Intercellular adhesion molecule-4 binds alpha(4)beta(1) and alpha(V)-family integrins through novel integrin-binding mechanisms
Spring, Frances A. ; Parsons, Stephen F. ; Ortlepp, Susan ; Olsson, Martin L LU
; Sessions, Richard
; Brady, R. Leo
and Anstee, David J.
(2001)
In Blood
98(2).
p.458-466
- Abstract
- The LW blood group glycoprotein, ICAM-4, is a member of the intercellular adhesion molecule (ICAM) family expressed in erythroid cells. To begin to address the function of this molecule, ligands for ICAM-4 on hemopoietic and nonhemopoietic cell lines were identified. Peptide inhibition studies suggest that adhesion of cell lines to an ICAM-4-Fc construct is mediated by an LDV-inhibitable integrin on hemopoietic cells and an RGD-inhibitable integrin on nonhemopoietic cells. Antibody inhibition studies identified the hemopoietic integrin as alpha(4)beta(1.) Antibody inhibition studies on alpha(4)beta(1)-negative, nonhemopoietic cell lines suggested that adhesion of these cells is mediated by alpha(V) integrins (notably alpha(V)beta(1) and... (More)
- The LW blood group glycoprotein, ICAM-4, is a member of the intercellular adhesion molecule (ICAM) family expressed in erythroid cells. To begin to address the function of this molecule, ligands for ICAM-4 on hemopoietic and nonhemopoietic cell lines were identified. Peptide inhibition studies suggest that adhesion of cell lines to an ICAM-4-Fc construct is mediated by an LDV-inhibitable integrin on hemopoietic cells and an RGD-inhibitable integrin on nonhemopoietic cells. Antibody inhibition studies identified the hemopoietic integrin as alpha(4)beta(1.) Antibody inhibition studies on alpha(4)beta(1)-negative, nonhemopoietic cell lines suggested that adhesion of these cells is mediated by alpha(V) integrins (notably alpha(V)beta(1) and alpha(V)beta(5)). The structure of ICAM-4 modeled on the crystal structure of ICAM-2 was used to identify surface-exposed amino acid residues for site-directed mutagenesis. Neither an unusual LETS nor an LDV motif in the first domain of ICAM-4 was critical for integrin binding. ICAM-4 is the first ICAM family member shown to be a ligand for integrins other than those of the beta(2) family, and the data suggest that ICAM-4 has a novel integrin-binding site(s). These findings suggest a role for ICAM-4 in normal erythropoiesis and may also be relevant to the adhesive interactions of sickle cells. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1122642
- author
- Spring, Frances A.
; Parsons, Stephen F.
; Ortlepp, Susan
; Olsson, Martin L
LU
; Sessions, Richard
; Brady, R. Leo
and Anstee, David J.
- organization
- publishing date
- 2001
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Blood
- volume
- 98
- issue
- 2
- pages
- 458 - 466
- publisher
- American Society of Hematology
- external identifiers
-
- pmid:11435317
- ISSN
- 1528-0020
- language
- English
- LU publication?
- yes
- id
- 7732fef0-2fe0-4a10-9579-e28acdec3b5d (old id 1122642)
- alternative location
- http://bloodjournal.hematologylibrary.org/cgi/content/full/98/2/458
- date added to LUP
- 2016-04-01 12:29:10
- date last changed
- 2022-01-25 12:53:44
@article{7732fef0-2fe0-4a10-9579-e28acdec3b5d,
abstract = {{The LW blood group glycoprotein, ICAM-4, is a member of the intercellular adhesion molecule (ICAM) family expressed in erythroid cells. To begin to address the function of this molecule, ligands for ICAM-4 on hemopoietic and nonhemopoietic cell lines were identified. Peptide inhibition studies suggest that adhesion of cell lines to an ICAM-4-Fc construct is mediated by an LDV-inhibitable integrin on hemopoietic cells and an RGD-inhibitable integrin on nonhemopoietic cells. Antibody inhibition studies identified the hemopoietic integrin as alpha(4)beta(1.) Antibody inhibition studies on alpha(4)beta(1)-negative, nonhemopoietic cell lines suggested that adhesion of these cells is mediated by alpha(V) integrins (notably alpha(V)beta(1) and alpha(V)beta(5)). The structure of ICAM-4 modeled on the crystal structure of ICAM-2 was used to identify surface-exposed amino acid residues for site-directed mutagenesis. Neither an unusual LETS nor an LDV motif in the first domain of ICAM-4 was critical for integrin binding. ICAM-4 is the first ICAM family member shown to be a ligand for integrins other than those of the beta(2) family, and the data suggest that ICAM-4 has a novel integrin-binding site(s). These findings suggest a role for ICAM-4 in normal erythropoiesis and may also be relevant to the adhesive interactions of sickle cells.}},
author = {{Spring, Frances A. and Parsons, Stephen F. and Ortlepp, Susan and Olsson, Martin L and Sessions, Richard and Brady, R. Leo and Anstee, David J.}},
issn = {{1528-0020}},
language = {{eng}},
number = {{2}},
pages = {{458--466}},
publisher = {{American Society of Hematology}},
series = {{Blood}},
title = {{Intercellular adhesion molecule-4 binds alpha(4)beta(1) and alpha(V)-family integrins through novel integrin-binding mechanisms}},
url = {{http://bloodjournal.hematologylibrary.org/cgi/content/full/98/2/458}},
volume = {{98}},
year = {{2001}},
}