Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies

Yoshikazu Takada, Wilma Puzon

研究成果: 雜誌貢獻文章

173 引文 (Scopus)

摘要

Members of the β1 integrin subfamily recognize multiple ligands such as fibronectin, laminin, and collagen and mediate cell-cell and cell-extracellular matrix interactions, β1 subunit may play a central role in regulating β1 integrin avidity. Here we have identified a small region of β1 subunit (residues 207-218) that is critical for the binding of both activating (8A2, A1A5, and TS2/16) and inhibiting (4B4, 4B5, 13, AIIB2, and P4C10) monoclonal antibodies against human β1 using interspecies chimeric β1 and site-directed mutagenesis. Chicken β1 that has human sequence within residues 207-218 (CH mutant) is recognized by all the human specific antibodies listed above. The region 207-218 is located between the two putative ligand binding sites (residues 120-182 and 220-231), and the amino acid sequence of the region involves a predicted bend structure. The other anti-β1 antibodies that do not affect cell . attachment to ligands (K20, 102DF5, LM442, and LM534) recognized the carboxyl-terminal regions of extracellular domain of β1 (residues 426-587 for K20 and 588-708 for 102DF5, LM442, and LM534, respectively). Our data suggest a potential mechanism for the avidity regulation of β1 integrin through conformational changes of β1 subunit.

原文英語
頁(從 - 到)17597-17601
頁數5
期刊Journal of Biological Chemistry
268
發行號23
出版狀態已發佈 - 八月 15 1993
對外發佈Yes

指紋

Nucleic Acid Regulatory Sequences
Integrins
Ligands
Antibodies
Mutagenesis
Laminin
Fibronectins
Collagen
Site-Directed Mutagenesis
Binding Sites
Monoclonal Antibodies
Extracellular Matrix
Amino Acids
Anti-Idiotypic Antibodies
Amino Acid Sequence
Chickens

ASJC Scopus subject areas

  • Biochemistry

引用此文

Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies. / Takada, Yoshikazu; Puzon, Wilma.

於: Journal of Biological Chemistry, 卷 268, 編號 23, 15.08.1993, p. 17597-17601.

研究成果: 雜誌貢獻文章

@article{1f62449a4052464bbe31a229b079588b,
title = "Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies",
abstract = "Members of the β1 integrin subfamily recognize multiple ligands such as fibronectin, laminin, and collagen and mediate cell-cell and cell-extracellular matrix interactions, β1 subunit may play a central role in regulating β1 integrin avidity. Here we have identified a small region of β1 subunit (residues 207-218) that is critical for the binding of both activating (8A2, A1A5, and TS2/16) and inhibiting (4B4, 4B5, 13, AIIB2, and P4C10) monoclonal antibodies against human β1 using interspecies chimeric β1 and site-directed mutagenesis. Chicken β1 that has human sequence within residues 207-218 (CH mutant) is recognized by all the human specific antibodies listed above. The region 207-218 is located between the two putative ligand binding sites (residues 120-182 and 220-231), and the amino acid sequence of the region involves a predicted bend structure. The other anti-β1 antibodies that do not affect cell . attachment to ligands (K20, 102DF5, LM442, and LM534) recognized the carboxyl-terminal regions of extracellular domain of β1 (residues 426-587 for K20 and 588-708 for 102DF5, LM442, and LM534, respectively). Our data suggest a potential mechanism for the avidity regulation of β1 integrin through conformational changes of β1 subunit.",
author = "Yoshikazu Takada and Wilma Puzon",
year = "1993",
month = "8",
day = "15",
language = "English",
volume = "268",
pages = "17597--17601",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "23",

}

TY - JOUR

T1 - Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies

AU - Takada, Yoshikazu

AU - Puzon, Wilma

PY - 1993/8/15

Y1 - 1993/8/15

N2 - Members of the β1 integrin subfamily recognize multiple ligands such as fibronectin, laminin, and collagen and mediate cell-cell and cell-extracellular matrix interactions, β1 subunit may play a central role in regulating β1 integrin avidity. Here we have identified a small region of β1 subunit (residues 207-218) that is critical for the binding of both activating (8A2, A1A5, and TS2/16) and inhibiting (4B4, 4B5, 13, AIIB2, and P4C10) monoclonal antibodies against human β1 using interspecies chimeric β1 and site-directed mutagenesis. Chicken β1 that has human sequence within residues 207-218 (CH mutant) is recognized by all the human specific antibodies listed above. The region 207-218 is located between the two putative ligand binding sites (residues 120-182 and 220-231), and the amino acid sequence of the region involves a predicted bend structure. The other anti-β1 antibodies that do not affect cell . attachment to ligands (K20, 102DF5, LM442, and LM534) recognized the carboxyl-terminal regions of extracellular domain of β1 (residues 426-587 for K20 and 588-708 for 102DF5, LM442, and LM534, respectively). Our data suggest a potential mechanism for the avidity regulation of β1 integrin through conformational changes of β1 subunit.

AB - Members of the β1 integrin subfamily recognize multiple ligands such as fibronectin, laminin, and collagen and mediate cell-cell and cell-extracellular matrix interactions, β1 subunit may play a central role in regulating β1 integrin avidity. Here we have identified a small region of β1 subunit (residues 207-218) that is critical for the binding of both activating (8A2, A1A5, and TS2/16) and inhibiting (4B4, 4B5, 13, AIIB2, and P4C10) monoclonal antibodies against human β1 using interspecies chimeric β1 and site-directed mutagenesis. Chicken β1 that has human sequence within residues 207-218 (CH mutant) is recognized by all the human specific antibodies listed above. The region 207-218 is located between the two putative ligand binding sites (residues 120-182 and 220-231), and the amino acid sequence of the region involves a predicted bend structure. The other anti-β1 antibodies that do not affect cell . attachment to ligands (K20, 102DF5, LM442, and LM534) recognized the carboxyl-terminal regions of extracellular domain of β1 (residues 426-587 for K20 and 588-708 for 102DF5, LM442, and LM534, respectively). Our data suggest a potential mechanism for the avidity regulation of β1 integrin through conformational changes of β1 subunit.

UR - http://www.scopus.com/inward/record.url?scp=0027248518&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027248518&partnerID=8YFLogxK

M3 - Article

C2 - 7688727

AN - SCOPUS:0027248518

VL - 268

SP - 17597

EP - 17601

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 23

ER -