Proteomics for Biomarker Discovery in Gynecological Cancers: A Systematic Review
Proteomics for Biomarker Discovery in Gynecological Cancers: A Systematic Review
Huang et al., 2025 | J Proteome Res | Systematic Review
Citation
Huang Dong-Hui, Li Yi-Zi, ... Wu Qi-Jun. Proteomics for Biomarker Discovery in Gynecological Cancers: A Systematic Review. J Proteome Res. 2025-Jan-03;24(1):1-12. doi:10.1021/acs.jproteome.4c00675
Abstract
The present study aims to summarize the current biomarker landscape in gynecological cancers (GCs) and incorporate bioinformatics analysis to highlight specific biological processes. The literature was retrieved from PubMed, Web of Science, Embase, Scopus, Ovid Medline, and Cochrane Library. The final search was conducted on December 7, 2022. Prospective registration was completed with the PROSPERO with registration number CRD42023477145. This systematic review covered proteomic research on biomarkers for cervical, endometrial, and ovarian cancers. The PANTHER classification system was used to classify the shortlisted candidate biomarkers (CBs), and the STRING database was utilized to visualize protein-protein interaction networks. A total of 23 articles were included in this systematic review. Consistently regulated CBs in the GCs include collagen alpha-2(I) chain, collagen alpha-1(III) chain, collagen alpha-2(V) chain, calreticulin, protein disulfide-isomerase A3, heat shock protein family A (Hsp70) member 5, prolyl 4-hydroxylase, beta polypeptide, fibrinogen alpha chain, fibrinogen gamma chain, apolipoprotein B-100, apolipoprotein C-IV, and apolipoprotein M. In conclusion, collagens, fibrinogens, chaperones, and apolipoproteins were revealed to be replicated in GCs and to be regulated consistently. These CBs contribute to GC etiology and physiology by participating in collagen fibril organization, blood coagulation, protein folding in endoplasmic reticulum, and lipid transporter activity.
Key Findings
These CBs contribute to GC etiology and physiology by participating in collagen fibril organization, blood coagulation, protein folding in endoplasmic reticulum, and lipid transporter activity.
Outcomes Measured
- Requires manual extraction
Population
| Field | Value |
|---|---|
| Population | See abstract |
| Sample Size | See abstract |
| Age Range | See abstract |
| Condition | See abstract |
MeSH Terms
- Humans
- Female
- Proteomics
- Biomarkers, Tumor
- Protein Interaction Maps
- Genital Neoplasms, Female
- Computational Biology
- Ovarian Neoplasms
- Endometrial Neoplasms
- Collagen Type I
- Collagen Type III
- Uterine Cervical Neoplasms
- Fibrinogen
- Calreticulin
Evidence Classification
- Level: Systematic Review
- Publication Types: Journal Article, Systematic Review, Research Support, Non-U.S. Gov't
- Vertical: collagen
Provenance
- PMID: 39698999
- DOI: 10.1021/acs.jproteome.4c00675
- PMCID: Not in PMC
- Verified: 2026-04-09 via PubMed E-utilities API
Source extracted via PubMed E-utilities API on 2026-04-09