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Differential expression of skeletal muscle mitochondrial proteins in yak, dzo, and cattle: a proteomics-based study.

ABSTRACT: Changes in yak mitochondria by natural selection in a hypoxic environment could be utilized to understand adaptation to low-oxygen conditions. Therefore, the differences in proteome profile of skeletal muscle mitochondria from yak, dzo, and cattle were analyzed by mass spectrometry, which were then classified into 3 groups, comparing between yak and dzo, yak and cattle, and dzo and cattle. 376 unique mitochondrial proteins were identified, including 192, 191, and 281 proteins in the yak-dzo, yak-cattle, and dzo-cattle groups, respectively. NRDP1 and COQ8A were expressed at higher levels in yak and dzo compared to those in cattle, indicating higher endurance capacity of yak and dzo in a low-oxygen environment. Gene Ontology (GO) terms of biological processes were significantly enriched in oxidation-reduction process, and that of molecular functions and cellular component were enriched in oxidoreductase activity and the mitochondrion, respectively. The most significantly affected pathways in Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis were Parkinson's disease, Huntington's disease, and oxidative phosphorylation between the yak-cattle and dzo-cattle groups; while metabolic pathways, citrate cycle, and carbon metabolism were significantly affected pathways in the yak-dzo group. ATP synthases, MTHFD1, MDH2, and SDHB were the most enriched hub proteins in the protein-protein interaction (PPI) network. These results indicated that mammals living at high altitudes could possibly possess better bioenergy metabolism than those living in the plains. The key proteins identified in the present study may be exploited as candidate proteins for understanding and fine-tuning mammalian adaptation to high altitudes.

SUBMITTER: Long L

PROVIDER: S-EPMC7468061 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature

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Differential expression of skeletal muscle mitochondrial proteins in yak, dzo, and cattle: a proteomics-based study.

Long Ling L Zhu Yipan Y Li Zhenzi Z Zhang Haixia H Liu Lixia L Bai Jialin J

The Journal of veterinary medical science 20200709 8

Changes in yak mitochondria by natural selection in a hypoxic environment could be utilized to understand adaptation to low-oxygen conditions. Therefore, the differences in proteome profile of skeletal muscle mitochondria from yak, dzo, and cattle were analyzed by mass spectrometry, which were then classified into 3 groups, comparing between yak and dzo, yak and cattle, and dzo and cattle. 376 unique mitochondrial proteins were identified, including 192, 191, and 281 proteins in the yak-dzo, yak ...[more]

PMID: 32641622

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Project description:Molecular chaperones and cytosolic stress proteins are actively involved in the stabilization, import and refolding of precursor proteins into mitochondria. The purpose of the present study was to evaluate the relationship between mitochondrial content under steady-state conditions, and during the induction of organelle biogenesis, with the expression of stress proteins and mitochondrial chaperonins. A comparison of steady-state levels of mitochondrial enzyme activity [cytochrome c oxidase (CYTOX)] with chaperonin levels [the heat-shock protein HSP60, the glucose-regulated protein GRP75 (mtHSP70)] in striated muscles possessing a wide range of oxidative capacities revealed a proportional expression between the two. This relationship was disrupted by chronic contractile activity brought about by 10 days of 10 Hz stimulation of the tibialis anterior (TA) muscle, which induced 2.4-fold increases in CYTOX activity, but 3.2- and 9.3-fold increases in HSP60 and GRP75 respectively. The inducible stress protein HSP70i was detected at low levels in control TA muscle, and was increased 9.6-fold by chronic contractile activity, to values comparable with those found in the unstressed soleus muscle. This increase occurred in the absence of changes in type I MHC levels, indicating independent regulation of these genes. Despite the increases in HSP60 and HSP70i proteins, contractile activity did not alter their respective mRNA levels, illustrating post-transcriptional mechanisms of gene regulation during contractile activity. In contrast, the mRNA levels encoding the co-chaperonin CPN10 were increased 3.3-fold by contractile activity. Thus, the expression of individual mitochondrial chaperonins is independently regulated and uncoordinated. The extent of the induction of these stress proteins and chaperonins by contractile activity exceeded that of membrane enzymes (e.g. CYTOX). It remains to be determined whether this marked induction of proteins comprising part of the protein import machinery is beneficial for the translocation of enzyme precursors into the mitochondria during conditions of accelerated biogenesis.

Project description:Electric organs (EOs) have evolved independently in vertebrates six times from skeletal muscle (SM). The transcriptional changes accompanying this developmental transformation are not presently well understood. Mormyrids and gymnotiforms are two highly convergent groups of weakly electric fish that have independently evolved EOs: while much is known about development and gene expression in gymnotiforms, very little is known about development and gene expression in mormyrids. This lack of data limits prospects for comparative work. We report here on the characterization of 28 differentially expressed genes between SM and EO tissues in the mormyrid Brienomyrus brachyistius, which were identified using suppressive subtractive hybridization (SSH). Forward and reverse SSH was performed on tissue samples of EO and SM resulting in one cDNA library enriched with mRNAs expressed in EO, and a second library representing mRNAs unique to SM. Nineteen expressed sequence tags (ESTs) were identified in EO and nine were identified in SM using BLAST searching of Danio rerio sequences available in NCBI databases. We confirmed differential expression of all 28 ESTs using RT-PCR. In EO, these ESTs represent four classes of proteins: (1) ion pumps, including the ?- and ?-subunits of Na(+)/K(+)-ATPase, and a plasma membrane Ca(2+)-ATPase; (2) Ca(2+)-binding protein S100, several parvalbumin paralogs, calcyclin-binding protein and neurogranin; (3) sarcomeric proteins troponin I, myosin heavy chain and actin-related protein complex subunit 3 (Arcp3); and (4) the transcription factors enhancer of rudimentary homolog (ERH) and myocyte enhancer factor 2A (MEF2A). Immunohistochemistry and western blotting were used to demonstrate the translation of seven proteins (myosin heavy chain, Na(+)/K(+)-ATPase, plasma membrane Ca(2+)-ATPase, MEF2, troponin and parvalbumin) and their cellular localization in EO and SM. Our findings suggest that mormyrids express several paralogs of muscle-specific genes and the proteins they encode in EOs, unlike gymnotiforms, which may post-transcriptionally repress several sarcomeric proteins. In spite of the similarity in the physiology and function of EOs in mormyrids and gymnotiforms, this study indicates that the mechanisms of development in the two groups may be considerably different.

Dataset Information

Differential expression of skeletal muscle mitochondrial proteins in yak, dzo, and cattle: a proteomics-based study.

Publications

Differential expression of skeletal muscle mitochondrial proteins in yak, dzo, and cattle: a proteomics-based study.

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