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Article: Subcellular localization of cyclic ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities in porcine airway smooth muscle

TitleSubcellular localization of cyclic ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities in porcine airway smooth muscle
Authors
KeywordsADP-ribosyl cyclase
Airway smooth muscle
Cyclic ADP-ribose
Cyclic ADP-ribose hydrolase
Issue Date2000
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbamcr
Citation
Biochimica Et Biophysica Acta - Molecular Cell Research, 2000, v. 1498 n. 1, p. 64-71 How to Cite?
AbstractRecent studies have provided evidence for a role of cyclic ADP-ribose (cADPR) in the regulation of intracellular calcium in smooth muscles of the intestine, blood vessels and airways. We investigated the presence and subcellular localization of ADP-ribosyl cyclase, the enzyme that catalyzes the conversion of β-NAD+ to cADPR, and cADPR hydrolase, the enzyme that degrades cADPR to ADPR, in tracheal smooth muscle (TSM). Sucrose density fractionation of TSM crude membranes provided evidence that ADP-ribosyl cyclase and cADPR hydrolase activities were associated with a fraction enriched in 5'-nucleotidase activity, a plasma membrane marker enzyme, but not in a fraction enriched in either sarcoplasmic endoplasmic reticulum calcium ATPase or ryanodine receptor channels, both sarcoplasmic reticulum markers. The ADP-ribosyl cyclase and cADPR hydrolase activities comigrated at a molecular weight of approximately 40 kDa on SDS-PAGE. This comigration was confirmed by gel filtration chromatography. Investigation of kinetics yielded K(m) values of 30.4 ± 1.5 and 695.3 ± 171.2 μM and V(max) values of 330.4 ± 90 and 102.8 ± 17.1 nmol/mg/h for ADP-ribosyl cyclase and cADPR hydrolase, respectively. These results suggest a possible role for cADPR as an endogenous modulator of [Ca2+](i) in porcine TSM cells. (C) 2000 Elsevier Science B.V.
Persistent Identifierhttp://hdl.handle.net/10722/132567
ISSN
2015 Impact Factor: 5.128
2015 SCImago Journal Rankings: 3.043
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWhite, TAen_HK
dc.contributor.authorJohnson, Sen_HK
dc.contributor.authorWalseth, TFen_HK
dc.contributor.authorLee, HCen_HK
dc.contributor.authorGraeff, RMen_HK
dc.contributor.authorMunshi, CBen_HK
dc.contributor.authorPrakash, YSen_HK
dc.contributor.authorSieck, GCen_HK
dc.contributor.authorKannan, MSen_HK
dc.date.accessioned2011-03-28T09:26:22Z-
dc.date.available2011-03-28T09:26:22Z-
dc.date.issued2000en_HK
dc.identifier.citationBiochimica Et Biophysica Acta - Molecular Cell Research, 2000, v. 1498 n. 1, p. 64-71en_HK
dc.identifier.issn0167-4889en_HK
dc.identifier.urihttp://hdl.handle.net/10722/132567-
dc.description.abstractRecent studies have provided evidence for a role of cyclic ADP-ribose (cADPR) in the regulation of intracellular calcium in smooth muscles of the intestine, blood vessels and airways. We investigated the presence and subcellular localization of ADP-ribosyl cyclase, the enzyme that catalyzes the conversion of β-NAD+ to cADPR, and cADPR hydrolase, the enzyme that degrades cADPR to ADPR, in tracheal smooth muscle (TSM). Sucrose density fractionation of TSM crude membranes provided evidence that ADP-ribosyl cyclase and cADPR hydrolase activities were associated with a fraction enriched in 5'-nucleotidase activity, a plasma membrane marker enzyme, but not in a fraction enriched in either sarcoplasmic endoplasmic reticulum calcium ATPase or ryanodine receptor channels, both sarcoplasmic reticulum markers. The ADP-ribosyl cyclase and cADPR hydrolase activities comigrated at a molecular weight of approximately 40 kDa on SDS-PAGE. This comigration was confirmed by gel filtration chromatography. Investigation of kinetics yielded K(m) values of 30.4 ± 1.5 and 695.3 ± 171.2 μM and V(max) values of 330.4 ± 90 and 102.8 ± 17.1 nmol/mg/h for ADP-ribosyl cyclase and cADPR hydrolase, respectively. These results suggest a possible role for cADPR as an endogenous modulator of [Ca2+](i) in porcine TSM cells. (C) 2000 Elsevier Science B.V.en_HK
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbamcren_HK
dc.relation.ispartofBiochimica et Biophysica Acta - Molecular Cell Researchen_HK
dc.subjectADP-ribosyl cyclaseen_HK
dc.subjectAirway smooth muscleen_HK
dc.subjectCyclic ADP-riboseen_HK
dc.subjectCyclic ADP-ribose hydrolaseen_HK
dc.titleSubcellular localization of cyclic ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities in porcine airway smooth muscleen_HK
dc.typeArticleen_HK
dc.identifier.emailLee, HC: leehc@hku.hken_HK
dc.identifier.emailGraeff, RM: graeffr@hku.hken_HK
dc.identifier.authorityLee, HC=rp00545en_HK
dc.identifier.authorityGraeff, RM=rp01464en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/S0167-4889(00)00077-Xen_HK
dc.identifier.pmid11042351-
dc.identifier.scopuseid_2-s2.0-0034693160en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034693160&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume1498en_HK
dc.identifier.issue1en_HK
dc.identifier.spage64en_HK
dc.identifier.epage71en_HK
dc.identifier.isiWOS:000165103400006-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridWhite, TA=7402587496en_HK
dc.identifier.scopusauthoridJohnson, S=20534581300en_HK
dc.identifier.scopusauthoridWalseth, TF=7005424273en_HK
dc.identifier.scopusauthoridLee, HC=26642959100en_HK
dc.identifier.scopusauthoridGraeff, RM=7003614053en_HK
dc.identifier.scopusauthoridMunshi, CB=7003972383en_HK
dc.identifier.scopusauthoridPrakash, YS=35554765100en_HK
dc.identifier.scopusauthoridSieck, GC=7102515415en_HK
dc.identifier.scopusauthoridKannan, MS=7006669988en_HK

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