Stepped changes of monovalent ligand-binding force during ligand-induced clustering of integrin αIIBβ3

Chia Fen Hsieh, Bo Jui Chang, Chyi Huey Pai, Hsuan Yi Chen, Jin Wu Tsaia, Yung Hsiang Yi, Yi Ting Chiang, Da Wei Wang, Sien Chi, Long Hsu, Chi Hung Lin

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Recent evidence demonstrated that conformational changes of the integrin during receptor activation affected its binding to extracellular matrix; however, experimental assessment of ligand-receptor binding following the initial molecular interaction has rarely been carried out at a single-molecule resolution. In the present study, laser tweezers were used to measure the binding force exerted by a live Chinese hamster ovary cell that expressed integrin αIIBβ3 (CHO α IIBβ3), to the bead carrier coated with the snake venom rhodostomin that served as an activated ligand for integrin αIIBβ3. A progressive increase of total binding force over time was noticed when the bead interacted with the CHO αIIBβ3 cell; such an increase was due mainly to the recruitment of more integrin molecules to the bead-cell interface. When the binding strength exerted by a single ligand-receptor pair was derived from the "polyvalent" measurements, surprisingly, a stepped decrease of the "monovalent binding force" was noted (from 4.15 to 2.54 piconewtons (pN)); such decrease appeared to occur during the ligand-induced integrin clustering process. On the other hand, the mutant rhodostomin defective in clustering integrins exhibited only one (1.81 pN) unit binding strength.

Original languageEnglish
Pages (from-to)25466-25474
Number of pages9
JournalJournal of Biological Chemistry
Volume281
Issue number35
DOIs
Publication statusPublished - Sep 1 2006
Externally publishedYes

Fingerprint

Integrins
Cluster Analysis
Ligands
Optical Tweezers
Snake Venoms
Molecules
Molecular interactions
CHO Cells
Cricetulus
Extracellular Matrix
Ovary
Chemical activation
Cells
Lasers
rhodostomin

ASJC Scopus subject areas

  • Biochemistry

Cite this

Stepped changes of monovalent ligand-binding force during ligand-induced clustering of integrin αIIBβ3 . / Hsieh, Chia Fen; Chang, Bo Jui; Pai, Chyi Huey; Chen, Hsuan Yi; Tsaia, Jin Wu; Yi, Yung Hsiang; Chiang, Yi Ting; Wang, Da Wei; Chi, Sien; Hsu, Long; Lin, Chi Hung.

In: Journal of Biological Chemistry, Vol. 281, No. 35, 01.09.2006, p. 25466-25474.

Research output: Contribution to journalArticle

Hsieh, CF, Chang, BJ, Pai, CH, Chen, HY, Tsaia, JW, Yi, YH, Chiang, YT, Wang, DW, Chi, S, Hsu, L & Lin, CH 2006, 'Stepped changes of monovalent ligand-binding force during ligand-induced clustering of integrin αIIBβ3 ', Journal of Biological Chemistry, vol. 281, no. 35, pp. 25466-25474. https://doi.org/10.1074/jbc.M601793200
Hsieh, Chia Fen ; Chang, Bo Jui ; Pai, Chyi Huey ; Chen, Hsuan Yi ; Tsaia, Jin Wu ; Yi, Yung Hsiang ; Chiang, Yi Ting ; Wang, Da Wei ; Chi, Sien ; Hsu, Long ; Lin, Chi Hung. / Stepped changes of monovalent ligand-binding force during ligand-induced clustering of integrin αIIBβ3 In: Journal of Biological Chemistry. 2006 ; Vol. 281, No. 35. pp. 25466-25474.
@article{2d41b19dab2147408591f24f15aa4422,
title = "Stepped changes of monovalent ligand-binding force during ligand-induced clustering of integrin αIIBβ3",
abstract = "Recent evidence demonstrated that conformational changes of the integrin during receptor activation affected its binding to extracellular matrix; however, experimental assessment of ligand-receptor binding following the initial molecular interaction has rarely been carried out at a single-molecule resolution. In the present study, laser tweezers were used to measure the binding force exerted by a live Chinese hamster ovary cell that expressed integrin αIIBβ3 (CHO α IIBβ3), to the bead carrier coated with the snake venom rhodostomin that served as an activated ligand for integrin αIIBβ3. A progressive increase of total binding force over time was noticed when the bead interacted with the CHO αIIBβ3 cell; such an increase was due mainly to the recruitment of more integrin molecules to the bead-cell interface. When the binding strength exerted by a single ligand-receptor pair was derived from the {"}polyvalent{"} measurements, surprisingly, a stepped decrease of the {"}monovalent binding force{"} was noted (from 4.15 to 2.54 piconewtons (pN)); such decrease appeared to occur during the ligand-induced integrin clustering process. On the other hand, the mutant rhodostomin defective in clustering integrins exhibited only one (1.81 pN) unit binding strength.",
author = "Hsieh, {Chia Fen} and Chang, {Bo Jui} and Pai, {Chyi Huey} and Chen, {Hsuan Yi} and Tsaia, {Jin Wu} and Yi, {Yung Hsiang} and Chiang, {Yi Ting} and Wang, {Da Wei} and Sien Chi and Long Hsu and Lin, {Chi Hung}",
year = "2006",
month = "9",
day = "1",
doi = "10.1074/jbc.M601793200",
language = "English",
volume = "281",
pages = "25466--25474",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "35",

}

TY - JOUR

T1 - Stepped changes of monovalent ligand-binding force during ligand-induced clustering of integrin αIIBβ3

AU - Hsieh, Chia Fen

AU - Chang, Bo Jui

AU - Pai, Chyi Huey

AU - Chen, Hsuan Yi

AU - Tsaia, Jin Wu

AU - Yi, Yung Hsiang

AU - Chiang, Yi Ting

AU - Wang, Da Wei

AU - Chi, Sien

AU - Hsu, Long

AU - Lin, Chi Hung

PY - 2006/9/1

Y1 - 2006/9/1

N2 - Recent evidence demonstrated that conformational changes of the integrin during receptor activation affected its binding to extracellular matrix; however, experimental assessment of ligand-receptor binding following the initial molecular interaction has rarely been carried out at a single-molecule resolution. In the present study, laser tweezers were used to measure the binding force exerted by a live Chinese hamster ovary cell that expressed integrin αIIBβ3 (CHO α IIBβ3), to the bead carrier coated with the snake venom rhodostomin that served as an activated ligand for integrin αIIBβ3. A progressive increase of total binding force over time was noticed when the bead interacted with the CHO αIIBβ3 cell; such an increase was due mainly to the recruitment of more integrin molecules to the bead-cell interface. When the binding strength exerted by a single ligand-receptor pair was derived from the "polyvalent" measurements, surprisingly, a stepped decrease of the "monovalent binding force" was noted (from 4.15 to 2.54 piconewtons (pN)); such decrease appeared to occur during the ligand-induced integrin clustering process. On the other hand, the mutant rhodostomin defective in clustering integrins exhibited only one (1.81 pN) unit binding strength.

AB - Recent evidence demonstrated that conformational changes of the integrin during receptor activation affected its binding to extracellular matrix; however, experimental assessment of ligand-receptor binding following the initial molecular interaction has rarely been carried out at a single-molecule resolution. In the present study, laser tweezers were used to measure the binding force exerted by a live Chinese hamster ovary cell that expressed integrin αIIBβ3 (CHO α IIBβ3), to the bead carrier coated with the snake venom rhodostomin that served as an activated ligand for integrin αIIBβ3. A progressive increase of total binding force over time was noticed when the bead interacted with the CHO αIIBβ3 cell; such an increase was due mainly to the recruitment of more integrin molecules to the bead-cell interface. When the binding strength exerted by a single ligand-receptor pair was derived from the "polyvalent" measurements, surprisingly, a stepped decrease of the "monovalent binding force" was noted (from 4.15 to 2.54 piconewtons (pN)); such decrease appeared to occur during the ligand-induced integrin clustering process. On the other hand, the mutant rhodostomin defective in clustering integrins exhibited only one (1.81 pN) unit binding strength.

UR - http://www.scopus.com/inward/record.url?scp=33748741297&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33748741297&partnerID=8YFLogxK

U2 - 10.1074/jbc.M601793200

DO - 10.1074/jbc.M601793200

M3 - Article

VL - 281

SP - 25466

EP - 25474

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 35

ER -