Biomedical subjects

Tsung-Hsien Chen

Publications and source records attributed to Tsung-Hsien Chen.

3 recordsLinked to original sources

PubMed2026

Integrative Transcriptomic and Proteomic Profiling Identifies S100P as a Potential Functional Biomarker for Sessile Serrated Lesions.

BACKGROUND: Sessile serrated lesions (SSLs) account for 15% of colorectal cancers (CRCs) but detection remains difficult due to flat morphology, mucinous features, and subtle histology. AIMS: This study aimed to identify novel and functionally relevant biomarkers of SSLs using transcriptomic screening and multi-omics validation. METHODS: Paired SSL and normal mucosa specimens (n = 6) underwent RNA sequencing. Differentially expressed genes (DEGs) were filtered for membrane or secretory proteins and validated across TCGA and adenoma transcriptomes. Functional significance was assessed using CRISPR dependency profiling, proteotranscriptomic concordance, pharmacogenomic sensitivity, and connectivity map analysis. RESULTS: We identified 216 upregulated genes in SSLs, including 68 encoding secretory/membrane proteins that better discriminated SSLs from controls and were enriched for adhesion and neuronal signaling while suppressing TNFα-NFκB inflammatory pathways. Cross-cohort comparison revealed five overlapping candidates between SSLs and TCGA CMS1 tumors. Among them, S100P emerged as the primary biomarker candidate, showing consistent upregulation in SSLs and CMS1 tumors while remaining low in normal mucosa and conventional adenomas. TFF1 also showed RNA-level upregulation but appeared more context-dependent. S100P demonstrated strong RNA-protein concordance in CRC cell-line profiling, supporting its detectability as a biomarker candidate. Pharmacogenomic profiling of LS411N cells revealed marked sensitivity to SN-38 and fluoropyrimidines, consistent with serrated CRC vulnerabilities. Connectivity map analysis identified perturbations, including MAPK1 and histone acetyltransferase suppression, that may reverse parts of the SSL transcriptional program. CONCLUSION: These findings prioritize S100P as a promising biomarker candidate for SSLs that warrants further validation in larger cohorts and clinically applicable platforms.

Humans↗

PubMed2003

Noninvasive glucose monitoring by back diffusion via skin: chemical and physical enhancements.

Blood glucose levels are routinely obtained by invasive and painful methods using glucose meters and test strips. The development of less invasive or non invasive techniques would be beneficial for diabetes patients. In this study, a noninvasive method was evaluated using the back diffusion of glucose across skin with or without permeation enhancement methods. An in vitro model was utilized. The stratum corneum (SC) was the predominant barrier for both back and forward diffusion of glucose across skin. Surfactants with various charges and essential oils (cyclic monoterpenes) were used as chemical enhancers to promote the back diffusion of glucose. A cationic surfactant (benzalkonium chloride) showed the highest enhancement, followed by anionic and nonionic surfactants. d-Limonene and 1,8-cineole dispersed in appropriate proportions of ethanol could enhance the glucose diffusion after pretreatment of the skin surface. Electroporation, defined as a physical method, significantly increased the amount of glucose that diffused back. The percentages of diffused glucose by 300 V (volts) and 500 V high voltage pulses on skin for 10 min were found to be 45 and 75 times greater than the control group, respectively.

Animals↗

PubMed2002

Cloning of a Ca(2+)/calmodulin-dependent protein kinase gene from the filamentous fungus Arthrobotrys dactyloides.

A Ca(2+)/calmodulin-dependent protein kinase (CaMK) gene was cloned and characterized from Arthrobotrys dactyloides, a nematode-trapping fungus. The resulting 373-amino-acid protein, FCaMK, has significant homology to mammalian CaMKs. FCaMK contains a serine/threonine kinase domain followed by a calmodulin-binding domain. The activation loop in FCaMK (amino acids 184-199) contains a phosphorylation site at threonine-188, which could be the target of a kinase activator. Truncated FCaMK mutants revealed that amino acids 296-324 are essential for calmodulin binding. An oligopeptide designed from residues 297-324 formed a stable peptide-calmodulin complex of 1:1 stoichiometry. Southern blot analysis detected a single copy of the fcamk gene, suggesting that FCaMK plays an important role in Ca(2+)/calmodulin signaling in A. dactyloides.

Amino Acid Sequence↗