ノグチ　レイ   NOGUCHI Rei   野口　玲    所属   医学部 医学科    職種   講師
論文種別	原著
言語種別	英語
査読の有無	査読あり
表題	Identification of Cancer-Associated Proteins in Colorectal Cancer Using Mass Spectrometry.
掲載誌名	正式名：Proteomes 略　 称：Proteomes ISSNコード：22277382/22277382
掲載区分	国外
巻・号・頁	13(3),pp.---
著者・共著者	Naoyuki Toyota, Ryo Konno, Shuhei Iwata, Shin Fujita, Yoshio Kodera, Rei Noguchi, Tadashi Kondo, Yusuke Kawashima, Yuki Yoshimatsu
発行年月	2025/08
概要	BACKGROUND:Colorectal cancer (CRC) is a leading cause of cancer-related mortality worldwide, with a multifactorial etiology involving genetic and environmental factors. Advanced proteomics offers valuable insights into the molecular mechanisms of cancer, identifying proteins that function as mediators in tumor biology.METHODS:In this study, we used mass spectrometry-based data-independent acquisition (DIA) to analyze the proteomic landscape of CRC. We compared protein abundance in normal and tumor tissues from 16 patients with CRC to identify cancer-associated proteins and examine their roles in disease progression.RESULTS:The analysis identified 10,329 proteins, including 531 cancer-associated proteins from the Catalogue Of Somatic Mutations In Cancer (COSMIC) database, and 48 proteins specifically linked to CRC. Notably, clusters of proteins showed consistent increases or decreases in abundance across disease stages, suggesting their roles in tumorigenesis and progression.CONCLUSIONS:Our findings suggest that proteome abundance trends may contribute to the identification of biomarker candidates and therapeutic targets in colorectal cancer. However, given the limited sample size and lack of subtype stratification, further studies using larger, statistically powered cohorts are warranted to establish clinical relevance. These proteins may provide insights into drug resistance and tumor heterogeneity. Limitations of the study include the inability to detect low-abundance proteins and reliance on protein abundance rather than functional activity. Future complementary approaches, such as affinity proteomics, are suggested to address these limitations.
DOI	10.3390/proteomes13030038
PMID	40843711