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In brief, the supernatant proteins were reconstituted in a lysis buffer containing 2% SDS and 20 mM TCEP. The mixtures were then heated to 95°C and maintained at that temperature for 10 minutes. A 1:1 (v/v) combination of SpeedBeads magnetic carboxylate-modified particles (Sigma Aldrich, beads A hydrophylic, cat.no GE45152105050250; beads B hydrophobic, cat.no GE65152105050250,) was prepared and subjected to four washes using LC-MS water. Subsequently, the beads were mixed with each sample in a binding buffer composed of 50% ethanol and 2.5% formic acid, followed by incubation with gentle shaking at 500 rpm for 15 minutes at room temperature. The resultant mixtures were then transferred into a filter plate (0.22 µm, Sigma Aldrich, part.no: MSGVN2210) to remove the unbound fraction via centrifugation at 1000 g.  The Beads were retained on the filter and subsequently washed four times with 70% ethanol. For digestion, trypsin was combined with a digestion solution containing 100 mM HEPES pH 7.5, 5 mM chloroacetamide, and 1.2 mM TCEP. This trypsin-containing solution was added to each sample on the plate at a ratio of 1 µg of trypsin per 25 µg of protein. The samples were digested overnight at room temperature with gentle shaking at 500 rpm. The resulting flowthrough, containing peptides, was collected through centrifugation at 1000 g. Subsequently, 10 µl of 2% DMSO was introduced to beads to elute bound peptides, which were then pooled with the previous flowthrough. To desalt the peptides, an Oasis HLB plate (Waters, cat.no 186001828BA) was employed following the manufacturer’s protocol. The desalted peptides were subsequently dried using a speed vacuum concentrator."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The raw data underwent a search against the Rattus norvegicus UniProt FASTA (proteome identifier [ID] UP000002494). For label-free quantification, the LFQ-MBR workflow is MSFragger was employed . Subsequently, proteins that were identified as contaminants or decoyed were eliminated from consideration. Only those proteins quantified in more than one replicate within each experimental group were selected for further analysis. The statistical analysis was conducted using R (version 4.2.2). To mitigate technical variation, the data was normalized using the vsn package. The evaluation of protein differential expression was performed utilizing the limma package. Differences in protein abundances were statistically assessed through the application of the Student’s t-test, moderated by Benjamini–Hochberg’s method, to ensure robust results. Two criteria were employed to identify proteins with significant secretion: Proteins showing a fold change greater than 2 and a p-value less than 0.05 were classified as increased in abundance, while proteins with a fold change less than 0.5 and a p-value less than 0.05 were categorized as decreased in abundance."],"omics_type":["Proteomics"],"labhead":["Ludvig J. Backman"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Medical and Translational Biology, Umeå University, Umeå SE-901 87, Sweden"],"species":["Rattus Norvegicus (rat)"],"publication":["10.1021/ACS.JPROTEOME.5C00068"],"submitter_mail":["shaochunzhu@gmail.com"],"submitter_affiliation":["Umea University"],"submitter_country":["Sweden"],"additional_accession":[]},"is_claimable":false,"name":"Impact of Static Myoblast Loading on Protein Secretion Linked to tenocyte Migration","description":"Exercise has been shown to promote wound healing, including tendon repair. Myokines released from exercised muscles are believed to play a significant role in this process. In our previous study, we used an in vitro co-culture and loading model to demonstrate that 2% static loading of myoblasts increased the migration and proliferation of co-cultured tenocytes—two crucial aspects of wound healing. IGF-1, released from myoblasts in response to 2% static loading, was identified as a contributor to the increased proliferation. However, the factors responsible for enhanced migration were not clear. In the current study, we subjected myoblasts in single culture conditions to 2%, 5%, and 10% static loading and performed proteomic analysis on the cell supernatants. Gene Ontology (GO) analysis revealed that 2% static loading induced the secretion of NBL1, C5, and EFEMP1, which are associated with cell migration and motility. Further investigation by adding exogenous recombinant proteins to human tenocytes showed that NBL1 increased tenocyte migration, but not proliferation. This effect was not replicated by treatment with C5 and 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