Evidence map›Paper›PMID 28436483›Full record

ArticleScientific reports2017

iTRAQ-based proteomic analysis reveals key proteins affecting muscle growth and lipid deposition in pigs.

Zhixiu Wang, Peng Shang, Qinggang Li, Liyuan Wang, Yangzom Chamba, Bo Zhang, Hao Zhang, Changxin Wu

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
10.3field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

52 citing papers in PubMed, 123 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Zhixiu WangNational Engineering Laboratory for Animal Breeding, China Agricultural University, No. 2 Yuanmingyuan Xilu, Beijing 100193, China.
Peng ShangNational Engineering Laboratory for Animal Breeding, China Agricultural University, No. 2 Yuanmingyuan Xilu, Beijing 100193, China.
Qinggang LiInstitute of Animal Sciences and Veterinary Medicine, Anhui Academy of Agricultural Sciences, Hefei 230031, China.
Liyuan WangNational Engineering Laboratory for Animal Breeding, China Agricultural University, No. 2 Yuanmingyuan Xilu, Beijing 100193, China.
Yangzom ChambaCollege of Animal Science, Tibet Agriculture and Animal Husbandry University, Linzhi, 100086, China.
Bo ZhangNational Engineering Laboratory for Animal Breeding, China Agricultural University, No. 2 Yuanmingyuan Xilu, Beijing 100193, China.
Hao ZhangNational Engineering Laboratory for Animal Breeding, China Agricultural University, No. 2 Yuanmingyuan Xilu, Beijing 100193, China.
Changxin WuNational Engineering Laboratory for Animal Breeding, China Agricultural University, No. 2 Yuanmingyuan Xilu, Beijing 100193, China.
China Agricultural University · CNTibet University · CNInstitute of Animal Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Growth rate and meat quality, two economically important traits in pigs, are controlled by multiple genes and biological pathways. In the present study, we performed a proteomic analysis of longissimus dorsi muscle from six-month-old pigs from two Chinese native mini-type breeds (TP and DSP) and two introduced western breeds (YY and LL) using isobaric tag for relative and absolute quantification (iTRAQ). In total, 4,815 peptides corresponding to 969 proteins were detected. Comparison of expression patterns between TP-DSP and YY-LL revealed 288 differentially expressed proteins (DEPs), of which 169 were up-regulated and 119 were down-regulated. Functional annotation suggested that 28 DEPs were related to muscle growth and 15 to lipid deposition. Protein interaction network predictions indicated that differences in muscle growth and muscle fibre between TP-DSP and YY-LL groups were regulated by ALDOC, ENO3, PGK1, PGK2, TNNT1, TNNT3, TPM1, TPM2, TPM3, MYL3, MYH4, and TNNC2, whereas differences in lipid deposition ability were regulated by LPL, APOA1, APOC3, ACADM, FABP3, ACADVL, ACAA2, ACAT1, HADH, and PECI. Twelve DEPs were analysed using parallel reaction monitoring to confirm the reliability of the iTRAQ analysis. Our findings provide new insights into key proteins involved in muscle growth and lipid deposition in the pig.

Indexed as

Adipose TissueAnimalsBreedingGene Expression ProfilingGene OntologyIsotope LabelingLipid MetabolismMuscle DevelopmentMuscle, SkeletalPeptidesProtein Interaction MapsProteomeProteomicsSwineTranscriptomePeptidesProteome

Identifiers

PMID28436483
PMCPMC5402282
OpenAlexW2609637812

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.