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Link to original content: https://pubmed.ncbi.nlm.nih.gov/18484766
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. 2008 Jun;7(6):2204-14.
doi: 10.1021/pr070371f. Epub 2008 May 17.

Altered proteome biology of cardiac mitochondria under stress conditions

Affiliations

Altered proteome biology of cardiac mitochondria under stress conditions

Jun Zhang et al. J Proteome Res. 2008 Jun.

Abstract

Myocardial ischemia-reperfusion induces mitochondrial dysfunction and, depending upon the degree of injury, may lead to cardiac cell death. However, our ability to understand mitochondrial dysfunction has been hindered by an absence of molecular markers defining the various degrees of injury. To address this paucity of knowledge, we sought to characterize the impact of ischemic damage on mitochondrial proteome biology. We hypothesized that ischemic injury induces differential alterations in various mitochondrial subcompartments, that these proteomic changes are specific to the severity of injury, and that they are important to subsequent cellular adaptations to myocardial ischemic injury. Accordingly, an in vitro model of cardiac mitochondria injury in mice was established to examine two stress conditions: reversible injury (induced by mild calcium overload) and irreversible injury (induced by hypotonic stimuli). Both forms of injury had a drastic impact on the proteome biology of cardiac mitochondria. Altered mitochondrial function was concomitant with significant protein loss/shedding from the injured organelles. In the setting of mild calcium overload, mitochondria retained functionality despite the release of numerous proteins, and the majority of mitochondria remained intact. In contrast, hypotonic stimuli caused severe damage to mitochondrial structure and function, induced increased oxidative modification of mitochondrial proteins, and brought about detrimental changes to the subproteomes of the inner mitochondrial membrane and matrix. Using an established in vivo murine model of regional myocardial ischemic injury, we validated key observations made by the in vitro model. This preclinical investigation provides function and suborganelle location information on a repertoire of cardiac mitochondrial proteins sensitive to ischemia reperfusion stress and highlights protein clusters potentially involved in mitochondrial dysfunction in the setting of ischemic injury.

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Figures

Figure 1
Figure 1. Schematic Diagram of Experimental Design Using the in vitro Model of CardiacMitochondrial Injury
Figure 2
Figure 2. Examination of Mitochondrial Function Under Stress Conditions. 2A
Index of mitochondrial integrity was assessed after reversible injury (RI) or irreversible injury (II) by measuring cytochrome c oxidase activity. Activity measured in the presence of DDM which destroys mitochondrial outer membranes, was taken as total cytochrome c oxidase activity as detailed in Experimental Procedures. Compared with control group, reversible calcium treatment (RI) induced injury of about 15% of mitochondria. In contrast, hypotonic treatment (II) caused more than 80% of mitochondria to burst. 2B. Measurement of cytochrome c release by immunoblotting. Irreversible injury (II) induced more cytochrome c release from mitochondria compared with reversible injury (RI). 2C. Determination of mitochondrial swelling. Mitochondrial swelling was determined in control group, where CsA did not have an effect; in the group of reversible injury (RI), where CsA prevented calcium-induced swelling; and in the group of irreversible injury (II), where CsA did not prevent calcium-induced swelling. 2D. The morphology of the isolated mitochondria as determined by electron microscopy. Left panel shows that control, non-treated mitochondria were a homogeneous population with intact membranes and orthodox cristae structure. The middle panel shows a similar picture of mitochondria after reversible injury (RI) with few injured/swollen mitochondria and moderately perturbed cristae structure. In contrast, irreversible injury (II) induced rupture of the majority of mitochondria with a marked absence of intact structure (right panel) (magnification 19,000×). 2E. Detection of oxidation as posttranslational modification of identified proteins by immunoblotting. Upper panel shows a stronger signal in irreversible injury, suggesting that irreversible injury was associated with the release of a greater level of ROS-modified proteins. Middle panel showed VDAC1 was modified by ROS in irreversible injury. Lower panel showed total VDAC1 protein expression as internal control.
Figure 3
Figure 3. Proteome Biology of Identified Proteins
Each protein was assigned to its respective functional cluster(s) and spatial location(s)according to the Gene Ontology Annotations database (GOA) and Swiss-Prot protein knowledgebase(http://www.expasy.org/). 3A. Sub-organellar location of identified proteins. Mitochondrial released proteins were previously annotated to be localized in the OMM, IMS, IMM, Matrix, or mitochondria in general. In addition, a subpopulation of mitochondrial released proteins was not previously annotated as mitochondrial proteins; their primarily annotated subcellular locations are shown in the lower panel. 3B. Biological function of identified proteins; 3C. Combined analyses of location and function. The x axis represents the subcellular compartment(s) for protein annotation according to current databases, whereas the y axis indicates the functional cluster the identified proteins belong to. The detailed information regarding the characterization of these proteins by mass spectrometry, functional and subcellular annotation (Swiss-Prot, GOA, and our own Annotations), the spectra counts data and probability scores for each peptide were included in Tables S1 and S2 in the Supplemental Material.
Figure 3
Figure 3. Proteome Biology of Identified Proteins
Each protein was assigned to its respective functional cluster(s) and spatial location(s)according to the Gene Ontology Annotations database (GOA) and Swiss-Prot protein knowledgebase(http://www.expasy.org/). 3A. Sub-organellar location of identified proteins. Mitochondrial released proteins were previously annotated to be localized in the OMM, IMS, IMM, Matrix, or mitochondria in general. In addition, a subpopulation of mitochondrial released proteins was not previously annotated as mitochondrial proteins; their primarily annotated subcellular locations are shown in the lower panel. 3B. Biological function of identified proteins; 3C. Combined analyses of location and function. The x axis represents the subcellular compartment(s) for protein annotation according to current databases, whereas the y axis indicates the functional cluster the identified proteins belong to. The detailed information regarding the characterization of these proteins by mass spectrometry, functional and subcellular annotation (Swiss-Prot, GOA, and our own Annotations), the spectra counts data and probability scores for each peptide were included in Tables S1 and S2 in the Supplemental Material.
Figure 4
Figure 4. Semi Quantitative Analysis of Identified Proteins Using Spectra Abundance Factors (SAF)
We established an index called normalized SAF, which is defined as peptide spectra counts ofindividual proteins divided by total peptide spectra counts. Protein IDs with their IPI numbers(shown in all x axis of this figure) can be located in Tables S1 and S2 in Supplemental Material. Protein names corresponding to IPI numbers in this figure were listed Table S4 in Supplemental Material.4A. Protein samples from both experimental groups were analyzed according to their functional clusters, e.g., redox. Three proteins (sulfite oxidase, [IPI00153144], superoxide dismutase [IPI00109109], and peroxiredoxin 5, [IPI00129517]) in the redox group were compared. The release of superoxide dismutase was found to be in a significant high amount in the experimental group of irreversible injury. 4B. Protein samples from both experimental groups were analyzed on the oxidative phosphorylation cluster. The majority of released proteins in this category were found to be in a greater level following irreversible injury, e.g., the release of ATP synthase alpha chain (IPI00130280) was found to be 7 times greater in the experimental group of irreversible group. 4C and 4D. Protein samples from both experimental groups were analyzed on metabolic cluster according to their submitochondrial localization. The significant amount of released proteins in this category was found to be associated with mitochondrial matrix; e.g., dihydrolipoyl dehydrogenase (IPI00115569).
Figure 4
Figure 4. Semi Quantitative Analysis of Identified Proteins Using Spectra Abundance Factors (SAF)
We established an index called normalized SAF, which is defined as peptide spectra counts ofindividual proteins divided by total peptide spectra counts. Protein IDs with their IPI numbers(shown in all x axis of this figure) can be located in Tables S1 and S2 in Supplemental Material. Protein names corresponding to IPI numbers in this figure were listed Table S4 in Supplemental Material.4A. Protein samples from both experimental groups were analyzed according to their functional clusters, e.g., redox. Three proteins (sulfite oxidase, [IPI00153144], superoxide dismutase [IPI00109109], and peroxiredoxin 5, [IPI00129517]) in the redox group were compared. The release of superoxide dismutase was found to be in a significant high amount in the experimental group of irreversible injury. 4B. Protein samples from both experimental groups were analyzed on the oxidative phosphorylation cluster. The majority of released proteins in this category were found to be in a greater level following irreversible injury, e.g., the release of ATP synthase alpha chain (IPI00130280) was found to be 7 times greater in the experimental group of irreversible group. 4C and 4D. Protein samples from both experimental groups were analyzed on metabolic cluster according to their submitochondrial localization. The significant amount of released proteins in this category was found to be associated with mitochondrial matrix; e.g., dihydrolipoyl dehydrogenase (IPI00115569).
Figure 5
Figure 5. Target Validation of Identified Proteins
Immunoblotting based verification of identified proteins. Creatine kinase and SOD were detected in both experimental groups of reversible injury and irreversible injury (upper left panel); whereas moesin, TOM40, and frataxin appeared dramatically more abundant in the experimental group of reversible injury (lower left panel). In contrast, the inner mitochondrial membrane proteins TIM44 and prohibitin, metaxin-2, fatty acid binding protein, and flotillin-1 were found to be much greater in the experimental group of irreversible injury (right panel).
Figure 6
Figure 6. The in vivo murine model of regional myocardial ischemia injury. 6A
The protocol to produce a myocardial infarction and the assessment of the risk zone wereillustrated as shown. The resultant infarct size was determined by postmortem tetrazolium staining. 6B. Validation of identified proteins in the experimental groups of irreversible injury using the in vivo model of regional myocardial ischemia/reperfusion injury. Risk zone and non-risk zone were collected and separated into cytosol and mitochondria by differential centrifugation. Increased presence of peroxiredoxin 5, TIM44, and catalase was observed in the cytosol of the risk zone as compared that observed in the sham control hearts, suggesting that these proteins were released from the mitochondria in vivo during injury (left panel); whereas no significant changes were detected in the mitochondrial fraction. Ponceau S image showed equal loading of proteins (lower panel).

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