Proteoform interpretation is necessary for SASP because of secretion as an intact protein, a fully processed variant, as oxidized, cysteinylated, acetylated, phosphorylated, and fragment proteoforms. The goal of the present manuscript is the answer to the question about possibility of generation of defensible validation order using top-down proteomics records of secretomes of senescent, quiescent and proliferating IMR90 fibroblasts, maintaining Context-Anchored Proteoform Scoring (CAPS) calculation. The numerical data include combined secretomes records of senescent, quiescent and proliferating conditions plus seven selective senescent proteoforms: FTL, UBE2V1, HMGA2, DAP, CCL2, TPM3 and EEF1A1. The senescent and proliferating secretomes were very similar in terms of the truncated form pressure, with respective values of 0.67954 and 0.67935, while the quiescent secretome had the lower value of 0.52846. The ratio of senescence-proliferation alignment versus the senescence-quiescence distance was 0.00125, which implies that the abundance of fragment forms is not a criterion for senescence selectivity. The leading senescence selective candidates FTL and UBE2V1 had high leakage-sensitive CAPS values and were relatively easy to confirm. HMGA2 had the highest number of annotated modification sites (4.63 per 100 residues) and needed phosphorylation-specific validation, while DAP and CCL2 needed annotation-resolved confirmation. TPM3 and EEF1A1 remained to be fragment records requiring exploration. To sum up, the answer to the central question is positive – the records can provide a defensible validation order considering control-state form pressure, residue span, modification type, mass agreement, and confirmation burden.