Loading…

Phosphorylation of the Small Heat Shock-related Protein, HSP20, in Vascular Smooth Muscles Is Associated with Changes in the Macromolecular Associations of HSP20

Cyclic nucleotide-dependent vasorelaxation is associated with increases in the phosphorylation of a small heat shock-related protein, HSP20. We hypothesized that phosphorylation of HSP20 in vascular smooth muscles is associated with alterations in the macromolecular associations of HSP20. Treatment...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1999-03, Vol.274 (10), p.6324-6329
Main Authors: Brophy, C M, Dickinson, M, Woodrum, D
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-c362t-d102b0182861b366f9bf601cf1f00c7da41c8e8e357643ae405c82adeeff4edf3
cites cdi_FETCH-LOGICAL-c362t-d102b0182861b366f9bf601cf1f00c7da41c8e8e357643ae405c82adeeff4edf3
container_end_page 6329
container_issue 10
container_start_page 6324
container_title The Journal of biological chemistry
container_volume 274
creator Brophy, C M
Dickinson, M
Woodrum, D
description Cyclic nucleotide-dependent vasorelaxation is associated with increases in the phosphorylation of a small heat shock-related protein, HSP20. We hypothesized that phosphorylation of HSP20 in vascular smooth muscles is associated with alterations in the macromolecular associations of HSP20. Treatment of bovine carotid artery smooth muscles with the phosphodiesterase inhibitor, 3-isobutyl-1-methylxanthine, and the adenylate cyclase activator, forskolin, led to increases in the phosphorylation of HSP20 and dissociation of macromolecular aggregates of HSP20. However, 3-isobutyl-1-methylxanthine and forskolin treatment of a muscle that is uniquely refractory to cyclic nucleotide-dependent vasorelaxation, human umbilical artery smooth muscle, did not result in increases in the phosphorylation of HSP20 or to dissociation of macromolecular aggregates. HSP20 can be phosphorylated in vitro by the catalytic subunit of cAMP-dependent protein kinase (PKA) in both carotid and umbilical arteries and this phosphorylation of HSP20 is associated with dissociation of macromolecular aggregates of HSP20. Activation of cyclic nucleotide-dependent signaling pathways does not lead to changes in the macromolecular associations of another small heat shock protein, HSP27. Interestingly, the myosin light chains (MLC 20 ) are in similar fractions as the HSP20, and phosphorylation of HSP20 is associated with changes in the macromolecular associations of MLC 20 . These data suggest that increases in the phosphorylation of HSP20 are associated with changes in the macromolecular associations of HSP20. HSP20 may regulate vasorelaxation through a direct interaction with specific contractile regulatory proteins.
doi_str_mv 10.1074/jbc.274.10.6324
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_69593666</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>69593666</sourcerecordid><originalsourceid>FETCH-LOGICAL-c362t-d102b0182861b366f9bf601cf1f00c7da41c8e8e357643ae405c82adeeff4edf3</originalsourceid><addsrcrecordid>eNpVkc1q3DAUhUVpaSZp190VQSGreKIfW7aXYWg6gYQOTBuyM7J8FSmVralkE_I4fdPIcQqtNuJyv3PugYPQJ0rWlJT5-UOr1qzM07AWnOVv0IqSime8oHdv0YoQRrOaFdUROo7xgaSX1_Q9OqKE8LJkdIX-7IyPB-PDk5Oj9QP2Go8G8L6XzuEtyBHvjVe_sgAJgA7vgh_BDmd4u98xcobtgG9lVJOTIYm8Hw2-maJyEPFVxBcxemVfhI82rTZGDvdplVTzlRupgu-9g0X_l0454hzk5cQH9E5LF-Hj63-Cfl5-_bHZZtffv11tLq4zxQUbs44S1hJasUrQlguh61YLQpWmmhBVdjKnqoIKeFGKnEvISaEqJjsArXPoND9Bp4vvIfjfE8Sx6W1U4JwcwE-xEXVRJ1-RwPMFTNljDKCbQ7C9DE8NJc3cSpNaaVIr8zy3khSfX62ntofuH36pIQFfFsDYe_NoAzSt9cpA_5_NMyO7lYs</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>69593666</pqid></control><display><type>article</type><title>Phosphorylation of the Small Heat Shock-related Protein, HSP20, in Vascular Smooth Muscles Is Associated with Changes in the Macromolecular Associations of HSP20</title><source>ScienceDirect</source><creator>Brophy, C M ; Dickinson, M ; Woodrum, D</creator><creatorcontrib>Brophy, C M ; Dickinson, M ; Woodrum, D</creatorcontrib><description>Cyclic nucleotide-dependent vasorelaxation is associated with increases in the phosphorylation of a small heat shock-related protein, HSP20. We hypothesized that phosphorylation of HSP20 in vascular smooth muscles is associated with alterations in the macromolecular associations of HSP20. Treatment of bovine carotid artery smooth muscles with the phosphodiesterase inhibitor, 3-isobutyl-1-methylxanthine, and the adenylate cyclase activator, forskolin, led to increases in the phosphorylation of HSP20 and dissociation of macromolecular aggregates of HSP20. However, 3-isobutyl-1-methylxanthine and forskolin treatment of a muscle that is uniquely refractory to cyclic nucleotide-dependent vasorelaxation, human umbilical artery smooth muscle, did not result in increases in the phosphorylation of HSP20 or to dissociation of macromolecular aggregates. HSP20 can be phosphorylated in vitro by the catalytic subunit of cAMP-dependent protein kinase (PKA) in both carotid and umbilical arteries and this phosphorylation of HSP20 is associated with dissociation of macromolecular aggregates of HSP20. Activation of cyclic nucleotide-dependent signaling pathways does not lead to changes in the macromolecular associations of another small heat shock protein, HSP27. Interestingly, the myosin light chains (MLC 20 ) are in similar fractions as the HSP20, and phosphorylation of HSP20 is associated with changes in the macromolecular associations of MLC 20 . These data suggest that increases in the phosphorylation of HSP20 are associated with changes in the macromolecular associations of HSP20. HSP20 may regulate vasorelaxation through a direct interaction with specific contractile regulatory proteins.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.274.10.6324</identifier><identifier>PMID: 10037721</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>1-Methyl-3-isobutylxanthine - pharmacology ; Animals ; Cattle ; Colforsin - pharmacology ; Heat-Shock Proteins - drug effects ; Heat-Shock Proteins - metabolism ; HSP20 Heat-Shock Proteins ; Humans ; Muscle, Smooth, Vascular - metabolism ; Phosphodiesterase Inhibitors - pharmacology ; Phosphoproteins - drug effects ; Phosphoproteins - metabolism ; Phosphorylation - drug effects</subject><ispartof>The Journal of biological chemistry, 1999-03, Vol.274 (10), p.6324-6329</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c362t-d102b0182861b366f9bf601cf1f00c7da41c8e8e357643ae405c82adeeff4edf3</citedby><cites>FETCH-LOGICAL-c362t-d102b0182861b366f9bf601cf1f00c7da41c8e8e357643ae405c82adeeff4edf3</cites></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/10037721$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brophy, C M</creatorcontrib><creatorcontrib>Dickinson, M</creatorcontrib><creatorcontrib>Woodrum, D</creatorcontrib><title>Phosphorylation of the Small Heat Shock-related Protein, HSP20, in Vascular Smooth Muscles Is Associated with Changes in the Macromolecular Associations of HSP20</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Cyclic nucleotide-dependent vasorelaxation is associated with increases in the phosphorylation of a small heat shock-related protein, HSP20. We hypothesized that phosphorylation of HSP20 in vascular smooth muscles is associated with alterations in the macromolecular associations of HSP20. Treatment of bovine carotid artery smooth muscles with the phosphodiesterase inhibitor, 3-isobutyl-1-methylxanthine, and the adenylate cyclase activator, forskolin, led to increases in the phosphorylation of HSP20 and dissociation of macromolecular aggregates of HSP20. However, 3-isobutyl-1-methylxanthine and forskolin treatment of a muscle that is uniquely refractory to cyclic nucleotide-dependent vasorelaxation, human umbilical artery smooth muscle, did not result in increases in the phosphorylation of HSP20 or to dissociation of macromolecular aggregates. HSP20 can be phosphorylated in vitro by the catalytic subunit of cAMP-dependent protein kinase (PKA) in both carotid and umbilical arteries and this phosphorylation of HSP20 is associated with dissociation of macromolecular aggregates of HSP20. Activation of cyclic nucleotide-dependent signaling pathways does not lead to changes in the macromolecular associations of another small heat shock protein, HSP27. Interestingly, the myosin light chains (MLC 20 ) are in similar fractions as the HSP20, and phosphorylation of HSP20 is associated with changes in the macromolecular associations of MLC 20 . These data suggest that increases in the phosphorylation of HSP20 are associated with changes in the macromolecular associations of HSP20. HSP20 may regulate vasorelaxation through a direct interaction with specific contractile regulatory proteins.</description><subject>1-Methyl-3-isobutylxanthine - pharmacology</subject><subject>Animals</subject><subject>Cattle</subject><subject>Colforsin - pharmacology</subject><subject>Heat-Shock Proteins - drug effects</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>HSP20 Heat-Shock Proteins</subject><subject>Humans</subject><subject>Muscle, Smooth, Vascular - metabolism</subject><subject>Phosphodiesterase Inhibitors - pharmacology</subject><subject>Phosphoproteins - drug effects</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation - drug effects</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNpVkc1q3DAUhUVpaSZp190VQSGreKIfW7aXYWg6gYQOTBuyM7J8FSmVralkE_I4fdPIcQqtNuJyv3PugYPQJ0rWlJT5-UOr1qzM07AWnOVv0IqSime8oHdv0YoQRrOaFdUROo7xgaSX1_Q9OqKE8LJkdIX-7IyPB-PDk5Oj9QP2Go8G8L6XzuEtyBHvjVe_sgAJgA7vgh_BDmd4u98xcobtgG9lVJOTIYm8Hw2-maJyEPFVxBcxemVfhI82rTZGDvdplVTzlRupgu-9g0X_l0454hzk5cQH9E5LF-Hj63-Cfl5-_bHZZtffv11tLq4zxQUbs44S1hJasUrQlguh61YLQpWmmhBVdjKnqoIKeFGKnEvISaEqJjsArXPoND9Bp4vvIfjfE8Sx6W1U4JwcwE-xEXVRJ1-RwPMFTNljDKCbQ7C9DE8NJc3cSpNaaVIr8zy3khSfX62ntofuH36pIQFfFsDYe_NoAzSt9cpA_5_NMyO7lYs</recordid><startdate>19990305</startdate><enddate>19990305</enddate><creator>Brophy, C M</creator><creator>Dickinson, M</creator><creator>Woodrum, D</creator><general>American Society for Biochemistry and Molecular Biology</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>7X8</scope></search><sort><creationdate>19990305</creationdate><title>Phosphorylation of the Small Heat Shock-related Protein, HSP20, in Vascular Smooth Muscles Is Associated with Changes in the Macromolecular Associations of HSP20</title><author>Brophy, C M ; Dickinson, M ; Woodrum, D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c362t-d102b0182861b366f9bf601cf1f00c7da41c8e8e357643ae405c82adeeff4edf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>1-Methyl-3-isobutylxanthine - pharmacology</topic><topic>Animals</topic><topic>Cattle</topic><topic>Colforsin - pharmacology</topic><topic>Heat-Shock Proteins - drug effects</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>HSP20 Heat-Shock Proteins</topic><topic>Humans</topic><topic>Muscle, Smooth, Vascular - metabolism</topic><topic>Phosphodiesterase Inhibitors - pharmacology</topic><topic>Phosphoproteins - drug effects</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation - drug effects</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brophy, C M</creatorcontrib><creatorcontrib>Dickinson, M</creatorcontrib><creatorcontrib>Woodrum, D</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brophy, C M</au><au>Dickinson, M</au><au>Woodrum, D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation of the Small Heat Shock-related Protein, HSP20, in Vascular Smooth Muscles Is Associated with Changes in the Macromolecular Associations of HSP20</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1999-03-05</date><risdate>1999</risdate><volume>274</volume><issue>10</issue><spage>6324</spage><epage>6329</epage><pages>6324-6329</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Cyclic nucleotide-dependent vasorelaxation is associated with increases in the phosphorylation of a small heat shock-related protein, HSP20. We hypothesized that phosphorylation of HSP20 in vascular smooth muscles is associated with alterations in the macromolecular associations of HSP20. Treatment of bovine carotid artery smooth muscles with the phosphodiesterase inhibitor, 3-isobutyl-1-methylxanthine, and the adenylate cyclase activator, forskolin, led to increases in the phosphorylation of HSP20 and dissociation of macromolecular aggregates of HSP20. However, 3-isobutyl-1-methylxanthine and forskolin treatment of a muscle that is uniquely refractory to cyclic nucleotide-dependent vasorelaxation, human umbilical artery smooth muscle, did not result in increases in the phosphorylation of HSP20 or to dissociation of macromolecular aggregates. HSP20 can be phosphorylated in vitro by the catalytic subunit of cAMP-dependent protein kinase (PKA) in both carotid and umbilical arteries and this phosphorylation of HSP20 is associated with dissociation of macromolecular aggregates of HSP20. Activation of cyclic nucleotide-dependent signaling pathways does not lead to changes in the macromolecular associations of another small heat shock protein, HSP27. Interestingly, the myosin light chains (MLC 20 ) are in similar fractions as the HSP20, and phosphorylation of HSP20 is associated with changes in the macromolecular associations of MLC 20 . These data suggest that increases in the phosphorylation of HSP20 are associated with changes in the macromolecular associations of HSP20. HSP20 may regulate vasorelaxation through a direct interaction with specific contractile regulatory proteins.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>10037721</pmid><doi>10.1074/jbc.274.10.6324</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0021-9258
ispartof The Journal of biological chemistry, 1999-03, Vol.274 (10), p.6324-6329
issn 0021-9258
1083-351X
language eng
recordid cdi_proquest_miscellaneous_69593666
source ScienceDirect
subjects 1-Methyl-3-isobutylxanthine - pharmacology
Animals
Cattle
Colforsin - pharmacology
Heat-Shock Proteins - drug effects
Heat-Shock Proteins - metabolism
HSP20 Heat-Shock Proteins
Humans
Muscle, Smooth, Vascular - metabolism
Phosphodiesterase Inhibitors - pharmacology
Phosphoproteins - drug effects
Phosphoproteins - metabolism
Phosphorylation - drug effects
title Phosphorylation of the Small Heat Shock-related Protein, HSP20, in Vascular Smooth Muscles Is Associated with Changes in the Macromolecular Associations of HSP20
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T20%3A40%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=Phosphorylation%20of%20the%20Small%20Heat%20Shock-related%20Protein,%20HSP20,%20in%20Vascular%20Smooth%20Muscles%20Is%20Associated%20with%20Changes%20in%20the%20Macromolecular%20Associations%20of%20HSP20&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Brophy,%20C%20M&rft.date=1999-03-05&rft.volume=274&rft.issue=10&rft.spage=6324&rft.epage=6329&rft.pages=6324-6329&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.274.10.6324&rft_dat=%3Cproquest_cross%3E69593666%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c362t-d102b0182861b366f9bf601cf1f00c7da41c8e8e357643ae405c82adeeff4edf3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=69593666&rft_id=info:pmid/10037721&rfr_iscdi=true