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Altered Glycosylation of PSA in Prostate Cancer Tissue.

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The Prostate 📖 저널 OA 40.1% 2021: 1/1 OA 2025: 33/75 OA 2026: 34/94 OA 2021~2026 2025 Vol.85(14) p. 1290-1298
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유사 논문
P · Population 대상 환자/모집단
162 patients, PSA-glycoforms detected by succinylated wheat germ (WGA) and Vicia villosa (VVA) lectins were enriched in cancerous tissues as compared to adjacent benign tissues from the same patients (p < 10 for both, Kruskal-Wallis H test), although strong total PSA staining was more often found in benign tissues (p = 6*10).
I · Intervention 중재 / 시술
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C · Comparison 대조 / 비교
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O · Outcome 결과 / 결론
we showed that glycosylation of PSA in cancerous tissues is different from that in benign prostate.

Koistinen H, Merivirta RM, Lehto TP, Lempiäinen A, Erickson A, Stenman UH

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[BACKGROUND] The glycosylation of proteins is commonly altered in cancer.

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↓ .bib ↓ .ris
APA Koistinen H, Merivirta RM, et al. (2025). Altered Glycosylation of PSA in Prostate Cancer Tissue.. The Prostate, 85(14), 1290-1298. https://doi.org/10.1002/pros.70014
MLA Koistinen H, et al.. "Altered Glycosylation of PSA in Prostate Cancer Tissue.." The Prostate, vol. 85, no. 14, 2025, pp. 1290-1298.
PMID 40635354 ↗
DOI 10.1002/pros.70014

Abstract

[BACKGROUND] The glycosylation of proteins is commonly altered in cancer. This offers novel opportunities for cancer biomarker development. As prostate-specific antigen (PSA) is a glycoprotein, identification of cancer-specific PSA-glycoforms is feasible. Such PSA-glycoforms may provide valuable diagnostic and prognostic information.

[METHODS] PSA-glycoforms were studied in tissues, using in situ proximity-ligation assay (PLA)-based detection with a PSA-specific antibody and 25 different glycan-binding lectins.

[RESULTS] Using 25 different lectins and a small tissue microarray (TMA), we showed that glycosylation of PSA in cancerous tissues is different from that in benign prostate. In a larger TMA with samples from 162 patients, PSA-glycoforms detected by succinylated wheat germ (WGA) and Vicia villosa (VVA) lectins were enriched in cancerous tissues as compared to adjacent benign tissues from the same patients (p < 10 for both, Kruskal-Wallis H test), although strong total PSA staining was more often found in benign tissues (p = 6*10).

[CONCLUSIONS] We showed here that glycosylation of PSA is changed in situ in prostate cancer. The identified lectins, showing preferential binding to cancer-associated PSA-glycoforms, will aid the future development of a diagnostic serum test of prostate cancer. Such a test has potential to revolutionize prostate cancer diagnostics.

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