A1 Refereed original research article in a scientific journal

Lectin-nanoparticle concept for free PSA glycovariant providing superior cancer specificity




AuthorsKekki H, Montoya Perez I, Taimen P, Boström P, Gidwani K, Pettersson K

PublisherElsevier

Publication year2024

JournalClinica Chimica Acta

Journal name in sourceClinica Chimica Acta

Article number119689

Volume559

ISSN0009-8981

eISSN1873-3492

DOIhttps://doi.org/10.1016/j.cca.2024.119689(external)

Web address https://doi.org/10.1016/j.cca.2024.119689(external)


Abstract

Background

Using lectins to target cancer-associated modifications of PSA glycostructure for identification of clinically significant prostate cancers, e.g., Gleason score (GS) ≥ 7, from benign and indolent cancers (GS 6), is highly promising yet technically challenging. From previous findings to quantify increased PSA fucosylation in urine, we set out to construct a robust, specific test concept suitable for plasma samples.

Methods

Macrophage galactose‐binding lectin (MGL) coupled to 100 nm Eu3 + -nanoparticles was used to probe PSA captured from cancer cell lines, seminal plasma, and plasma samples from 249 patients with a clinical suspicion of prostate cancer onto 3 mm dense spots of free PSA antibody fab fragments. Results were compared to four kallikrein tests: tPSA, fPSA, iPSA and hK2.

Results

The fPSAMGLglycovariant provided superior discrimination of the GS ≥ 7 and benign + GS 6 groups (p 0.0003) compared to fPSA (NS). The corresponding AUC in ROC analysis was 0.70 compared to 0.66 for tPSA. In contrast to all four kallikrein tests, the fPSAMGLGV was independent of prostate gland volume. Using a logistic regression analysis the fPSAMGLGV significantly improved on the four-kallikrein model.

Conclusions

Due to Eu-nanoparticles and a dense fPSA capture spot, the fPSAMGLGV identifies an fPSA subform with the highest cancer specificity compared to the four conventional kallikreins.



Last updated on 2024-26-11 at 18:52