{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077261/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077261/Raw_file-X101SC19093128_Z01_J002_B1_43.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD077261/Match_result-X101SC19093128_Z01_J002_B1_43.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["46506962@qq.com"],"submitter":["yang zhang"],"technology_type":["Mass Spectrometry","Gel-based experiment"],"software":[""],"submitter_keywords":["rna splicing","hand2","Bclaf1","Bclaf1; hand2; hfref; rna splicing; therapeutic target","therapeutic target","hfref"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077261"],"tissue":["Heart"],"sample_protocol":["1. Sample Treatment The stained protein band was cut, volume of the cut gel is 0.5-1 mm3. The cut gel was destained by 50% acetonitrile (ACN) in 50 mM triethylammonium bicarbonate (TEAB) and dehydrated upon washing with 100% ACN till the gel turned white. Proteins in gel were treated with 1000 µL 10 mM DTT for 40 min at 56°C and subsequently alkylated with 1000 µL 50mM IAM for 30 min in the dark. The gel was then washed by destained buffer and treated with ACN as above.  2. In-gel Digestion 10-20 μL 10 ng/µL trypsin was added into gel and incubation for 30 min on ice, then made up to 100 μL with 100 mM TEAB, proteins were digested overnight at 37°C. After centrifugation in low speed, the supernatant was collected and remaining peptides were extracted in 100 μL of 0.1% formic acid (FA). Combined the two supernatant and centrifuged at 12000 g for 5 min at room temperature. The supernatant was slowly loaded to the C18 desalting column, washed with 1 mL of washing solution (0.1% formic acid, 4% acetonitrile) 3 times, then eluted twice by 0.4 mL of elution buffer (0.1% formic acid, 75% acetonitrile). The eluents were combined and lyophilized. 3. LC-MS/MS Analysis Mobile phase A (100% water, 0.1% formic acid) and B solution (80% acetonitrile, 0.1% formic acid) were prepared. The lyophilized powder was dissolved in 10 μL of solution A, centrifuged at 15,000 rpm for 20 min at 4℃, and 1 μg of sample was injected into a home-made C18 Nano-Trap column (2 cm×75 μm, 3 μm). Peptides were separated in a home-made analytical column (15 cm×150 μm, 1.9 μm), using a linear gradient elution as listed in Table 1. The separated peptides were analyzed by Q Exactive HF-X mass spectrometer (Thermo Fisher), with ion source of Nanospray Flex™（ESI）, spray voltage of 2.3 kV and ion transport capillary temperature of 320°C. Full scan range from m/z 350 to 1500 with resolution of 60000 (at m/z 200), an automatic gain  control (AGC) target value was 3×106 and a maximum ion injection time was 20 ms. The top 40 precursors of the highest abundant in the full scan were selected and fragmented by higher energy collisional dissociation (HCD) and analyzed in MS/MS, where resolution was 15000 (at m/z 200), the automatic gain control (AGC) target value was 1×105, the maximum ion injection time was 45 2ms, a normalized collision energy was set as 27%, an intensity threshold was 2.2×104, and the dynamic exclusion parameter was 20 s. The raw data of MS detection was named as “.raw”."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["1 The identification of protein The resulting spectra from each fraction were searched separately against *** database by the search engines: Proteome Discoverer 2.2 (PD 2.2, Thermo). The search parameters are set as follows: mass tolerance for precursor ion was 10 ppm and mass tolerance for product ion was 0.02 Da. Carbamidomethyl was specified in PD 2.2 as fixed modifications. Oxidation of methionine (M) and acetylation of the N-terminus were specified in PD 2.2 as variable modifications. A maximum of 2 missed cleavage sites were allowed.  The identified protein contains at least 1 unique peptide with FDR no more than 1.0%. Proteins containing similar peptides that could not be distinguished by MS/MS analysis were identified as a same protein group."],"omics_type":["Proteomics"],"labhead":["yang zhang"],"instrument_platform":[""],"labhead_affiliation":["harbin medical university"],"species":["Mus Musculus (mouse)"],"submission_type":["PARTIAL"],"publication":["Not available"],"submitter_mail":["46506962@qq.com"],"submitter_affiliation":["Harbin Medica university"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"Bclaf1 Drives Heart Failure by Recruiting Srsf2 to Enhance Hand2 Pre-mRNA Splicing and Pathological Hypertrophy","description":"Heart failure with reduced ejection fraction (HFrEF) remains a major therapeutic challenge. Bcl2-associated transcription factor 1 (Bclaf1) is implicated in RNA splicing and cardiac disease, but its role in HFrEF pathogenesis is unknown. Here, we demonstrate that Bclaf1 expression is elevated in human HFrEF myocardium and in murine pressure-overload models. Cardiac-specific Bclaf1 overexpression drives pathological hypertrophy and systolic dysfunction, whereas its genetic knockout or AAV9-mediated knockdown attenuates these phenotypes. Mechanistically, Bclaf1 interacts with the splicing factor Srsf2 to bind and enhance the splicing efficiency of Hand2 pre-mRNA, leading to increased mature Hand2 levels and maladaptive remodeling. Inhibition of either Bclaf1 or Hand2 rescues cardiac function and structure in experimental HFrEF. Our work defines a novel Bclaf1/Srsf2/Hand2 splicing axis as a critical driver of HFrEF and reveals a promising therapeutic target for heart 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