into immunodeficient mice and the precise ultrastructural location of bound IgG between the mucosal epithelial cells in vivo was statistically measured and analyzed. The binding site of the AK23 mAb that recognizes the N-terminal EC1 domain was localized to the electron-dense mid-line of desmosomes. The binding sites of AK7 and AK18, which recognize the C-terminal membrane proximal and middle portions of the EC domains, were localized to the desmosomal region proximal to the membrane and the region between the plasma membrane and the dense mid-line, respectively. These results indicate that the N-terminal regions of Dsg3 from opposing cells interact at the dense mid-line of desmosomes where EC1 overlaps.

AB - Desmoglein (Dsg) is a cadherin cell-cell adhesion molecule located in desmosomes and its precise mechanism for cell-cell adhesion still remains to be elucidated. Opposing cadherin molecules may adhere to the N-terminal EC1 domains, or the entire length of the extracellular (EC) domains may overlap. To solve this controversy, we performed immunoelectron microscopy to map the Dsg3 epitopes in desmosomes. Three different hybridoma cell lines producing anti-Dsg3 monoclonal antibodies (mAb) were intraperitoneally injected into immunodeficient mice and the precise ultrastructural location of bound IgG between the mucosal epithelial cells in vivo was statistically measured and analyzed. The binding site of the AK23 mAb that recognizes the N-terminal EC1 domain was localized to the electron-dense mid-line of desmosomes. The binding sites of AK7 and AK18, which recognize the C-terminal membrane proximal and middle portions of the EC domains, were localized to the desmosomal region proximal to the membrane and the region between the plasma membrane and the dense mid-line, respectively. These results indicate that the N-terminal regions of Dsg3 from opposing cells interact at the dense mid-line of desmosomes where EC1 overlaps.

KW - Adhesion molecule

KW - Cadherin

KW - Immunoelectron microscopy

KW - Pemphigus vulgaris

UR - http://www.scopus.com/inward/record.url?scp=18244380061&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=18244380061&partnerID=8YFLogxK

U2 - 10.1111/j.0022-202X.2005.23706.x

DO - 10.1111/j.0022-202X.2005.23706.x

M3 - Article

VL - 124

SP - 984

EP - 989

JO - Journal of Investigative Dermatology

JF - Journal of Investigative Dermatology

SN - 0022-202X

IS - 5

ER -