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1.
J Cancer Res Clin Oncol ; 150(7): 334, 2024 Jul 05.
Artigo em Inglês | MEDLINE | ID: mdl-38969842

RESUMO

PURPOSE: Proteasome inhibitors (PIs), which cause cell death via tumor suppressor and pro-apoptotic proteins, are integral to treatment of many hematologic malignancies but are limited by their gastrointestinal adverse effects. Evidence regarding these PI-related adverse effects is scant. In this study, we evaluated gastrointestinal adverse events caused by PIs and compared gastrointestinal toxicities between bortezomib, carfilzomib, and ixazomib. METHODS: We conducted a retrospective study of cancer patients treated with PIs at a tertiary care cancer center to investigate the clinical characteristics of PI-related gastrointestinal adverse events. RESULTS: Our sample comprised 973 patients with PI exposure and stool studies ordered between January 2017 and December 2022. Of these, 193 patients (20%) had PI-related gastrointestinal toxicity based on clinical symptoms and stool study results. The most common symptom was diarrhea, present in 169 (88% of those with gastrointestinal toxicity). Twenty-two (11%) required hospitalization, and 71 (37%) developed recurrence of symptoms. Compared to bortezomib or carfilzomib, ixazomib had a longer interval from PI initiation to the onset of gastrointestinal symptoms (313 days vs 58 days vs 89 days, p = 0.002) and a significantly lower percentage of diarrhea-predominant presentation of gastrointestinal toxicity (71% vs 96% vs 91%, p = 0.048). CONCLUSION: While PI-related gastrointestinal toxicities have various presentations and courses based on different regimens, the vast majority of patients presented with milder disease behavior. Despite a considerably high rate of hospitalization and recurrence after treatment necessitating optimization of clinical management, our cohort demonstrates favorable outcomes without long-term consequences.


Assuntos
Compostos de Boro , Bortezomib , Gastroenteropatias , Glicina , Inibidores de Proteassoma , Humanos , Inibidores de Proteassoma/efeitos adversos , Masculino , Feminino , Estudos Retrospectivos , Pessoa de Meia-Idade , Compostos de Boro/efeitos adversos , Compostos de Boro/uso terapêutico , Idoso , Glicina/análogos & derivados , Glicina/efeitos adversos , Bortezomib/efeitos adversos , Bortezomib/administração & dosagem , Gastroenteropatias/induzido quimicamente , Oligopeptídeos/efeitos adversos , Adulto , Idoso de 80 Anos ou mais
2.
Cancers (Basel) ; 14(17)2022 Aug 31.
Artigo em Inglês | MEDLINE | ID: mdl-36077792

RESUMO

The era of personalized cancer therapy is here. Advances in the field of immunotherapy have paved the way for the development of individualized neoantigen-based therapies that can translate into favorable treatment outcomes and fewer side effects for patients. Addressing challenges related to the identification, access, and clinical application of neoantigens is critical to accelerating the development of individualized immunotherapy for cancer patients.

3.
FEBS Lett ; 594(1): 144-152, 2020 01.
Artigo em Inglês | MEDLINE | ID: mdl-31432503

RESUMO

Purinergic signaling plays important roles in bone. P2X5, a member of ligand-gated ion channel receptors, has been demonstrated to regulate osteoclast maturation. However, the molecular mechanism of P2X5-mediated osteoclast regulation remains unclear. Here, we identified methylosome protein 50 (MEP50), a critical cofactor of the protein arginine methyltransferase 5 (PRMT5), as a P2X5-associating molecule. RNAi-mediated knockdown of MEP50 results in decreased formation of mature osteoclasts. MEP50 associates with P2X5, and this association requires the C-terminal intracellular region of P2X5. Additionally, impaired maturation of P2X5-deficient osteoclasts could be restored by transduction of full-length P2X5, but not a C-terminal deletion mutant of P2X5. These results indicate that P2X5 associates with MEP50 and suggest a link between the PRMT5 complex and P2X5 signaling in osteoclast maturation.


Assuntos
Diferenciação Celular , Osteoclastos/metabolismo , Receptores Purinérgicos P2X5/metabolismo , Fatores de Transcrição/metabolismo , Animais , Sítios de Ligação , Células HEK293 , Humanos , Camundongos , Osteoclastos/citologia , Ligação Proteica , Proteína-Arginina N-Metiltransferases/metabolismo , Receptores Purinérgicos P2X5/química , Transdução de Sinais , Fatores de Transcrição/genética
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