title: The sheep (Ovis aries) muscle proteome: Decoding the mechanisms of tolerance to Seasonal Weight Loss using label-free proteomics.
abstract: Seasonal Weight Loss (SWL) is one of the most pressing issues in animal production in the tropics and Mediterranean. This work aims to characterize muscle proteome changes as a consequence of SWL in meat producing sheep, using a label-free proteomics approach. We compare three breeds: the Australian Merino (SWL susceptible), the Damara (SWL tolerant) and the Dorper (SWL intermediate tolerance). We identified 668 proteins of the sheep proteome, 95 with differential regulation. Also we observe that the more vulnerable to SWL a breed is, the more differential abundance proteins we find. Protein binding was the most frequently altered molecular function identified. We suggest 6 putative markers for restricted nutritional conditions independently of breed: ferritin heavy-chain; immunoglobulin V lambda chain; transgelin; fatty acid synthase; glutathione S-transferase A2; dihydrodiol dehydrogenase 3-like. Moreover, we suggest as related to SWL tolerance: S100-A10 Serpin A3-5-like and Catalase, subject however to necessary validation assays. The identification of SWL-tolerance related proteins using proteomics will lead to increased stock productivity of relevant interest to animal production, particularly if identified at the muscle level, the tissue of economic importance in meat production.
  
  
  
  Seasonal Weight Loss (SWL) is the most pressing issue in animal production in the tropics and the Mediterranean. To counter SWL, farmers often use animal breeds that have a natural ability to withstand pasture scarcity. Here we study the sheep muscle proteome at the muscle level, the tissue of economic importance in meat production. Furthermore, the identification of proteins that change their abundance in response to SWL using proteomics can contribute to increased stock productivity of relevant interest to animal production. We identified 668 proteins of the sheep proteome. We demonstrate that the following proteins are affected by restricted nutritional conditions: ferritin heavy chain; immunoglobulin V lambda chain; transgelin; fatty acid synthase; glutathione S-transferase A2; dihydrodiol dehydrogenase 3-like. Furthermore, S100-A10, Serpin A3-5-like and Catalase are proteins that changed their abundance in response to SWL. Nevertheless, it is important to highlight that Catalase values for the merino breed were close to significance and therefore catalase validation is of utmost importance.
authors.affiliation: Plant Cell Biotechnology Laboratory, Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal; ICAAM - Instituto de Ciências Agrárias e Ambientais Mediterrânicas, Universidade de Évora, Évora, Portugal.
authors.forename: Ana M
authors.initials: AM
authors.lastname: Ferreira
authors.affiliation: Functional Genomics Center Zurich, ETH/UZH, Zurich, Switzerland.
authors.forename: Jonas
authors.initials: J
authors.lastname: Grossmann
authors.affiliation: Functional Genomics Center Zurich, ETH/UZH, Zurich, Switzerland.
authors.forename: Claudia
authors.initials: C
authors.lastname: Fortes
authors.affiliation: Department of Agriculture and Food Western Australia, Perth, WA, Australia.
authors.forename: Tanya
authors.initials: T
authors.lastname: Kilminster
authors.affiliation: Department of Agriculture and Food Western Australia, Perth, WA, Australia.
authors.forename: Tim
authors.initials: T
authors.lastname: Scanlon
authors.affiliation: University of Western Australia, Crawley, WA, Australia.
authors.forename: John
authors.initials: J
authors.lastname: Milton
authors.affiliation: Department of Agriculture and Food Western Australia, Perth, WA, Australia.
authors.forename: Johan
authors.initials: J
authors.lastname: Greeff
authors.affiliation: Department of Agriculture and Food Western Australia, Perth, WA, Australia.
authors.forename: Chris
authors.initials: C
authors.lastname: Oldham
authors.affiliation: Functional Genomics Center Zurich, ETH/UZH, Zurich, Switzerland.
authors.forename: Paolo
authors.initials: P
authors.lastname: Nanni
authors.affiliation: IBET - Instituto de Biologia Experimental e Tecnológica, Oeiras, Portugal; Plant Cell Biotechnology Laboratory, Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal; Ross University School of Veterinary Medicine, Saint Kitts and Nevis; Instituto Superior de Agronomia, Universidade de Lisboa, Lisboa, Portugal. Electronic address: aalmeida@isa.ulisboa.pt.
authors.forename: André M
authors.initials: AM
authors.lastname: Almeida
mesh_terms: D000222:Adaptation, Physiological; D000818:Animals; D001052:Apoferritins / Q000032:analysis; D015415:Biomarkers / Q000032:analysis; D064429:Fatty Acid Synthases / Q000032:analysis; D020869:Gene Expression Profiling; D005982:Glutathione Transferase / Q000032:analysis; D007135:Immunoglobulin Variable Region / Q000032:analysis; D007527:Isoenzymes / Q000032:analysis; D008840:Microfilament Proteins / Q000032:analysis; D009124:Muscle Proteins / Q000032:analysis; D009132:Muscles / Q000378:metabolism*; D020543:Proteome / Q000032:analysis / Q000378:metabolism*; D040901:Proteomics / Q000379:methods; D012621:Seasons; D012756:Sheep / Q000502:physiology*; D013045:Species Specificity; D015431:Weight Loss
chemical_list: D015415:Biomarkers; D007135:Immunoglobulin Variable Region; D007527:Isoenzymes; D008840:Microfilament Proteins; D009124:Muscle Proteins; D020543:Proteome; C051615:transgelin; D001052:Apoferritins; D064429:Fatty Acid Synthases; D005982:Glutathione Transferase; C119995:glutathione S-transferase alpha
keywords: Proteome; Seasonal Weight Loss; Sheep; Skeletal muscle