The effect of Ca2+, Cd2+ and Ni2+ on detergent-permeabilized vascular smooth muscle from the shark, Squalus acanthias

We examined the effect of Ca2+, Cd2+, or Ni2+ on vascular smooth muscle intracellular proteins involved in contraction, using rings of detergent-permeabilized aortae from the spiny dogfish, Squalus acanthias. Addition of Ca2+ stimulated contraction of the vascular smooth muscle, and permeabilization...

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Main Authors: DH Evans, E Chipouras, T Toop, John Donald
Format: Article in Journal/Newspaper
Language:unknown
Published: 1993
Subjects:
Online Access:http://hdl.handle.net/10536/DRO/DU:30094419
https://figshare.com/articles/journal_contribution/The_effect_of_Ca2_Cd2_and_Ni2_on_detergent-permeabilized_vascular_smooth_muscle_from_the_shark_Squalus_acanthias/20868067
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spelling ftdeakinunifig:oai:figshare.com:article/20868067 2024-06-23T07:57:32+00:00 The effect of Ca2+, Cd2+ and Ni2+ on detergent-permeabilized vascular smooth muscle from the shark, Squalus acanthias DH Evans E Chipouras T Toop John Donald 1993-10-25T00:00:00Z http://hdl.handle.net/10536/DRO/DU:30094419 https://figshare.com/articles/journal_contribution/The_effect_of_Ca2_Cd2_and_Ni2_on_detergent-permeabilized_vascular_smooth_muscle_from_the_shark_Squalus_acanthias/20868067 unknown http://hdl.handle.net/10536/DRO/DU:30094419 https://figshare.com/articles/journal_contribution/The_effect_of_Ca2_Cd2_and_Ni2_on_detergent-permeabilized_vascular_smooth_muscle_from_the_shark_Squalus_acanthias/20868067 All Rights Reserved Pharmacology and pharmaceutical sciences not elsewhere classified Animals Aorta Cadmium Calcium In Vitro Techniques Nickel Octoxynol Sharks Vascular smooth muscle Detergent-permeabilized Text Journal contribution 1993 ftdeakinunifig 2024-06-06T02:00:31Z We examined the effect of Ca2+, Cd2+, or Ni2+ on vascular smooth muscle intracellular proteins involved in contraction, using rings of detergent-permeabilized aortae from the spiny dogfish, Squalus acanthias. Addition of Ca2+ stimulated contraction of the vascular smooth muscle, and permeabilization by treatment with Triton X-100 increased the sensitivity to Ca2+ nearly 5 log units, demonstrating that this protocol left contractile and regulatory proteins intact. Addition of 1 microM calmodulin did not increase the sensitivity of the rings to Ca2+, suggesting that this preparation is not leaky to this regulatory protein. Neither Cd2+ nor Ni2+ stimulated contraction of permeabilized rings demonstrating that the previously-described contractile action of these heavy metals is not mediated by direct stimulation of intracellular proteins, rather by interaction with sarcolemmal proteins. Article in Journal/Newspaper spiny dogfish Squalus acanthias DRO - Deakin Research Online Triton ENVELOPE(-55.615,-55.615,49.517,49.517)
institution Open Polar
collection DRO - Deakin Research Online
op_collection_id ftdeakinunifig
language unknown
topic Pharmacology and pharmaceutical sciences not elsewhere classified
Animals
Aorta
Cadmium
Calcium
In Vitro Techniques
Nickel
Octoxynol
Sharks
Vascular smooth muscle
Detergent-permeabilized
spellingShingle Pharmacology and pharmaceutical sciences not elsewhere classified
Animals
Aorta
Cadmium
Calcium
In Vitro Techniques
Nickel
Octoxynol
Sharks
Vascular smooth muscle
Detergent-permeabilized
DH Evans
E Chipouras
T Toop
John Donald
The effect of Ca2+, Cd2+ and Ni2+ on detergent-permeabilized vascular smooth muscle from the shark, Squalus acanthias
topic_facet Pharmacology and pharmaceutical sciences not elsewhere classified
Animals
Aorta
Cadmium
Calcium
In Vitro Techniques
Nickel
Octoxynol
Sharks
Vascular smooth muscle
Detergent-permeabilized
description We examined the effect of Ca2+, Cd2+, or Ni2+ on vascular smooth muscle intracellular proteins involved in contraction, using rings of detergent-permeabilized aortae from the spiny dogfish, Squalus acanthias. Addition of Ca2+ stimulated contraction of the vascular smooth muscle, and permeabilization by treatment with Triton X-100 increased the sensitivity to Ca2+ nearly 5 log units, demonstrating that this protocol left contractile and regulatory proteins intact. Addition of 1 microM calmodulin did not increase the sensitivity of the rings to Ca2+, suggesting that this preparation is not leaky to this regulatory protein. Neither Cd2+ nor Ni2+ stimulated contraction of permeabilized rings demonstrating that the previously-described contractile action of these heavy metals is not mediated by direct stimulation of intracellular proteins, rather by interaction with sarcolemmal proteins.
format Article in Journal/Newspaper
author DH Evans
E Chipouras
T Toop
John Donald
author_facet DH Evans
E Chipouras
T Toop
John Donald
author_sort DH Evans
title The effect of Ca2+, Cd2+ and Ni2+ on detergent-permeabilized vascular smooth muscle from the shark, Squalus acanthias
title_short The effect of Ca2+, Cd2+ and Ni2+ on detergent-permeabilized vascular smooth muscle from the shark, Squalus acanthias
title_full The effect of Ca2+, Cd2+ and Ni2+ on detergent-permeabilized vascular smooth muscle from the shark, Squalus acanthias
title_fullStr The effect of Ca2+, Cd2+ and Ni2+ on detergent-permeabilized vascular smooth muscle from the shark, Squalus acanthias
title_full_unstemmed The effect of Ca2+, Cd2+ and Ni2+ on detergent-permeabilized vascular smooth muscle from the shark, Squalus acanthias
title_sort effect of ca2+, cd2+ and ni2+ on detergent-permeabilized vascular smooth muscle from the shark, squalus acanthias
publishDate 1993
url http://hdl.handle.net/10536/DRO/DU:30094419
https://figshare.com/articles/journal_contribution/The_effect_of_Ca2_Cd2_and_Ni2_on_detergent-permeabilized_vascular_smooth_muscle_from_the_shark_Squalus_acanthias/20868067
long_lat ENVELOPE(-55.615,-55.615,49.517,49.517)
geographic Triton
geographic_facet Triton
genre spiny dogfish
Squalus acanthias
genre_facet spiny dogfish
Squalus acanthias
op_relation http://hdl.handle.net/10536/DRO/DU:30094419
https://figshare.com/articles/journal_contribution/The_effect_of_Ca2_Cd2_and_Ni2_on_detergent-permeabilized_vascular_smooth_muscle_from_the_shark_Squalus_acanthias/20868067
op_rights All Rights Reserved
_version_ 1802651222308552704