Loading…
Fibrin exposure triggers αIIbβ3‐independent platelet aggregate formation, ADAM10 activity and glycoprotein VI shedding in a charge‐dependent manner
Background Collagen and fibrin engagement and activation of glycoprotein (GP) VI induces proteolytic cleavage of the GPVI ectodomain generating shed soluble GPVI (sGPVI). Collagen‐mediated GPVI shedding requires intracellular signalling to release the sGPVI, mediated by A Disintegrin And Metalloprot...
Saved in:
Published in: | Journal of thrombosis and haemostasis 2020-06, Vol.18 (6), p.1447-1458 |
---|---|
Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites 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-c3037-c2384c5d87fc08c38f850bd06d9dd117e036831270a92fc7acd7cad28c6654583 |
---|---|
cites | cdi_FETCH-LOGICAL-c3037-c2384c5d87fc08c38f850bd06d9dd117e036831270a92fc7acd7cad28c6654583 |
container_end_page | 1458 |
container_issue | 6 |
container_start_page | 1447 |
container_title | Journal of thrombosis and haemostasis |
container_volume | 18 |
creator | Montague, Samantha J. Hicks, Sarah M. Lee, Christine S‐M. Coupland, Lucy A. Parish, Christopher R. Lee, Woei M. Andrews, Robert K. Gardiner, Elizabeth E. |
description | Background
Collagen and fibrin engagement and activation of glycoprotein (GP) VI induces proteolytic cleavage of the GPVI ectodomain generating shed soluble GPVI (sGPVI). Collagen‐mediated GPVI shedding requires intracellular signalling to release the sGPVI, mediated by A Disintegrin And Metalloproteinase 10 (ADAM10); however, the precise mechanism by which fibrin induces GPVI shedding remains elusive. Plasma sGPVI levels are elevated in patients with coagulopathies, sepsis, or inflammation and can predict onset of sepsis and sepsis‐related mortality; therefore, it is clinically important to understand the mechanisms of GPVI shedding under conditions of minimal collagen exposure.
Objectives
Our aim was to characterize mechanisms by which fibrin‐GPVI interactions trigger GPVI shedding.
Methods
Platelet aggregometry, sGPVI ELISA, and an ADAM10 fluorescence resonance energy transfer assay were used to measure fibrin‐mediated platelet responses.
Results
Fibrin induced αIIbβ3‐independent washed platelet aggregate formation, GPVI shedding, and increased ADAM10 activity, all of which were insensitive to pre‐treatment with inhibitors of Src family kinases but were divalent cation‐ and metalloproteinase‐dependent. In contrast, treatment of washed platelets with other GPVI ligands, collagen, and collagen‐related peptide caused αIIbβ3‐dependent platelet aggregation and GPVI release but did not increase constitutive ADAM10 activity.
Conclusions
Fibrin engages GPVI in a manner that differs from other GPVI ligands. Inclusion of polyanionic molecules disrupted fibrin‐induced platelet aggregate formation and sGPVI release, suggesting that electrostatic charge may play a role in fibrin/GPVI engagement. It may be feasible to exploit this property and specifically disrupt GPVI/fibrin interactions whilst sparing GPVI/collagen engagement.Fibrin engages GPVI in a manner that differs from other GPVI ligands. Inclusion of polyanionic molecules disrupted fibrin‐induced platelet aggregate formation and sGPVI release, suggesting that electrostatic charge may play a role in fibrin/GPVI engagement. It may be feasible to exploit this property and specifically disrupt GPVI/fibrin interactions whilst sparing GPVI/collagen engagement. |
doi_str_mv | 10.1111/jth.14797 |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2381629637</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2381629637</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3037-c2384c5d87fc08c38f850bd06d9dd117e036831270a92fc7acd7cad28c6654583</originalsourceid><addsrcrecordid>eNp1kUFu1DAUhq0K1Ja2i16gssQGJKa14yS2l6NC6aAiNoWt5bFfMh4lTrAdYHYcgS3HgIP0EJwEw7RFQqoXtp_06fuf9CN0TMkpzedsnVantOSS76B9WjEx44LVj-7-krE99CTGNSFUVgXZRXusoFLIiu-j7xduGZzH8GUc4hQAp-DaFkLENz8Wi-XNT_br6zfnLYyQL5_w2OkEHSSs2zZAmwfcDKHXyQ3-BZ6_nL-lBGuT3CeXNlh7i9tuY4YxDAlyzocFjiuw1vkW51Fjs9KhhRzyL6LX3kM4RI8b3UU4un0P0PuLV9fnl7Ord68X5_OrmWGE8ZkpmChNZQVvDBGGiUZUZGlJbaW1lHIgrBaMFpxoWTSGa2O50bYQpq6rshLsAD3bevOKHyeISfUuGug67WGYosp-WheyZjyjT_9D18MUfN5OFSWRlDAqy0w931ImDDEGaNQYXK_DRlGi_vSlcl_qb1-ZPbk1Tsse7D15V1AGzrbAZ9fB5mGTenN9uVX-Bp5No9g</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2409103194</pqid></control><display><type>article</type><title>Fibrin exposure triggers αIIbβ3‐independent platelet aggregate formation, ADAM10 activity and glycoprotein VI shedding in a charge‐dependent manner</title><source>EZB Electronic Journals Library</source><creator>Montague, Samantha J. ; Hicks, Sarah M. ; Lee, Christine S‐M. ; Coupland, Lucy A. ; Parish, Christopher R. ; Lee, Woei M. ; Andrews, Robert K. ; Gardiner, Elizabeth E.</creator><creatorcontrib>Montague, Samantha J. ; Hicks, Sarah M. ; Lee, Christine S‐M. ; Coupland, Lucy A. ; Parish, Christopher R. ; Lee, Woei M. ; Andrews, Robert K. ; Gardiner, Elizabeth E.</creatorcontrib><description>Background
Collagen and fibrin engagement and activation of glycoprotein (GP) VI induces proteolytic cleavage of the GPVI ectodomain generating shed soluble GPVI (sGPVI). Collagen‐mediated GPVI shedding requires intracellular signalling to release the sGPVI, mediated by A Disintegrin And Metalloproteinase 10 (ADAM10); however, the precise mechanism by which fibrin induces GPVI shedding remains elusive. Plasma sGPVI levels are elevated in patients with coagulopathies, sepsis, or inflammation and can predict onset of sepsis and sepsis‐related mortality; therefore, it is clinically important to understand the mechanisms of GPVI shedding under conditions of minimal collagen exposure.
Objectives
Our aim was to characterize mechanisms by which fibrin‐GPVI interactions trigger GPVI shedding.
Methods
Platelet aggregometry, sGPVI ELISA, and an ADAM10 fluorescence resonance energy transfer assay were used to measure fibrin‐mediated platelet responses.
Results
Fibrin induced αIIbβ3‐independent washed platelet aggregate formation, GPVI shedding, and increased ADAM10 activity, all of which were insensitive to pre‐treatment with inhibitors of Src family kinases but were divalent cation‐ and metalloproteinase‐dependent. In contrast, treatment of washed platelets with other GPVI ligands, collagen, and collagen‐related peptide caused αIIbβ3‐dependent platelet aggregation and GPVI release but did not increase constitutive ADAM10 activity.
Conclusions
Fibrin engages GPVI in a manner that differs from other GPVI ligands. Inclusion of polyanionic molecules disrupted fibrin‐induced platelet aggregate formation and sGPVI release, suggesting that electrostatic charge may play a role in fibrin/GPVI engagement. It may be feasible to exploit this property and specifically disrupt GPVI/fibrin interactions whilst sparing GPVI/collagen engagement.Fibrin engages GPVI in a manner that differs from other GPVI ligands. Inclusion of polyanionic molecules disrupted fibrin‐induced platelet aggregate formation and sGPVI release, suggesting that electrostatic charge may play a role in fibrin/GPVI engagement. It may be feasible to exploit this property and specifically disrupt GPVI/fibrin interactions whilst sparing GPVI/collagen engagement.</description><identifier>ISSN: 1538-7933</identifier><identifier>ISSN: 1538-7836</identifier><identifier>EISSN: 1538-7836</identifier><identifier>DOI: 10.1111/jth.14797</identifier><identifier>PMID: 32198957</identifier><language>eng</language><publisher>England: Elsevier Limited</publisher><subject>ADAM10 ; ADAM10 Protein ; Amyloid Precursor Protein Secretases ; Blood Platelets ; Collagen ; Enzyme-linked immunosorbent assay ; Fibrin ; Fluorescence resonance energy transfer ; Glycoprotein VI ; Glycoproteins ; GPVI ; Humans ; Intracellular signalling ; Ligands ; Membrane Proteins ; Platelet Aggregation ; Platelet Glycoprotein GPIIb-IIIa Complex ; Platelet Membrane Glycoproteins ; Proteolysis ; receptor shedding ; Sepsis ; thrombosis</subject><ispartof>Journal of thrombosis and haemostasis, 2020-06, Vol.18 (6), p.1447-1458</ispartof><rights>2020 International Society on Thrombosis and Haemostasis</rights><rights>2020 International Society on Thrombosis and Haemostasis.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3037-c2384c5d87fc08c38f850bd06d9dd117e036831270a92fc7acd7cad28c6654583</citedby><cites>FETCH-LOGICAL-c3037-c2384c5d87fc08c38f850bd06d9dd117e036831270a92fc7acd7cad28c6654583</cites><orcidid>0000-0002-3912-6095 ; 0000-0001-9453-9688 ; 0000-0001-7740-0430 ; 0000-0002-3851-9364 ; 0000-0001-9577-8082 ; 0000-0002-8934-3901 ; 0000-0002-8912-9534 ; 0000-0001-5712-124X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32198957$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Montague, Samantha J.</creatorcontrib><creatorcontrib>Hicks, Sarah M.</creatorcontrib><creatorcontrib>Lee, Christine S‐M.</creatorcontrib><creatorcontrib>Coupland, Lucy A.</creatorcontrib><creatorcontrib>Parish, Christopher R.</creatorcontrib><creatorcontrib>Lee, Woei M.</creatorcontrib><creatorcontrib>Andrews, Robert K.</creatorcontrib><creatorcontrib>Gardiner, Elizabeth E.</creatorcontrib><title>Fibrin exposure triggers αIIbβ3‐independent platelet aggregate formation, ADAM10 activity and glycoprotein VI shedding in a charge‐dependent manner</title><title>Journal of thrombosis and haemostasis</title><addtitle>J Thromb Haemost</addtitle><description>Background
Collagen and fibrin engagement and activation of glycoprotein (GP) VI induces proteolytic cleavage of the GPVI ectodomain generating shed soluble GPVI (sGPVI). Collagen‐mediated GPVI shedding requires intracellular signalling to release the sGPVI, mediated by A Disintegrin And Metalloproteinase 10 (ADAM10); however, the precise mechanism by which fibrin induces GPVI shedding remains elusive. Plasma sGPVI levels are elevated in patients with coagulopathies, sepsis, or inflammation and can predict onset of sepsis and sepsis‐related mortality; therefore, it is clinically important to understand the mechanisms of GPVI shedding under conditions of minimal collagen exposure.
Objectives
Our aim was to characterize mechanisms by which fibrin‐GPVI interactions trigger GPVI shedding.
Methods
Platelet aggregometry, sGPVI ELISA, and an ADAM10 fluorescence resonance energy transfer assay were used to measure fibrin‐mediated platelet responses.
Results
Fibrin induced αIIbβ3‐independent washed platelet aggregate formation, GPVI shedding, and increased ADAM10 activity, all of which were insensitive to pre‐treatment with inhibitors of Src family kinases but were divalent cation‐ and metalloproteinase‐dependent. In contrast, treatment of washed platelets with other GPVI ligands, collagen, and collagen‐related peptide caused αIIbβ3‐dependent platelet aggregation and GPVI release but did not increase constitutive ADAM10 activity.
Conclusions
Fibrin engages GPVI in a manner that differs from other GPVI ligands. Inclusion of polyanionic molecules disrupted fibrin‐induced platelet aggregate formation and sGPVI release, suggesting that electrostatic charge may play a role in fibrin/GPVI engagement. It may be feasible to exploit this property and specifically disrupt GPVI/fibrin interactions whilst sparing GPVI/collagen engagement.Fibrin engages GPVI in a manner that differs from other GPVI ligands. Inclusion of polyanionic molecules disrupted fibrin‐induced platelet aggregate formation and sGPVI release, suggesting that electrostatic charge may play a role in fibrin/GPVI engagement. It may be feasible to exploit this property and specifically disrupt GPVI/fibrin interactions whilst sparing GPVI/collagen engagement.</description><subject>ADAM10</subject><subject>ADAM10 Protein</subject><subject>Amyloid Precursor Protein Secretases</subject><subject>Blood Platelets</subject><subject>Collagen</subject><subject>Enzyme-linked immunosorbent assay</subject><subject>Fibrin</subject><subject>Fluorescence resonance energy transfer</subject><subject>Glycoprotein VI</subject><subject>Glycoproteins</subject><subject>GPVI</subject><subject>Humans</subject><subject>Intracellular signalling</subject><subject>Ligands</subject><subject>Membrane Proteins</subject><subject>Platelet Aggregation</subject><subject>Platelet Glycoprotein GPIIb-IIIa Complex</subject><subject>Platelet Membrane Glycoproteins</subject><subject>Proteolysis</subject><subject>receptor shedding</subject><subject>Sepsis</subject><subject>thrombosis</subject><issn>1538-7933</issn><issn>1538-7836</issn><issn>1538-7836</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNp1kUFu1DAUhq0K1Ja2i16gssQGJKa14yS2l6NC6aAiNoWt5bFfMh4lTrAdYHYcgS3HgIP0EJwEw7RFQqoXtp_06fuf9CN0TMkpzedsnVantOSS76B9WjEx44LVj-7-krE99CTGNSFUVgXZRXusoFLIiu-j7xduGZzH8GUc4hQAp-DaFkLENz8Wi-XNT_br6zfnLYyQL5_w2OkEHSSs2zZAmwfcDKHXyQ3-BZ6_nL-lBGuT3CeXNlh7i9tuY4YxDAlyzocFjiuw1vkW51Fjs9KhhRzyL6LX3kM4RI8b3UU4un0P0PuLV9fnl7Ord68X5_OrmWGE8ZkpmChNZQVvDBGGiUZUZGlJbaW1lHIgrBaMFpxoWTSGa2O50bYQpq6rshLsAD3bevOKHyeISfUuGug67WGYosp-WheyZjyjT_9D18MUfN5OFSWRlDAqy0w931ImDDEGaNQYXK_DRlGi_vSlcl_qb1-ZPbk1Tsse7D15V1AGzrbAZ9fB5mGTenN9uVX-Bp5No9g</recordid><startdate>202006</startdate><enddate>202006</enddate><creator>Montague, Samantha J.</creator><creator>Hicks, Sarah M.</creator><creator>Lee, Christine S‐M.</creator><creator>Coupland, Lucy A.</creator><creator>Parish, Christopher R.</creator><creator>Lee, Woei M.</creator><creator>Andrews, Robert K.</creator><creator>Gardiner, Elizabeth E.</creator><general>Elsevier Limited</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>7T5</scope><scope>H94</scope><scope>K9.</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-3912-6095</orcidid><orcidid>https://orcid.org/0000-0001-9453-9688</orcidid><orcidid>https://orcid.org/0000-0001-7740-0430</orcidid><orcidid>https://orcid.org/0000-0002-3851-9364</orcidid><orcidid>https://orcid.org/0000-0001-9577-8082</orcidid><orcidid>https://orcid.org/0000-0002-8934-3901</orcidid><orcidid>https://orcid.org/0000-0002-8912-9534</orcidid><orcidid>https://orcid.org/0000-0001-5712-124X</orcidid></search><sort><creationdate>202006</creationdate><title>Fibrin exposure triggers αIIbβ3‐independent platelet aggregate formation, ADAM10 activity and glycoprotein VI shedding in a charge‐dependent manner</title><author>Montague, Samantha J. ; Hicks, Sarah M. ; Lee, Christine S‐M. ; Coupland, Lucy A. ; Parish, Christopher R. ; Lee, Woei M. ; Andrews, Robert K. ; Gardiner, Elizabeth E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3037-c2384c5d87fc08c38f850bd06d9dd117e036831270a92fc7acd7cad28c6654583</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>ADAM10</topic><topic>ADAM10 Protein</topic><topic>Amyloid Precursor Protein Secretases</topic><topic>Blood Platelets</topic><topic>Collagen</topic><topic>Enzyme-linked immunosorbent assay</topic><topic>Fibrin</topic><topic>Fluorescence resonance energy transfer</topic><topic>Glycoprotein VI</topic><topic>Glycoproteins</topic><topic>GPVI</topic><topic>Humans</topic><topic>Intracellular signalling</topic><topic>Ligands</topic><topic>Membrane Proteins</topic><topic>Platelet Aggregation</topic><topic>Platelet Glycoprotein GPIIb-IIIa Complex</topic><topic>Platelet Membrane Glycoproteins</topic><topic>Proteolysis</topic><topic>receptor shedding</topic><topic>Sepsis</topic><topic>thrombosis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Montague, Samantha J.</creatorcontrib><creatorcontrib>Hicks, Sarah M.</creatorcontrib><creatorcontrib>Lee, Christine S‐M.</creatorcontrib><creatorcontrib>Coupland, Lucy A.</creatorcontrib><creatorcontrib>Parish, Christopher R.</creatorcontrib><creatorcontrib>Lee, Woei M.</creatorcontrib><creatorcontrib>Andrews, Robert K.</creatorcontrib><creatorcontrib>Gardiner, Elizabeth E.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of thrombosis and haemostasis</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Montague, Samantha J.</au><au>Hicks, Sarah M.</au><au>Lee, Christine S‐M.</au><au>Coupland, Lucy A.</au><au>Parish, Christopher R.</au><au>Lee, Woei M.</au><au>Andrews, Robert K.</au><au>Gardiner, Elizabeth E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fibrin exposure triggers αIIbβ3‐independent platelet aggregate formation, ADAM10 activity and glycoprotein VI shedding in a charge‐dependent manner</atitle><jtitle>Journal of thrombosis and haemostasis</jtitle><addtitle>J Thromb Haemost</addtitle><date>2020-06</date><risdate>2020</risdate><volume>18</volume><issue>6</issue><spage>1447</spage><epage>1458</epage><pages>1447-1458</pages><issn>1538-7933</issn><issn>1538-7836</issn><eissn>1538-7836</eissn><abstract>Background
Collagen and fibrin engagement and activation of glycoprotein (GP) VI induces proteolytic cleavage of the GPVI ectodomain generating shed soluble GPVI (sGPVI). Collagen‐mediated GPVI shedding requires intracellular signalling to release the sGPVI, mediated by A Disintegrin And Metalloproteinase 10 (ADAM10); however, the precise mechanism by which fibrin induces GPVI shedding remains elusive. Plasma sGPVI levels are elevated in patients with coagulopathies, sepsis, or inflammation and can predict onset of sepsis and sepsis‐related mortality; therefore, it is clinically important to understand the mechanisms of GPVI shedding under conditions of minimal collagen exposure.
Objectives
Our aim was to characterize mechanisms by which fibrin‐GPVI interactions trigger GPVI shedding.
Methods
Platelet aggregometry, sGPVI ELISA, and an ADAM10 fluorescence resonance energy transfer assay were used to measure fibrin‐mediated platelet responses.
Results
Fibrin induced αIIbβ3‐independent washed platelet aggregate formation, GPVI shedding, and increased ADAM10 activity, all of which were insensitive to pre‐treatment with inhibitors of Src family kinases but were divalent cation‐ and metalloproteinase‐dependent. In contrast, treatment of washed platelets with other GPVI ligands, collagen, and collagen‐related peptide caused αIIbβ3‐dependent platelet aggregation and GPVI release but did not increase constitutive ADAM10 activity.
Conclusions
Fibrin engages GPVI in a manner that differs from other GPVI ligands. Inclusion of polyanionic molecules disrupted fibrin‐induced platelet aggregate formation and sGPVI release, suggesting that electrostatic charge may play a role in fibrin/GPVI engagement. It may be feasible to exploit this property and specifically disrupt GPVI/fibrin interactions whilst sparing GPVI/collagen engagement.Fibrin engages GPVI in a manner that differs from other GPVI ligands. Inclusion of polyanionic molecules disrupted fibrin‐induced platelet aggregate formation and sGPVI release, suggesting that electrostatic charge may play a role in fibrin/GPVI engagement. It may be feasible to exploit this property and specifically disrupt GPVI/fibrin interactions whilst sparing GPVI/collagen engagement.</abstract><cop>England</cop><pub>Elsevier Limited</pub><pmid>32198957</pmid><doi>10.1111/jth.14797</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0002-3912-6095</orcidid><orcidid>https://orcid.org/0000-0001-9453-9688</orcidid><orcidid>https://orcid.org/0000-0001-7740-0430</orcidid><orcidid>https://orcid.org/0000-0002-3851-9364</orcidid><orcidid>https://orcid.org/0000-0001-9577-8082</orcidid><orcidid>https://orcid.org/0000-0002-8934-3901</orcidid><orcidid>https://orcid.org/0000-0002-8912-9534</orcidid><orcidid>https://orcid.org/0000-0001-5712-124X</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1538-7933 |
ispartof | Journal of thrombosis and haemostasis, 2020-06, Vol.18 (6), p.1447-1458 |
issn | 1538-7933 1538-7836 1538-7836 |
language | eng |
recordid | cdi_proquest_miscellaneous_2381629637 |
source | EZB Electronic Journals Library |
subjects | ADAM10 ADAM10 Protein Amyloid Precursor Protein Secretases Blood Platelets Collagen Enzyme-linked immunosorbent assay Fibrin Fluorescence resonance energy transfer Glycoprotein VI Glycoproteins GPVI Humans Intracellular signalling Ligands Membrane Proteins Platelet Aggregation Platelet Glycoprotein GPIIb-IIIa Complex Platelet Membrane Glycoproteins Proteolysis receptor shedding Sepsis thrombosis |
title | Fibrin exposure triggers αIIbβ3‐independent platelet aggregate formation, ADAM10 activity and glycoprotein VI shedding in a charge‐dependent manner |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T20%3A19%3A20IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Fibrin%20exposure%20triggers%20%CE%B1IIb%CE%B23%E2%80%90independent%20platelet%20aggregate%20formation,%20ADAM10%20activity%20and%20glycoprotein%20VI%20shedding%20in%20a%20charge%E2%80%90dependent%20manner&rft.jtitle=Journal%20of%20thrombosis%20and%20haemostasis&rft.au=Montague,%20Samantha%20J.&rft.date=2020-06&rft.volume=18&rft.issue=6&rft.spage=1447&rft.epage=1458&rft.pages=1447-1458&rft.issn=1538-7933&rft.eissn=1538-7836&rft_id=info:doi/10.1111/jth.14797&rft_dat=%3Cproquest_cross%3E2381629637%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c3037-c2384c5d87fc08c38f850bd06d9dd117e036831270a92fc7acd7cad28c6654583%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2409103194&rft_id=info:pmid/32198957&rfr_iscdi=true |