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Habermann, J.

Publications and source records attributed to Habermann, J..

2 recordsLinked to original sources

Menin-Inhibition Sensitizes Acute Myeloid Leukemia to CLEC12A-Directed CAR Cell Therapy

Menin inhibitors targeting the Menin-KMT2A chromatin complex have emerged as highly selective therapies for KMT2A-rearranged (KMT2A-r) and NPM1-mutated (NPM1mut) acute myeloid leukemia (AML), with recent regulatory approval and increasing interest in combination strategies. In contrast, CAR cell therapies have not yet been successfully established for AML. Here, we show that menin-inhibition primes KMT2A-r and NPM1mut AML for CAR-based targeting by inducing robust and uniform expression of the myeloid antigen CLEC12A (CLL-1). Menin inhibitors did not impair T or NK cell viability, phenotype, or effector function. We engineered second-generation CLEC12A-directed CAR T cells that efficiently eliminated CLEC12A-positive AML. Across in vitro systems and xenograft models, the combination therapy consistently outperformed either monotherapy, resulting in profound disease control and significantly prolonged survival, with evidence of near-complete leukemia eradication in vivo. These findings support epigenetic priming with menin inhibitors to enhance CLEC12A-directed CAR cell-therapy in these AML subtypes. SignificanceMenin inhibitors, now approved for AML treatment, induce the immune target CLEC12A in NPM1mut and KMT2A-r AML subtypes and sensitize AML cells to CLEC12A-directed CAR T cells without compromising immune function. As CLEC12A-CARs are already in clinical testing, this combination is immediately actionable for clinical investigation.

cancer biology↗

Impact of Single Freeze-Thaw Cycles on Serum Protein Stability: Implications for Clinical Biomarker Validation Using Mass Spectrometry

BackgroundValidation of biomarkers for clinical diagnostics and therapy necessitates the availability of a substantial number of high-quality samples, along with a complete set of clinical data. Establishing standards for sample collection, storage, and quality control is essential to reduce the variability of sample quality. MethodsThis study evaluated the impact of a single freeze-and-thaw (FT) cycle on the quality of liquid nitrogen-stored clinical serum aliquots. Data-independent acquisition mass spectrometry (DIA-MS) was performed to measure serum protein abundance in a test cohort comprising 25 patients and 99 samples, and a validation cohort comprising 109 patients/samples. Abundance differences of paired fresh and FT samples were assessed by employing biostatistics and bioinformatics approaches, including clustering analyses, linear mixed models, machine learning, and functional annotation. ResultsFollowing the library-free data analysis and implementation of strict data preprocessing procedures, data on the relative abundance of 213 (test cohort) and 248 (validation cohort) human serum proteins was available. Overall, the proteomic data demonstrated high quality and reproducibility. Significant changes in abundance between fresh and FT samples was observed for 30 proteins in the test cohort (q-value [≤]0.05). Of these, 11 proteins (36.6%) were successfully validated in the validation cohort, including CP and IGHV6-1 which were identified as potential biomarker candidates for discriminating between patients with malignant or benign pancreatic disease. A correlation analysis of the measured protein intensity and storage duration revealed no significant association between the two variables. ConclusionsDistinct protein abundance patterns can be discerned between fresh serum samples and samples stored in liquid nitrogen. The findings of this study suggest that FT cycles are an important pre-analytical factor and should be addressed during the translation of protein-based biomarkers into clinical use.

molecular biology↗