Quantitative phosphoproteomic analysis of porcine muscle within 24 h postmortem

Huang, Honggang; Larsen, Martin R.; Palmisano, Giuseppe; Dai, Jie; Lametsch, René

doi:10.1016/j.jprot.2014.04.020

Cited by 54 publications

(53 citation statements)

References 56 publications

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“…More recently, the skeletal muscle proteins of the most common mammalian livestock species, namely cattle (Talamo and others ; Bouley and others ; Chaze and others ; Bjarnadóttir and others ; Wu and others ), sheep (Addis and others , ; Yu and others ), and pig (Hakimov and others ; Di Luca and others ; Huang and others ), have been mapped and/or catalogued using mass spectrometry (MS)‐based proteomic approaches. These are less comprehensive than the human (Højlund and others ; Parker and others ) and murine skeletal muscle proteomes (Deshmukh and others ).…”

Section: Skeletal Muscle As Meatmentioning

confidence: 99%

Cooking‐Induced Protein Modifications in Meat

Morton

Clerens

et al. 2016

Comp Rev Food Sci Food Safe

186

115

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Food ingredients commonly undergo heat treatment. Meat, in particular, is typically consumed after some form of heating, such as boiling or roasting. Heating of meat can introduce a wide range of structural changes in its proteinaceous components. At the 3-dimensional structural level, meat proteins may denature and form aggregates upon heating. At the molecular level, primary structure (amino acid residue) alterations reported in cooked meat include protein carbonylation, modification of aromatic residues, and the formation of Maillard reaction products. Identification of these modifications is essential for determining the mechanism of thermal processing of meat and allowing better control of the nutritional and functional properties of products. This article reviews and summarizes the current state of understanding of protein modifications at the molecular level in commonly consumed mammalian food. In addition, relevant case studies relating to characterization of heat-induced amino acid residue-level modifications in other biological materials such as milk and wool are discussed to provide complementary insights.

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Section: Skeletal Muscle As Meatmentioning

confidence: 99%

Cooking‐Induced Protein Modifications in Meat

Morton

Clerens

et al. 2016

Comp Rev Food Sci Food Safe

186

115

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“…Currently, most of them are differential studies aiming to identify only the proteins that exhibit differential abundance, to the best of our knowledge. A few studies focusing on LTL did involve identification of the proteome in their samples, including one for bovine [82] and three for porcine [28,83,84]. They are briefly summarised in Table 1.…”

Section: Fig 3 -Number Of Proteins Identified In the Three Crude Framentioning

confidence: 99%

“…Secondly, species-specific database coverage at the time when the studies were conducted might differ. For example, the bovine longissimus thoracis proteomic study carried out by Bjarnadóttir et al [82] used a bovine database whereas the porcine LTL phosphoproteomic study published recently by Huang et al [83] utilised the mammalian database because the porcine database was not complete at that time.…”

Section: Fig 3 -Number Of Proteins Identified In the Three Crude Framentioning

confidence: 99%

In-depth characterisation of the lamb meat proteome from longissimus lumborum

Morton

Clerens

et al. 2015

EuPA Open Proteomics

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Lamb MuscleMeat Proteomics a b s t r a c t Lamb is one of the major red meats consumed globally, both as a key component in the diet of some countries, and as a niche meat product in others. Despite this relatively wide consumption, an in-depth description of the global protein composition of lamb has not been reported. In this study, we investigated the proteome of the 48 h post-mortem lamb longissimus lumborum through separation of the samples into sarcoplasmic, myofibrillar and insoluble fractions, followed by an in-depth shotgun proteomic evaluation and bioinformatic analysis. As a result, 388 ovine-specific proteins were identified and characterised.The 207 proteins found in the sarcoplasmic fraction were dominated by glycolytic enzymes and mitochondrial proteins. This fraction also contained several sarcomeric proteins, e.g., myosin light chains and titin. Some of them might be the degradation products from the post-mortem proteolysis. Actin, myosin and tropomyosin were abundant in the myofibrillar fraction while nebulin and titin were also present. Collagen type I, III and IV were found in the insoluble fraction but there were also sequences from myosin and titin. The present study also confirms the existence of at least 300 predicted protein sequences obtained from the latest issue of the sheep genome (version 3) with high confidence.

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“…5 A further study indicated that protein phosphorylation may play an important role in glycolysis and rigor mortis development in postmortem muscle through the regulation of proteins involved in glucose metabolism and muscle contraction. 7 Specifically, protein phosphorylation prevents proteolytic susceptibility of myofibrillar proteins to degradation by -calpain 8 and also negatively affects -calpain activity. 9 However, despite existing research, the mechanism of protein phosphorylation regulation on meat tenderness remains unknown.…”

Section: Introductionmentioning

confidence: 99%