Expression of discoidin domain receptor 1 tyrosine kinase on the human bronchial epithelium

O. Sakamoto, M. Suga, T. Suda, M. Ando

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Discoidin domain receptor 1 (DDR1) tyrosine kinases constitute a novel family of receptors characterized by a unique structure in the ectodomain (discoidin-I domain). The DDR1 ligand is the extracellular matrix protein collagen. To identify receptor tyrosine kinases (RTKs) involved in control of growth and differentiation of human bronchial epithelial (HBE) cells, a polymerase chain reaction-based search for RTKs in HBE cells was performed. DDR1 was the most abundant clone identified. Northern analysis detected a 3.6 kb DDR1 messenger ribonucleic acid (mRNA) expressed in HBE cells and transformed HBE lines, BET-1A and BEAS-2B. In addition, fluorescence-activated cell sorter (FACS) analyses using an anti-DDR1 antibody showed that DDR1 was expressed on HBE cells and two HBE lines. Immunohistochemical staining using human bronchial tissue demonstrated that DDR1 was mainly expressed at the basolateral cell surface of the bronchial epithelium. Furthermore, immunostaining of type IV collagen, a major component of the basement membrane, clearly showed that the basement membrane was closely attached to the basal surface of the bronchial epithelium. Since collagen binds to and activates discoidin domain receptor 1 tyrosine kinase, colocalization of discoidin domain receptor 1 and its ligand type IV collagen demonstrates a potential interaction of discoidin domain receptor 1 on the bronchial epithelium with type IV collagen. Further study of this interaction may define the functional significance of the collagen-discoidin domain receptor 1 signalling pathway in health and in disease.

Original languageEnglish
Pages (from-to)969-974
Number of pages6
JournalEuropean Respiratory Journal
Volume17
Issue number5
DOIs
Publication statusPublished - 2001

Fingerprint

Epithelium
Collagen Type IV
Epithelial Cells
Collagen
Receptor Protein-Tyrosine Kinases
Basement Membrane
Discoidin Domain Receptor 1
Ligands
Extracellular Matrix Proteins
Clone Cells
Fluorescence
RNA
Staining and Labeling
Polymerase Chain Reaction
Antibodies
Health
Growth

Keywords

  • Bronchial epithelium
  • Discoidin domain receptor 1
  • Receptor tyrosine kinase
  • Type IV collagen

ASJC Scopus subject areas

  • Pulmonary and Respiratory Medicine

Cite this

Expression of discoidin domain receptor 1 tyrosine kinase on the human bronchial epithelium. / Sakamoto, O.; Suga, M.; Suda, T.; Ando, M.

In: European Respiratory Journal, Vol. 17, No. 5, 2001, p. 969-974.

Research output: Contribution to journalArticle

Sakamoto, O. ; Suga, M. ; Suda, T. ; Ando, M. / Expression of discoidin domain receptor 1 tyrosine kinase on the human bronchial epithelium. In: European Respiratory Journal. 2001 ; Vol. 17, No. 5. pp. 969-974.
@article{daa64b405f5f40509514a73f8fcbc7d8,
title = "Expression of discoidin domain receptor 1 tyrosine kinase on the human bronchial epithelium",
abstract = "Discoidin domain receptor 1 (DDR1) tyrosine kinases constitute a novel family of receptors characterized by a unique structure in the ectodomain (discoidin-I domain). The DDR1 ligand is the extracellular matrix protein collagen. To identify receptor tyrosine kinases (RTKs) involved in control of growth and differentiation of human bronchial epithelial (HBE) cells, a polymerase chain reaction-based search for RTKs in HBE cells was performed. DDR1 was the most abundant clone identified. Northern analysis detected a 3.6 kb DDR1 messenger ribonucleic acid (mRNA) expressed in HBE cells and transformed HBE lines, BET-1A and BEAS-2B. In addition, fluorescence-activated cell sorter (FACS) analyses using an anti-DDR1 antibody showed that DDR1 was expressed on HBE cells and two HBE lines. Immunohistochemical staining using human bronchial tissue demonstrated that DDR1 was mainly expressed at the basolateral cell surface of the bronchial epithelium. Furthermore, immunostaining of type IV collagen, a major component of the basement membrane, clearly showed that the basement membrane was closely attached to the basal surface of the bronchial epithelium. Since collagen binds to and activates discoidin domain receptor 1 tyrosine kinase, colocalization of discoidin domain receptor 1 and its ligand type IV collagen demonstrates a potential interaction of discoidin domain receptor 1 on the bronchial epithelium with type IV collagen. Further study of this interaction may define the functional significance of the collagen-discoidin domain receptor 1 signalling pathway in health and in disease.",
keywords = "Bronchial epithelium, Discoidin domain receptor 1, Receptor tyrosine kinase, Type IV collagen",
author = "O. Sakamoto and M. Suga and T. Suda and M. Ando",
year = "2001",
doi = "10.1183/09031936.01.17509690",
language = "English",
volume = "17",
pages = "969--974",
journal = "European Respiratory Journal",
issn = "0903-1936",
publisher = "European Respiratory Society",
number = "5",

}

TY - JOUR

T1 - Expression of discoidin domain receptor 1 tyrosine kinase on the human bronchial epithelium

AU - Sakamoto, O.

AU - Suga, M.

AU - Suda, T.

AU - Ando, M.

PY - 2001

Y1 - 2001

N2 - Discoidin domain receptor 1 (DDR1) tyrosine kinases constitute a novel family of receptors characterized by a unique structure in the ectodomain (discoidin-I domain). The DDR1 ligand is the extracellular matrix protein collagen. To identify receptor tyrosine kinases (RTKs) involved in control of growth and differentiation of human bronchial epithelial (HBE) cells, a polymerase chain reaction-based search for RTKs in HBE cells was performed. DDR1 was the most abundant clone identified. Northern analysis detected a 3.6 kb DDR1 messenger ribonucleic acid (mRNA) expressed in HBE cells and transformed HBE lines, BET-1A and BEAS-2B. In addition, fluorescence-activated cell sorter (FACS) analyses using an anti-DDR1 antibody showed that DDR1 was expressed on HBE cells and two HBE lines. Immunohistochemical staining using human bronchial tissue demonstrated that DDR1 was mainly expressed at the basolateral cell surface of the bronchial epithelium. Furthermore, immunostaining of type IV collagen, a major component of the basement membrane, clearly showed that the basement membrane was closely attached to the basal surface of the bronchial epithelium. Since collagen binds to and activates discoidin domain receptor 1 tyrosine kinase, colocalization of discoidin domain receptor 1 and its ligand type IV collagen demonstrates a potential interaction of discoidin domain receptor 1 on the bronchial epithelium with type IV collagen. Further study of this interaction may define the functional significance of the collagen-discoidin domain receptor 1 signalling pathway in health and in disease.

AB - Discoidin domain receptor 1 (DDR1) tyrosine kinases constitute a novel family of receptors characterized by a unique structure in the ectodomain (discoidin-I domain). The DDR1 ligand is the extracellular matrix protein collagen. To identify receptor tyrosine kinases (RTKs) involved in control of growth and differentiation of human bronchial epithelial (HBE) cells, a polymerase chain reaction-based search for RTKs in HBE cells was performed. DDR1 was the most abundant clone identified. Northern analysis detected a 3.6 kb DDR1 messenger ribonucleic acid (mRNA) expressed in HBE cells and transformed HBE lines, BET-1A and BEAS-2B. In addition, fluorescence-activated cell sorter (FACS) analyses using an anti-DDR1 antibody showed that DDR1 was expressed on HBE cells and two HBE lines. Immunohistochemical staining using human bronchial tissue demonstrated that DDR1 was mainly expressed at the basolateral cell surface of the bronchial epithelium. Furthermore, immunostaining of type IV collagen, a major component of the basement membrane, clearly showed that the basement membrane was closely attached to the basal surface of the bronchial epithelium. Since collagen binds to and activates discoidin domain receptor 1 tyrosine kinase, colocalization of discoidin domain receptor 1 and its ligand type IV collagen demonstrates a potential interaction of discoidin domain receptor 1 on the bronchial epithelium with type IV collagen. Further study of this interaction may define the functional significance of the collagen-discoidin domain receptor 1 signalling pathway in health and in disease.

KW - Bronchial epithelium

KW - Discoidin domain receptor 1

KW - Receptor tyrosine kinase

KW - Type IV collagen

UR - http://www.scopus.com/inward/record.url?scp=0034954802&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034954802&partnerID=8YFLogxK

U2 - 10.1183/09031936.01.17509690

DO - 10.1183/09031936.01.17509690

M3 - Article

C2 - 11488334

AN - SCOPUS:0034954802

VL - 17

SP - 969

EP - 974

JO - European Respiratory Journal

JF - European Respiratory Journal

SN - 0903-1936

IS - 5

ER -