Differential proteomics mass spectrometry of melanosis coli.

This study aims to reveal the biological relevancy between melanosis coli (MC) with colon cancer by analyzing the proteomics differences of tissues of melanosis coli, colon cancer, and normal ones to probe into the causes and development mechanisms of MC from the perspective of biomolecules. Fourteen differential protein spots were found in the study after using two-dimensional gel electrophoresis (2-DE) and bio-mass spectrometry (MALDI-TOF/TOF-MS). Specifically, six and eight differential protein spots in the melanosis coli tissues were detected, respectively, compared with the normal tissues and colon cancer tissues. Eight kinds of proteins, including keratin 8 (KRT8), keratin 18 (KRT18), fibrinogen beta chain isoform 2 preproprotein (FGB), catalase (CAT), 26s protease regulatory subunit 10b (PSMC6), isoform 1 of tropomyosin alpha-4 chain (TPM4), carbonic anhydrase 1 (CA1), isoform of prelammin-A/C (LMNA), were retrieved through the mass spectral database, which could be deemed as associated proteins of MC and colon cancer. The different expressions in the disease tissues indicate that these proteins may be connected with the carcinogenesis of MC as well as the malignant proliferation, development, differentiation, and diffusion of cancer cells. PMID: 32774690 [PubMed]
Source: American Journal of Translational Research - Category: Research Tags: Am J Transl Res Source Type: research