{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/checksum.txt"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_2.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_8.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_5.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_1.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_3.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_6.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_4.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_7.mzML"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_4.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/Uniprot_Rat_2025_09_24.Fasta"],"Mztab":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069737/030423_CaM_Fraction_.mzTab"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["mnader@alfaisal.edu"],"submitter":["Liaqat Ali"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Type 2 Diabetes Mellitus"],"software":["Not available"],"submitter_keywords":["Lc-msms","Rat","Tmt","Cardiac left ventricles"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069737"],"tissue":["Heart"],"sample_protocol":["Cardiac left ventricles were homogenized on ice in ice-cold lysis radioimmunoprecipitation assay buffer supplemented with complete protease inhibitor cocktail using an electric tissue ruptor. Samples were kept on ice for 30 min for maximal yield of proteins. The homogenate was cleared by centrifugation at 10,000g, 5 min, 4°C and the supernatant was collected. Protein concentration of each sample was determined using the Pierce BCA protein assay kit (Cat. No. 23225, Thermo Fisher Scientific). Immuno-isolated samples were reduced, S-alkylated and digested from the beads (1.25µg trypsin/lys-C, 37°C, overnight). The peptide digests were TMT labelled then pooled and desalted using a SepPak cartridge according to the manufacturer’s instructions (Waters).  The eluted peptides from the cartridge were fractionated by high pH reversed-phase chromatography system (Ultimate 3000 HPLC, Thermo Fisher Scientific).  In brief, the peptide digests were loaded onto a C18 Column (XBridge BEH, 130Å, 3.5 µm, 2.1 mm x 150 mm, Waters) in buffer A and eluted with an increasing gradient of buffer B (20 mM Ammonium hydroxide in acetonitrile, pH 10) from 0-95% over 60 minutes. The resulting fractions (8 in total) were dried and resuspended in 1% formic acid prior to online liquid chromatography tandem mass spectrometry."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Principal Component Analysis (PCA) and volcano plots were employed to explore the data. Raw data was processed to remove keratin and blood-related proteins (albumin and immunoglobulin). Data was preprocessed using standardization (z-score normalization) prior to PCA. The statistical software Python 3.11.6 was used for data analysis. The analysis included 5 Normal and 5 Diabetic samples. PCA was applied to explore patterns of variation, while volcano plots combined log2 fold-change (FC) and -log10(p-value) from a two-tailed Student’s t-test to assess differential protein expression between diabetics and controls. Differential protein expression analysis was conducted using a FC threshold of 1.3 and p-value cutoff of 0.05. The top 10 upregulated and downregulated proteins were selected based on FC magnitude and statistical significance. Z-score normalization was applied to the expression values for heatmap visualization. Variable Importance in Projection (VIP) scores were calculated to identify key proteins contributing to the separation between cases and controls; VIP>1, |FC| > 1.3, p-value<0.05."],"omics_type":["Proteomics"],"labhead":["Moni Nader"],"instrument_platform":[""],"labhead_affiliation":["Department of Medical Sciences, College of Medicine and Health Sciences, Khalifa University of Science and Technology, Abu Dhabi, United Arab Emirates and/or Department of Physiological Sciences, College of Medicine, Alfaisal University, Riyadh, Kingdom of Saudi Arabia."],"submission_type":["COMPLETE"],"species":["Rattus Norvegicus (rat)"],"publication":["42255577 Chacar S, Al Hageh C, Ali L, Zalloua P, Suleiman MS, Howarth FC, Khraibi AA, Nader M. The Calmodulin/Striatin Interaction Is Enhanced in Diabetic Hearts and Defines Novel Signaling Clusters Implicated in Cardiac Remodeling. ACS Omega. 2026 11(21):30801-30811 10.1021/acsomega.5c13122"],"submitter_mail":["la77@nyu.edu"],"submitter_affiliation":["New York University Abu Dhabi"],"submitter_country":["United Arab Emirates"],"doi":["10.6019/PXD069737"],"pubmed_abstract":["Diabetic cardiomyopathy (DbCM) impairs cardiac performance through complex mechanisms, which limits effective therapies. We investigated the protein networks of calmodulin (CaM), a striatin (STRN)-binding protein implicated in DbCM, and compared them with the STRN network from the same tissues. Using CaM as bait, we precipitated protein clusters from left ventricles (LVs) of diabetic rat hearts at 8 and 24 weeks post-streptozotocin (post-STZ). Diabetic rats exhibited pathological remodeling, evidenced by increased heart-to-body weight ratio, β-MHC protein, and ANF mRNA expression. Western blotting showed elevated STRN, but not PP2A-A or -C subunits, in chronic stages. Proteomic analysis at 24 weeks revealed 49 differentially interacting proteins (DIPs) with CaM: 18 enhanced and 31 diminished in diabetic LVs. Functional annotation highlighted the recruitment of proteins in metabolic pathways (fatty acid elongation and lipid metabolism) and PPAR signaling, alongside reduced interactions in lipid response, glucocorticoid response, calcium signaling, and amino acid biosynthesis. Comparative analysis of CaM and STRN interactomes converged to 231 proteins implicated mainly in metabolic processes. Out of these, three proteins (Hnrnpm, Acot7, and Gsta3) surfaced as regulators of metabolic, oxidative, and post-transcriptional remodeling. These findings reveal novel functional roles for the CaM/STRN complex in DbCM and identify a shared signaling hub that may guide therapeutic strategies for diabetes-associated cardiac deterioration."],"pubmed_title":["The Calmodulin/Striatin Interaction Is Enhanced in Diabetic Hearts and Defines Novel Signaling Clusters Implicated in Cardiac Remodeling."],"pubmed_authors":["Chacar Stephanie S, Al Hageh Cynthia C, Ali Liaqat L, Zalloua Pierre P, Suleiman M-Saadeh MS, Howarth Frank Christopher FC, Khraibi Ali A AA, Nader Moni M"],"additional_accession":[]},"is_claimable":false,"name":"The Calmodulin/Striatin Interaction is Enhanced in Diabetic Hearts and Defines Novel Signaling Clusters implicated in Cardiac Remodeling","description":"Diabetic cardiomyopathy (DbCM) halts cardiac performance with a complex etiology, hence the absence of an effective therapy for this disease. Herein we decoded the proteins hub interconnected with Calmodulin (CaM), a striatin (STRN) binding protein, that plays a role in DbCM. Using CaM as a bait, we precipitated protein clusters from left ventricles (LVs) of diabetic hearts at two stages of diabetes; 8- and 24-weeks rats treated with streptozotocin-STZ. Diabetic rats showed pathological heart remodeling confirmed by increased heart/body weight (HW/BW) ratio and increased β-MHC protein levels and ANF mRNA 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