Loading…
Heparin Is an Adhesive Ligand for the Leukocyte Integrin Mac-1 (CD11b/CD18)
Previous studies have demonstrated that the leukocyte integrin Mac-1 adheres to several cell surface and soluble ligands including intercellular adhesion molecule-1, fibrinogen, iC3b, and factor X. However, experiments with Mac-1-expressing transfectants, purified Mac-1, and mAbs to Mac-1 indicate t...
Saved in:
Published in: | The Journal of cell biology 1995-09, Vol.130 (6), p.1473-1482 |
---|---|
Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c499t-e1bfe2d1697e6dc56f754dabdf5ceac0f2661bc880654c00b821996eac47a5043 |
---|---|
cites | |
container_end_page | 1482 |
container_issue | 6 |
container_start_page | 1473 |
container_title | The Journal of cell biology |
container_volume | 130 |
creator | Diamond, Michael S. Alon, Ronen Parkos, Charles A. Quinn, Mark T. Springer, Timothy A. |
description | Previous studies have demonstrated that the leukocyte integrin Mac-1 adheres to several cell surface and soluble ligands including intercellular adhesion molecule-1, fibrinogen, iC3b, and factor X. However, experiments with Mac-1-expressing transfectants, purified Mac-1, and mAbs to Mac-1 indicate the existence of additional ligands. In this paper, we demonstrate a direct interaction between Mac-1 and heparan sulfate glycans. Heparin affinity resins immunoprecipitate Mac-1, and neutrophils and transfectant cells that express Mac-1 bind to heparin and heparan sulfate, but not to other sulfated glycosaminoglycans. Inhibition studies with mAbs and chemically modified forms of heparin suggest the I domain as a recognition site on Mac-1 for heparin, and suggest that either N- or O-sulfation is sufficient for heparin to bind efficiently to Mac-1. Under conditions of continuous flow in which heparins and E-selectin are cosubstrates, neutrophils tether to E-selectin and form firm adhesions through a Mac-1-heparin interaction. |
doi_str_mv | 10.1083/jcb.130.6.1473 |
format | article |
fullrecord | <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2120570</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>1617159</jstor_id><sourcerecordid>1617159</sourcerecordid><originalsourceid>FETCH-LOGICAL-c499t-e1bfe2d1697e6dc56f754dabdf5ceac0f2661bc880654c00b821996eac47a5043</originalsourceid><addsrcrecordid>eNpdkc9P2zAUx61pE-vYrpyYFHGY4JDwXuIfyQUJdQMqOu2ynS3HeWnTtXGxEyT-e1y1YoyLLev7fZ_3tb6MnSBkCGVxubJ1hgVkMkOuindsgoJDWiKH92wCkGNaiVx8ZJ9CWAEAV7w4YkdKiEpJNWH3d7Q1vuuTWUhMn1w3SwrdIyXzbmH6JmmdT4ZlfNL419mngZJZP9BiN_DT2BST8-l3xPoynuXFZ_ahNetAXw73Mftz8-P39C6d_7qdTa_nqeVVNaSEdUt5g7JSJBsrZKsEb0zdtMKSsdDmUmJtyxKk4BagLnOsKhklrowAXhyzqz13O9Ybaiz1gzdrvfXdxvgn7Uyn_1f6bqkX7lHnmINQEAHfDgDvHkYKg950wdJ6bXpyY9BKiRJjiGg8e2NcudH38XORpRBR8jKasr3JeheCp_YlCYLedaRjRzp2pKXedRQHvr7O_2I_lBL1072-CoPz_2gyrhRV8QxbhZRA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>217111648</pqid></control><display><type>article</type><title>Heparin Is an Adhesive Ligand for the Leukocyte Integrin Mac-1 (CD11b/CD18)</title><source>JSTOR Archival Journals and Primary Sources Collection</source><creator>Diamond, Michael S. ; Alon, Ronen ; Parkos, Charles A. ; Quinn, Mark T. ; Springer, Timothy A.</creator><creatorcontrib>Diamond, Michael S. ; Alon, Ronen ; Parkos, Charles A. ; Quinn, Mark T. ; Springer, Timothy A.</creatorcontrib><description>Previous studies have demonstrated that the leukocyte integrin Mac-1 adheres to several cell surface and soluble ligands including intercellular adhesion molecule-1, fibrinogen, iC3b, and factor X. However, experiments with Mac-1-expressing transfectants, purified Mac-1, and mAbs to Mac-1 indicate the existence of additional ligands. In this paper, we demonstrate a direct interaction between Mac-1 and heparan sulfate glycans. Heparin affinity resins immunoprecipitate Mac-1, and neutrophils and transfectant cells that express Mac-1 bind to heparin and heparan sulfate, but not to other sulfated glycosaminoglycans. Inhibition studies with mAbs and chemically modified forms of heparin suggest the I domain as a recognition site on Mac-1 for heparin, and suggest that either N- or O-sulfation is sufficient for heparin to bind efficiently to Mac-1. Under conditions of continuous flow in which heparins and E-selectin are cosubstrates, neutrophils tether to E-selectin and form firm adhesions through a Mac-1-heparin interaction.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.130.6.1473</identifier><identifier>PMID: 7559767</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Adhesives ; Animals ; Cell Adhesion ; Cellular biology ; CHO Cells ; Circulatory system ; Cricetinae ; Endothelial cells ; Fibrosis ; Heparin ; Heparin - metabolism ; Humans ; Integrins ; Leukocytes ; Ligands ; Macrophage-1 Antigen - metabolism ; Middle Aged ; Neutrophils ; Neutrophils - metabolism ; Sensitivity and Specificity ; Shear stress ; Sulfates</subject><ispartof>The Journal of cell biology, 1995-09, Vol.130 (6), p.1473-1482</ispartof><rights>Copyright 1995 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Sep 1995</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c499t-e1bfe2d1697e6dc56f754dabdf5ceac0f2661bc880654c00b821996eac47a5043</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/1617159$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/1617159$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,881,27903,27904,58216,58449</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7559767$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Diamond, Michael S.</creatorcontrib><creatorcontrib>Alon, Ronen</creatorcontrib><creatorcontrib>Parkos, Charles A.</creatorcontrib><creatorcontrib>Quinn, Mark T.</creatorcontrib><creatorcontrib>Springer, Timothy A.</creatorcontrib><title>Heparin Is an Adhesive Ligand for the Leukocyte Integrin Mac-1 (CD11b/CD18)</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Previous studies have demonstrated that the leukocyte integrin Mac-1 adheres to several cell surface and soluble ligands including intercellular adhesion molecule-1, fibrinogen, iC3b, and factor X. However, experiments with Mac-1-expressing transfectants, purified Mac-1, and mAbs to Mac-1 indicate the existence of additional ligands. In this paper, we demonstrate a direct interaction between Mac-1 and heparan sulfate glycans. Heparin affinity resins immunoprecipitate Mac-1, and neutrophils and transfectant cells that express Mac-1 bind to heparin and heparan sulfate, but not to other sulfated glycosaminoglycans. Inhibition studies with mAbs and chemically modified forms of heparin suggest the I domain as a recognition site on Mac-1 for heparin, and suggest that either N- or O-sulfation is sufficient for heparin to bind efficiently to Mac-1. Under conditions of continuous flow in which heparins and E-selectin are cosubstrates, neutrophils tether to E-selectin and form firm adhesions through a Mac-1-heparin interaction.</description><subject>Adhesives</subject><subject>Animals</subject><subject>Cell Adhesion</subject><subject>Cellular biology</subject><subject>CHO Cells</subject><subject>Circulatory system</subject><subject>Cricetinae</subject><subject>Endothelial cells</subject><subject>Fibrosis</subject><subject>Heparin</subject><subject>Heparin - metabolism</subject><subject>Humans</subject><subject>Integrins</subject><subject>Leukocytes</subject><subject>Ligands</subject><subject>Macrophage-1 Antigen - metabolism</subject><subject>Middle Aged</subject><subject>Neutrophils</subject><subject>Neutrophils - metabolism</subject><subject>Sensitivity and Specificity</subject><subject>Shear stress</subject><subject>Sulfates</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNpdkc9P2zAUx61pE-vYrpyYFHGY4JDwXuIfyQUJdQMqOu2ynS3HeWnTtXGxEyT-e1y1YoyLLev7fZ_3tb6MnSBkCGVxubJ1hgVkMkOuindsgoJDWiKH92wCkGNaiVx8ZJ9CWAEAV7w4YkdKiEpJNWH3d7Q1vuuTWUhMn1w3SwrdIyXzbmH6JmmdT4ZlfNL419mngZJZP9BiN_DT2BST8-l3xPoynuXFZ_ahNetAXw73Mftz8-P39C6d_7qdTa_nqeVVNaSEdUt5g7JSJBsrZKsEb0zdtMKSsdDmUmJtyxKk4BagLnOsKhklrowAXhyzqz13O9Ybaiz1gzdrvfXdxvgn7Uyn_1f6bqkX7lHnmINQEAHfDgDvHkYKg950wdJ6bXpyY9BKiRJjiGg8e2NcudH38XORpRBR8jKasr3JeheCp_YlCYLedaRjRzp2pKXedRQHvr7O_2I_lBL1072-CoPz_2gyrhRV8QxbhZRA</recordid><startdate>19950901</startdate><enddate>19950901</enddate><creator>Diamond, Michael S.</creator><creator>Alon, Ronen</creator><creator>Parkos, Charles A.</creator><creator>Quinn, Mark T.</creator><creator>Springer, Timothy A.</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19950901</creationdate><title>Heparin Is an Adhesive Ligand for the Leukocyte Integrin Mac-1 (CD11b/CD18)</title><author>Diamond, Michael S. ; Alon, Ronen ; Parkos, Charles A. ; Quinn, Mark T. ; Springer, Timothy A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c499t-e1bfe2d1697e6dc56f754dabdf5ceac0f2661bc880654c00b821996eac47a5043</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Adhesives</topic><topic>Animals</topic><topic>Cell Adhesion</topic><topic>Cellular biology</topic><topic>CHO Cells</topic><topic>Circulatory system</topic><topic>Cricetinae</topic><topic>Endothelial cells</topic><topic>Fibrosis</topic><topic>Heparin</topic><topic>Heparin - metabolism</topic><topic>Humans</topic><topic>Integrins</topic><topic>Leukocytes</topic><topic>Ligands</topic><topic>Macrophage-1 Antigen - metabolism</topic><topic>Middle Aged</topic><topic>Neutrophils</topic><topic>Neutrophils - metabolism</topic><topic>Sensitivity and Specificity</topic><topic>Shear stress</topic><topic>Sulfates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Diamond, Michael S.</creatorcontrib><creatorcontrib>Alon, Ronen</creatorcontrib><creatorcontrib>Parkos, Charles A.</creatorcontrib><creatorcontrib>Quinn, Mark T.</creatorcontrib><creatorcontrib>Springer, Timothy A.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Diamond, Michael S.</au><au>Alon, Ronen</au><au>Parkos, Charles A.</au><au>Quinn, Mark T.</au><au>Springer, Timothy A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heparin Is an Adhesive Ligand for the Leukocyte Integrin Mac-1 (CD11b/CD18)</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1995-09-01</date><risdate>1995</risdate><volume>130</volume><issue>6</issue><spage>1473</spage><epage>1482</epage><pages>1473-1482</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>Previous studies have demonstrated that the leukocyte integrin Mac-1 adheres to several cell surface and soluble ligands including intercellular adhesion molecule-1, fibrinogen, iC3b, and factor X. However, experiments with Mac-1-expressing transfectants, purified Mac-1, and mAbs to Mac-1 indicate the existence of additional ligands. In this paper, we demonstrate a direct interaction between Mac-1 and heparan sulfate glycans. Heparin affinity resins immunoprecipitate Mac-1, and neutrophils and transfectant cells that express Mac-1 bind to heparin and heparan sulfate, but not to other sulfated glycosaminoglycans. Inhibition studies with mAbs and chemically modified forms of heparin suggest the I domain as a recognition site on Mac-1 for heparin, and suggest that either N- or O-sulfation is sufficient for heparin to bind efficiently to Mac-1. Under conditions of continuous flow in which heparins and E-selectin are cosubstrates, neutrophils tether to E-selectin and form firm adhesions through a Mac-1-heparin interaction.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>7559767</pmid><doi>10.1083/jcb.130.6.1473</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0021-9525 |
ispartof | The Journal of cell biology, 1995-09, Vol.130 (6), p.1473-1482 |
issn | 0021-9525 1540-8140 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2120570 |
source | JSTOR Archival Journals and Primary Sources Collection |
subjects | Adhesives Animals Cell Adhesion Cellular biology CHO Cells Circulatory system Cricetinae Endothelial cells Fibrosis Heparin Heparin - metabolism Humans Integrins Leukocytes Ligands Macrophage-1 Antigen - metabolism Middle Aged Neutrophils Neutrophils - metabolism Sensitivity and Specificity Shear stress Sulfates |
title | Heparin Is an Adhesive Ligand for the Leukocyte Integrin Mac-1 (CD11b/CD18) |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-26T00%3A28%3A19IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Heparin%20Is%20an%20Adhesive%20Ligand%20for%20the%20Leukocyte%20Integrin%20Mac-1%20(CD11b/CD18)&rft.jtitle=The%20Journal%20of%20cell%20biology&rft.au=Diamond,%20Michael%20S.&rft.date=1995-09-01&rft.volume=130&rft.issue=6&rft.spage=1473&rft.epage=1482&rft.pages=1473-1482&rft.issn=0021-9525&rft.eissn=1540-8140&rft.coden=JCLBA3&rft_id=info:doi/10.1083/jcb.130.6.1473&rft_dat=%3Cjstor_pubme%3E1617159%3C/jstor_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c499t-e1bfe2d1697e6dc56f754dabdf5ceac0f2661bc880654c00b821996eac47a5043%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=217111648&rft_id=info:pmid/7559767&rft_jstor_id=1617159&rfr_iscdi=true |