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Difference between revisions of "Konrad 2012 Abstract Bioblast"

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{{Abstract
{{Abstract
|title=Konrad C (2012) Absence of Ca2+-induced mitochondrial permeability transition but presence of bongkrekate-sensitive nucleotide exchange in C. crangon and P. serratus. Mitochondr Physiol Network 17.12.
|title=Konrad C, Kiss G, Torocsik B, Adam-Vizi V, Chinopoulos C (2012) Absence of Ca<sup>2+</sup>-induced mitochondrial permeability transition but presence of bongkrekate-sensitive nucleotide exchange in ''C. crangon'' and ''P. serratus''. Mitochondr Physiol Network 17.12.
|info=[[MiPNet17.12 Bioblast 2012|MiPNet17.12 Bioblast 2012 - Open Access]]
|info=[[MiPNet17.12 Bioblast 2012|MiPNet17.12 Bioblast 2012 - Open Access]]
|authors=Konrad C
|authors=Konrad C, Kiss G, Torocsik B, Adam-Vizi V, Chinopoulos C
|year=2012
|year=2012
|event=[[Bioblast 2012]]
|event=[[Bioblast 2012]]
|abstract=Mitochondria from the embryos of brine shrimp (Artemia franciscana) do not
|abstract=[[File:Konrad C Bioblast 2012.jpg|right|200px|Csaba Konrad]]
undergo Ca2+-induced permeability transition in the presence of a profound Ca2+ uptake
Mitochondria from the embryos of brine shrimp (''Artemia franciscana'') do not
capacity. Furthermore, this crustacean is the only organism known to exhibit bongkrekateinsensitive
undergo Ca<sup>2+</sup>-induced permeability transition in the presence of a profound Ca<sup>2+</sup> uptake
capacity [1]. Furthermore, this crustacean is the only organism known to exhibit bongkrekateinsensitive
mitochondrial adenine nucleotide exchange, prompting the conjecture that
mitochondrial adenine nucleotide exchange, prompting the conjecture that
refractoriness to bongkrekate and absence of Ca2+-induced permeability transition are
refractoriness to bongkrekate and absence of Ca<sup>2+</sup>-induced permeability transition are
somehow related phenomena. Here we report that mitochondria isolated from two other
somehow related phenomena [2]. Here we report that mitochondria isolated from two other
crustaceans, brown shrimp (Crangon crangon) and common prawn (Palaemon serratus)
crustaceans, brown shrimp (''Crangon crangon'') and common prawn (''Palaemon serratus'')
exhibited bongkrekate-sensitive mitochondrial adenine nucleotide transport, but lacked a
exhibited bongkrekate-sensitive mitochondrial adenine nucleotide transport, but lacked a
Ca2+-induced permeability transition. Ca2+ uptake capacity was robust in the absence of
Ca<sup>2+</sup>-induced permeability transition. Ca<sup>2+</sup> uptake capacity was robust in the absence of
adenine nucleotides in both crustaceans, unaffected by either bongkrekate or cyclosporin
adenine nucleotides in both crustaceans, unaffected by either bongkrekate or cyclosporin
A. Transmission electron microscopy images of Ca2+-loaded mitochondria showed
A. Transmission electron microscopy images of Ca<sup>2+</sup>-loaded mitochondria showed
needle-like formations of electron-dense material strikingly similar to those observed in
needle-like formations of electron-dense material strikingly similar to those observed in
mitochondria from the hepatopancreas of blue crab (Callinectes sapidus) and the embryos
mitochondria from the hepatopancreas of blue crab (''Callinectes sapidus'') [3] and the embryos
of Artemia franciscana. Alignment analysis of the partial coding sequences of the adenine
of ''Artemia franciscana'' [2]. Alignment analysis of the partial coding sequences of the adenine
nucleotide translocase (ANT) expressed in Crangon crangon and Palaemon serratus
nucleotide translocase ([[ANT]]) expressed in ''Crangon crangon'' and ''Palaemon serratus'' versus the complete sequence expressed in ''Artemia franciscana'' reappraised the possibility of the 208-214 amino acid region for conferring sensitivity to bongkrekate. However, our findings suggest that the ability to undergo Ca<sup>2+</sup>-induced mitochondrial permeability transition and the sensitivity of adenine nucleotide translocase to bongkrekate
versus the complete sequence expressed in Artemia franciscana reappraised the
possibility of the 208-214 amino acid region for conferring sensitivity to bongkrekate.
However, our findings suggest that the ability to undergo Ca2+-induced mitochondrial
permeability transition and the sensitivity of adenine nucleotide translocase to bongkrekate
are not necessarily related phenomena.
are not necessarily related phenomena.
|mipnetlab=HU Budapest Chinopoulos C, Β 
Β 
|journal=Mitochondr Physiol Network
# [http://www.ncbi.nlm.nih.gov/pubmed/15718386 Menze MA, Hutchinson K, Laborde SM, Hand SC (2005) Mitochondrial permeability transition in the crustacean ''Artemia franciscana'': absence of a calcium-regulated pore in the face of profound calcium storage. Am J Physiol Regul Integr Comp Physiol 289: R68-R76. Open Access]
|articletype=Abstract
# [http://www.ncbi.nlm.nih.gov/pubmed/21205213 Konrad C, Kiss G, Toeroecsik B, Labar JL, Gerencser AA, Mandi M, Adam-Vizi V, Chinopoulos C (2011) A distinct sequence in the adenine nucleotide translocase from ''Artemia franciscana'' embryos is associated with insensitivity to bongkrekate and atypical effects of adenine nucleotides on Ca(2+) uptake and sequestration. FEBS J 278: 822–836.]
}}
# [http://www.ncbi.nlm.nih.gov/pubmed/4827906 Chen CH, Greenawalt JW, Lehninger AL (1974) Biochemical and ultrastructural aspects of Ca2+ transport by mitochondria of the hepatopancreas of the blue crab ''Callinectes sapidus''. J Cell Biol 61: 301–315. Open Access]
{{Labeling|journal=Mitochondr Physiol Network
|keywords=Mitochondrial permeability transition, Crustacean, Bongkrekate,
|articletype=Abstract
|mipnetlab=HU Budapest Chinopoulos C,
}}
}}
__NOTOC__
__NOTOC__
== Affiliations and author contributions ==
== Affiliations and author contributions ==


Csaba Konrad (1), Gergely Kiss (1), Beata Torocsik (1), Vera Adam-Vizi (1), Christos Chinopoulos (1)
:::: Csaba Konrad (1), Gergely Kiss (1), Beata Torocsik (1), Vera Adam-Vizi (1), Christos Chinopoulos (1)


(1) Department of Medical Biochemistry, Semmelweis University, Hungary; Email: [email protected]
:::: (1) Department of Medical Biochemistry, Semmelweis University, Hungary; Email: [email protected]


== Figure 1 ==
== Help ==
::::* [[MitoPedia: Terms and abbreviations]]


Β 
{{Labeling
== Help ==
|area=Respiration, mt-Structure;fission;fusion, Comparative MiP;environmental MiP
* [[Abstracts help]]
|injuries=Permeability transition
* [[MitoPedia Glossary: Terms and abbreviations]]
|organism=Artemia, Crustaceans
|preparations=Isolated mitochondria
|enzymes=Adenine nucleotide translocase
|topics=ADP, ATP, Calcium, pH
|instruments=Oxygraph-2k, O2k-Fluorometer, Ca
}}

Latest revision as of 14:15, 7 March 2020

Konrad C, Kiss G, Torocsik B, Adam-Vizi V, Chinopoulos C (2012) Absence of Ca2+-induced mitochondrial permeability transition but presence of bongkrekate-sensitive nucleotide exchange in C. crangon and P. serratus. Mitochondr Physiol Network 17.12.

Link: MiPNet17.12 Bioblast 2012 - Open Access

Konrad C, Kiss G, Torocsik B, Adam-Vizi V, Chinopoulos C (2012)

Event: Bioblast 2012

Csaba Konrad

Mitochondria from the embryos of brine shrimp (Artemia franciscana) do not undergo Ca2+-induced permeability transition in the presence of a profound Ca2+ uptake capacity [1]. Furthermore, this crustacean is the only organism known to exhibit bongkrekateinsensitive mitochondrial adenine nucleotide exchange, prompting the conjecture that refractoriness to bongkrekate and absence of Ca2+-induced permeability transition are somehow related phenomena [2]. Here we report that mitochondria isolated from two other crustaceans, brown shrimp (Crangon crangon) and common prawn (Palaemon serratus) exhibited bongkrekate-sensitive mitochondrial adenine nucleotide transport, but lacked a Ca2+-induced permeability transition. Ca2+ uptake capacity was robust in the absence of adenine nucleotides in both crustaceans, unaffected by either bongkrekate or cyclosporin A. Transmission electron microscopy images of Ca2+-loaded mitochondria showed needle-like formations of electron-dense material strikingly similar to those observed in mitochondria from the hepatopancreas of blue crab (Callinectes sapidus) [3] and the embryos of Artemia franciscana [2]. Alignment analysis of the partial coding sequences of the adenine nucleotide translocase (ANT) expressed in Crangon crangon and Palaemon serratus versus the complete sequence expressed in Artemia franciscana reappraised the possibility of the 208-214 amino acid region for conferring sensitivity to bongkrekate. However, our findings suggest that the ability to undergo Ca2+-induced mitochondrial permeability transition and the sensitivity of adenine nucleotide translocase to bongkrekate are not necessarily related phenomena.

  1. Menze MA, Hutchinson K, Laborde SM, Hand SC (2005) Mitochondrial permeability transition in the crustacean Artemia franciscana: absence of a calcium-regulated pore in the face of profound calcium storage. Am J Physiol Regul Integr Comp Physiol 289: R68-R76. Open Access
  2. Konrad C, Kiss G, Toeroecsik B, Labar JL, Gerencser AA, Mandi M, Adam-Vizi V, Chinopoulos C (2011) A distinct sequence in the adenine nucleotide translocase from Artemia franciscana embryos is associated with insensitivity to bongkrekate and atypical effects of adenine nucleotides on Ca(2+) uptake and sequestration. FEBS J 278: 822–836.
  3. Chen CH, Greenawalt JW, Lehninger AL (1974) Biochemical and ultrastructural aspects of Ca2+ transport by mitochondria of the hepatopancreas of the blue crab Callinectes sapidus. J Cell Biol 61: 301–315. Open Access

β€’ Keywords: Mitochondrial permeability transition, Crustacean, Bongkrekate

β€’ O2k-Network Lab: HU Budapest Chinopoulos C


Affiliations and author contributions

Csaba Konrad (1), Gergely Kiss (1), Beata Torocsik (1), Vera Adam-Vizi (1), Christos Chinopoulos (1)
(1) Department of Medical Biochemistry, Semmelweis University, Hungary; Email: [email protected]

Help


Labels: MiParea: Respiration, mt-Structure;fission;fusion, Comparative MiP;environmental MiP 

Stress:Permeability transition  Organism: Artemia, Crustaceans 

Preparation: Isolated mitochondria  Enzyme: Adenine nucleotide translocase  Regulation: ADP, ATP, Calcium, pH 


HRR: Oxygraph-2k, O2k-Fluorometer, Ca