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Briefly, the microdissected tissue was homogenized in GCHO buffer using glass-Teflon homogenizer coupled with Hei-TORQUE overhead stirrer (Heidolph) with thirteen slow and even strokes at 900 rpm. The homogenate was transferred to a reaction tube and centrifuged for 15 min at 1,700 x g, at 4°C (Eppendorf, Refrigerated Microcentrifuge 5426). The post-nuclear homogenate (PNH) was separated from the pellet and subsequently diluted with GCHO buffer to a final volume of 1.7 mL. A discontinuous sucrose gradient was layered in ultra-clear centrifugation tubes (5.6 mL, Beckman No: 344075) with three layers: a bottom cushion (4 mM Hepes, 2.5 M sucrose, pH 7.4), a middle layer (4 mM Hepes, 0.83 M sucrose, pH 7.4), and a top layer of the diluted PNH, all with a volume of 1.7 mL. The tube necks were sealed, and the gradient was centrifuged at 250 000 x g for 50 min at 4°C using a Sorvall Discovery 100SE (Thermo Scientific) or Optima XE-90 (Beckman Coulter) equipped with a VTi50 Rotor (Beckman Coulter). Following centrifugation, growth cone particles (F1 fraction) were recovered from the interface between the middle and top sucrose layer using an 18-gauge needle and a 3 mL syringe. The F1 fraction was either transferred onto a polycarbonate membrane filter previously washed with PBS (Millipore, No: VCT02500, pore size 0.1 µm), filtered with Rotavac Valve Control vacuum pump (Heidolph, No: 591-00130-00-2), washed with PBS (4 times with 1 mL of PBS) to remove potential proteomic contaminations, and stored at -80°C until analysis by LC-MS/MS. For each time point and input tissue five biological replicates were generated. Mass spectrometry sample analysis was performed by the Proteomics and Modomics Experimental Core Facility (PROMEC, NTNU). Tryptic samples were prepared from polycarbonate filters by first recovering the GCs in 600 µl 1% SDC, 100 mM Tris-HCl pH 8.5, 10 mM TCEP, 40 mM CAA and sonicated for 30 min 70°C. Afterwards, 600 µl 0.1 M Ammonium bicarbonate, 0.5 µg trypsin were added and the samples digested over-night at 37°C. Peptides were desalted using C18 spin columns, dried in a speedvac centrifuge and resuspended in 0.1% Formic acid before MS analysis. LC-MS/MS were performed on a timsTOF Pro (Bruker Daltonics) connected to a nanoElute (Bruker Daltonics) HPLC. The peptide solution was injected, and separation was done using a Pepsep 25 (150 µm x 25 cm) column with running buffers A (0.1% Formic acid) and B (0.1% Formic acid in Acetonitrile) with a gradient from 0% B to 40%B for 75 min. The timsTof instrument was operated in DDA PASEF mode with 10 PASEF scans per acquisition cycle and accumulation and ramp times of 100 ms each. The ‘target value’ was set to 20,000 and a dynamic exclusion was activated and set to 0.4 min. The quadrupole isolation width was set to 2 Th for m/z < 700 and 3 Th for m/z > 800."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["TimsTOF DDA raw data files were interpreted using MaxQuant software v. 2.6.1.0 (Cox & Mann, 2008). Proteins were identified with one unique peptide and a false discovery rate of 0.01 using the mouse proteome including isoforms from Uniprot (downloaded: 14.03.2024) as a reference dataset. Analysis parameters were Trypsin/P as a digestion enzyme; a maximum of two missed cleavages were allowed; six amino acids were used as minimum peptide length; oxidation (M), acetyl (protein N-term), and deamidation (NQ) were set as variable modifications. Label-free quantification (LFQ) was performed with match between runs enabled using MaxQuant standard settings. PTXQC R package (Bielow et al., 2016) was used to quality control results generated by MaxQuant. All further downstream analyses were conducted using a custom R script (R v. 4.2.3, script available from https://github.com/Quattrocolo-Lab/krause-et-al-2026). All proteins labelled as potential contaminants, only identified by site, and reverse were removed from the dataset. Proteins were considered as identified for a timepoint and tissue type if three out of five biological replicates showed an LFQ intensity value. GO term analyses were performed using ClusterProfiler v. 4.4.4 (S. Xu et al., 2024). GO term results were manually curated and redundant terms triggered by identical proteins removed. KEGG pathway analyses for mouse protein terms were performed using the online platform ShinyGO 0.85 (Ge et al., 2020). For single and multi-series time course analyses the package maSigPro v. 1.68.0 (Conesa & Nueda, 2025) was used with a quadratic regression model (degree = 2) and the parameters Q = 0.05, Benjamini-Hochberg correction for multiple testing adjustment, and a minimum of four observations for single series time course analysis using P1 as reference and the parameters Q = 0.05, Benjamini-Hochberg correction for multiple testing adjustment, and a minimum of six observations for the multi-series time course analysis with the hippocampal data as reference dataset. Human orthologues genes were identified using orthogene v. 1.2.1 (Schilder & Skene, 2022). Disease terms were identified by using DOSE v. 3.22.1 (Yu et al., 2015). All plots were generated in R using the packages ggplot2 v. 4.0.0 (Wickham, 2016), ggVennDiagram v. 1.5.2 (Gao & Dusa, 2025), ggvenn v. 0.1.10, ggalluvial v. 0.12.5 (Bojanowski & Edwards, 2016), and ComplexHeatmap v. 2.14.0 (Gu et al., 2016)."],"omics_type":["Proteomics"],"labhead":["Giulia Quattrocolo"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Group Leader, Quattrocolo Lab, Kavli Institute for Systems Neuroscience and Centre for Neural Computation, Norwegian University of Science and Technology (NTNU), Trondheim 7491, Norway"],"species":["Mus Musculus (mouse)"],"publication":["10.1242/DEV.205342"],"submitter_mail":["maike.krause@ntnu.no"],"submitter_affiliation":["Kavli Institute for Systems Neuroscience and Center for Neural Computation\nNorwegian University of Science and Technology (NTNU)\nTrondheim 7491"],"submitter_country":["Norway"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic profile of hippocampal growth cones through early postnatal development","description":"During early postnatal development, hippocampal circuits are assembled through the coordinated navigation of axonal growth cones toward their synaptic targets. While growth cones are known to rely on local proteomic changes to interpret guidance cues, the developmental dynamics of their proteomic composition remain poorly understood. We performed a systematic proteomic characterization of growth cones isolated from whole Hippocampus or Dentate gyrus tissue at postnatal day (P) 1, 3, and 5 from wildtype animals. Our analysis showed that at P1 growth cones of both tissues have a common proteomic signature. While hippocampal growth cones undergo a rapid transition from exploratory to a more mature state until P5, growth cones of the Dentate Gyrus maintain their exploratory profile in the same time frame suggesting a delayed maturation. Growth cones of the Hippocampus and Dentate Gyrus are characterized by several temporally regulated proteins, reflecting their dynamicity and different developmental trajectories.","dates":{"publication":"2026-06-11","submission":"2026-04-05"},"accession":"PXD076616","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:284812","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:3750","NEWT:291146","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:130821","NEWT:2320211","NEWT:27606","NEWT:290610","NEWT:1519788","NEWT:59202","NEWT:9975","NEWT:8643","NEWT:1801631","NEWT:1159899","NEWT:502780","NEWT:860688","NEWT:35231","NEWT:1774208","NEWT:8644","NEWT:1125630","NEWT:28930","NEWT:202914","NEWT:27602","NEWT:502779","NEWT:297246","NEWT:483139","NEWT:101491","NEWT:8639","NEWT:8637","NEWT:1114970","NEWT:285272","NEWT:192222","NEWT:9963","NEWT:197911","NEWT:197912","NEWT:239386","NEWT:2785785","NEW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