Serum core‐type fucosylated prostate‐specific antigen index for the detection of high‐risk prostate cancer

Fujita, Kazutoshi; Hatano, Koji; Tomiyama, Eisuke; Hayashi, Yujiro; Matsushita, Makoto; Tsuchiya, Masato; Yoshikawa, Tomoyasu; Date, Mutsuhiro; Miyoshi, Eiji; Nonomura, Norio

doi:10.1002/ijc.33517

Cited by 19 publications

(12 citation statements)

References 38 publications

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“…[ 24 , 26 , 27 ] Besides, core fucosylated serum proteins also serve as promising biomarkers for disease diagnosis. [ 28 ] Thus, it is important to develop strategies for the detection of core fucosylated glycans with high sensitivity. Pholiota squarrosa lectin PhoSL, isolated from a mushroom, specifically recognizes core‐fucosylated N ‐glycans.…”

Section: Resultsmentioning

confidence: 99%

A Computational and Chemical Design Strategy for Manipulating Glycan‐Protein Recognition

Zhu,

Geng,

et al. 2024

Advanced Science

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Glycans are complex biomolecules that encode rich information and regulate various biological processes, such as fertilization, host‐pathogen binding, and immune recognition, through interactions with glycan‐binding proteins. A key driving force for glycan‐protein recognition is the interaction between the π electron density of aromatic amino acid side chains and polarized C─H groups of the pyranose (termed the CH–π interaction). However, the relatively weak binding affinity between glycans and proteins has hindered the application of glycan detection and imaging. Here, computational modeling and molecular dynamics simulations are employed to design a chemical strategy that enhances the CH–π interaction between glycans and proteins by genetically incorporating electron‐rich tryptophan derivatives into a lectin PhoSL, which specifically recognizes core fucosylated N‐linked glycans. This significantly enhances the binding affinity of PhoSL with the core fucose ligand and enables sensitive detection and imaging of core fucosylated glycans in vitro and in xenograft tumors in mice. Further, the study showed that this strategy is applicable to improve the binding affinity of GafD lectin for N‐acetylglucosamine‐containing glycans. The approach thus provides a general and effective way to manipulate glycan‐protein recognition for glycoscience applications.

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Section: Resultsmentioning

confidence: 99%

A Computational and Chemical Design Strategy for Manipulating Glycan‐Protein Recognition

Zhu,

Geng,

et al. 2024

Advanced Science

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“…Namely, N -glycans attached to N -glycosylation site N 220 have lower recoveries than the other two glycosylation sites and, more importantly, N -glycans occupying this site possess important N -glycomic features, such as fucosylation, sialylation, and a higher level of branching, which could be interesting for cancer biomarker discovery studies (Figure S-7). − Furthermore, PAP has three disulfide bonds. To facilitate digestion, the disulfide bonds are generally reduced with a reducing reagent.…”

Section: Results and Discussionmentioning

confidence: 99%

In-Depth Glycoproteomic Assay of Urinary Prostatic Acid Phosphatase

Wang,

de Nier,

Wuhrer

et al. 2023

ACS Meas. Sci. Au

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Prostate-specific antigen (PSA) is a well-known clinical biomarker in prostate cancer (PCa) diagnosis, but a better test is still needed, as the serum-level-based PSA quantification exhibits limited specificity and comes with poor predictive value. Prior to PSA, prostatic acid phosphatase (PAP) was used, but it was replaced by PSA because PSA improved the early detection of PCa. Upon revisiting PAP and its glycosylation specifically, it appears to be a promising new biomarker candidate. Namely, previous studies have indicated that PAP glycoforms differ between PCa and non-PCa individuals. However, an in-depth characterization of PAP glycosylation is still lacking. In this study, we established an in-depth glycoproteomic assay for urinary PAP by characterizing both the micro-and macroheterogeneity of the PAP glycoprofile. For this purpose, PAP samples were analyzed by capillary electrophoresis coupled to mass spectrometry after affinity purification from urine and proteolytic digestion. The developed urinary PAP assay was applied on a pooled DRE (digital rectal examination) urine sample from nine individuals. Three glycosylation sites were characterized, namely N 94 , N 220 , and N 333 , via N-glycopeptide analysis. Taking sialic acid linkage isomers into account, a total of 63, 27, and 4 N-glycan structures were identified, respectively. The presented PAP glycoproteomic assay will enable the determination of potential glycomic biomarkers for the early detection and prognosis of PCa in cohort studies.

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“…With recent advances in glycan structure analysis technology, promising glycan structures have been identified as biomarkers. 45 , 46 Among them, α2,3‐sialylation, 47 , 48 , 49 core fucosylation, 50 or GalNAcβ1‐4GlcNAc (LacdiNAc) structure 51 , 52 , 53 have received much attention as promising candidates (Figure 2 ), and platforms for corresponding clinical application are being developed.…”

Section: Post‐translational Modification Analysis For Precise Biomark...mentioning

confidence: 99%

Frontiers in mass spectrometry–based clinical proteomics for cancer diagnosis and treatment

2023

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Numerous omics studies, primarily genomics analyses, have been conducted to fully understand the molecular biological characteristics of cancer. In recent years, the depth of proteomic analysis, which comprehensively analyzes proteins and molecules that function directly in vivo, has increased dramatically. Proteomics using mass spectrometry (MS) is a promising technology to directly examine proteoforms, including post‐translational modifications and variants originating from genomic aberrations. Recent advances in MS‐based proteomics have enabled direct, in depth, and quantitative analysis of the expression levels of various cancer‐related proteins, as well as their cancer‐specific proteoforms, and proteins that fluctuate with cancer initiation and progression in cell lines and tissue samples. Additionally, the integration of proteomic data with genomic, epigenomic, and transcriptomic data has formed the growing field of proteogenomics, which is already yielding new biological and diagnostic knowledge. Deep proteomic profiling provides clinically useful information in various aspects, including understanding the mechanisms of cancer development and progression and discovering targets for diagnosis and drug development. Furthermore, it is expected to make a significant contribution to the promotion of personalized medicine. In this review, recent advances and impacts in MS‐based clinical proteomics are highlighted with a focus on oncology.

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Serum core‐type fucosylated prostate‐specific antigen index for the detection of high‐risk prostate cancer

Cited by 19 publications

References 38 publications

A Computational and Chemical Design Strategy for Manipulating Glycan‐Protein Recognition

A Computational and Chemical Design Strategy for Manipulating Glycan‐Protein Recognition

In-Depth Glycoproteomic Assay of Urinary Prostatic Acid Phosphatase

Frontiers in mass spectrometry–based clinical proteomics for cancer diagnosis and treatment

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