Diagnostic accuracy of serum insulin-like growth factor-binding protein 2 for ovarian cancer

Prayudi, Pande Kadek Aditya; Budiana, I Nyoman Gede; Mahayasa, Putu Doster; Surya, I Gede Ngurah Harry Wijaya; Wiradnyana, Anak Agung Gede Putra; Suwiyoga, Ketut

doi:10.1136/ijgc-2020-001479

Cited by 4 publications

(4 citation statements)

References 23 publications

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“…IGFBP2, a crucial member of the IGFBP family and a 36-kDa protein that is highly produced throughout fetal development, has been recognized as a significant oncogene (Shimasaki & Ling, 1991;Wei et al, 2021). IGFBP2 and the functionality of cancer cells are intimately connected, according to numerous studies (Prayudi et al, 2020;Sun et al, 2021;Tan et al, 2023;Tang et al, 2018;Zheng et al, 2020;Zhu et al, 2019). The heparin-binding domain 1 of matured IGFBP2 is required for IGFBP2-mediated cell proliferation, migration, and invasion (Arai et al, 1996;Li et al, 2020;Russo et al, 1997Russo et al, , 1999Russo et al, , 2005.…”

Section: Discussionmentioning

confidence: 99%

“…In all of these species, IGFs and a number of small‐molecular‐weight IGFBPs, particularly IGFBP‐2 and IGFBP‐4, are thought to stimulate or inhibit follicular development and maturation (Mazerbourg & Monget, 2018). In ovarian cancer, IGFBPs can serve as predictable biomarkers and potential therapeutic targets (Prayudi et al., 2020; Tan et al., 2023; Zheng et al., 2020). IGFBP‐2 is primarily expressed in fetal tissues that are highly proliferative (Li et al., 2020) including the early postimplantation progenitor cells of the upper layer, the ventricular region of the rostral neuroepithelium (Pintar et al., 1991; Wood et al., 1992), the apical ectodermal crest (van Kleffens et al., 1998), and progenitor cells of the spleen (Pintar et al., 1991) and liver (Streck & Pintar, 1992).…”

Section: Introductionmentioning

confidence: 99%

“…In rats, IGFBP‐2 expression has been shown to exist in the prenatal neocortex in a pattern consistent with that of neonatal astrocytic expression but is greatly reduced during postpartum development (Lee et al., 1993). In addition, serum IGFBP2 has a potential promising biomarker for detecting ovarian cancer (Prayudi et al., 2020). However, the role of IGFBP2 in trophoblast cell proliferation and RSA development is still unknown.…”

Section: Introductionmentioning

confidence: 99%

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Role of increased IGFBP2 in trophoblast cell proliferation and recurrent spontaneous abortion development: A pilot study

Ji,

Jiao,

Zhang

et al. 2024

Physiological Reports

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Recurrent spontaneous abortion (RSA) is a serious condition that adversely affects women's health. Differentially expressed proteins (DEPs) in plasma of patients experiencing RSA is helpful to find new therapeutic targets and identified with mass spectrometry. In 57 DEPs, 21 were upregulated and 36 were downregulated in RSA. Gene ontology analyses indicated that identified DEPs were associated with cell proliferation, including significantly downregulated insulin‐like growth factor binding protein 2 (IGFBP2). Immunohistochemical result using clinical decidual tissues also showed that IGFBP2 expression was significantly decreased in RSA trophoblasts. Cell proliferation assay indicated that IGFBP2 treatment increased the proliferation and mRNA expressions of PCNA and Ki67 in trophoblast cells. Transcriptome sequencing experiments and Kyoto Encyclopedia of Genes and Genomes analyses revealed that gene expression for components in PI3K‐Akt pathway in trophoblasts was significantly upregulated following IGFBP2 treatment. To confirm bioinformatics findings, we did cell‐based experiments and found that treatment of inhibitors for insulin‐like growth factor (IGF)‐1 receptor‐PI3K‐Akt pathway significantly reduced IGFBP2‐induced trophoblast cell proliferation and mRNA expressions of PCNA and Ki67. Our findings suggest that IGFBP2 may increase trophoblast proliferation through the PI3K‐Akt signaling pathway to affect pregnancy outcomes and that IGFBP2 may be a new target for future research and treatment of RSA.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Role of increased IGFBP2 in trophoblast cell proliferation and recurrent spontaneous abortion development: A pilot study

Ji,

Jiao,

Zhang

et al. 2024

Physiological Reports

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“…For example, the most prominent effects of insulin-like growth factor-binding protein 2 in ovarian cancer include promoting driving invasion, proliferation, and suppressing apoptosis. The area under the ROC curve of insulin-like growth factor-binding protein 2 in detecting ovarian cancer was 0.815 (95% CI: 0.721-0.910, P < 0.001), further studies are needed to confirm its diagnostic performance at an early stage of ovarian cancer [26].…”

Section: The Ms/ms Spectra Of Tryptic Peptides With Silac Labeling (A...mentioning

confidence: 99%

The Use of Stable Isotope Labeling with Amino Acids in Cell Culture (SILAC) to Study Ivermectin-Mediated Molecular Pathway Changes in Human Ovarian Cancer Cells

Li¹,

Zhan²

2022

Cell Culture - Advanced Technology and Applications in Medical and Life Sciences

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Stable isotope labeling with amino acids in cell culture (SILAC) was to use isotopic essential amino acids to replace the original amino acids for cell culture and passage for 8–10 generations, followed by mass spectrometry to identify proteins and the isotopic abundance difference to quantify proteins. SILAC can be used to characterize proteomic changes, and analyze protein turnover, protein interactions, and dynamic changes with quantitative accuracy, and high reproducibility. For this study, SILAC “light” (L-Lysine-2HCl [12C6, 14N2], L-Arginine-HCl [12C6, 14N4])- or “heavy” (L-Lysine-2HCl [13C6, 15N2], L-Arginine-HCl [13C6, 15N4])-labeling RPMI 1640 medium was used to culture human ovarian cancer TOV-21G cells for 10 passages, followed by the treatment of 0.1% dimethylsulfoxide for 24 h and 20 µM ivermectin for 24 h, respectively. The light- and heavy-isotope-labeled proteins were equally mixed (1:1) for digestion with trypsin. The tryptic peptide mixture was fractionated with liquid chromatography and analyzed with tandem mass spectrometry. In total, 4,447 proteins were identified in ivermectin-treated TOV-21G cells in relation to controls. Those proteins were enriched in 89 statistically significant signaling pathways and 62 statistically significant biological processes. These findings clearly demonstrated that SILAC quantitative proteomics was a useful and reliable method to study ivermectin-related proteomic changes in cancer cells, which in combination with molecular pathway networks and biological processes enrichments provided more comprehensive insights into molecular mechanisms of ivermectin in inhibiting TOV-21G cells.

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Quantification of putative ovarian cancer serum protein biomarkers using a multiplexed targeted mass spectrometry assay

Ryu,

Boylan,

Twigg

et al. 2024

Clin Proteom

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Background Ovarian cancer is the most lethal gynecologic malignancy in women, and high-grade serous ovarian cancer (HGSOC) is the most common subtype. Currently, no clinical test has been approved by the FDA to screen the general population for ovarian cancer. This underscores the critical need for the development of a robust methodology combined with novel technology to detect diagnostic biomarkers for HGSOC in the sera of women. Targeted mass spectrometry (MS) can be used to identify and quantify specific peptides/proteins in complex biological samples with high accuracy, sensitivity, and reproducibility. In this study, we sought to develop and conduct analytical validation of a multiplexed Tier 2 targeted MS parallel reaction monitoring (PRM) assay for the relative quantification of 23 putative ovarian cancer protein biomarkers in sera. Methods To develop a PRM method for our target peptides in sera, we followed nationally recognized consensus guidelines for validating fit-for-purpose Tier 2 targeted MS assays. The endogenous target peptide concentrations were calculated using the calibration curves in serum for each target peptide. Receiver operating characteristic (ROC) curves were analyzed to evaluate the diagnostic performance of the biomarker candidates. Results We describe an effort to develop and analytically validate a multiplexed Tier 2 targeted PRM MS assay to quantify candidate ovarian cancer protein biomarkers in sera. Among the 64 peptides corresponding to 23 proteins in our PRM assay, 24 peptides corresponding to 16 proteins passed the assay validation acceptability criteria. A total of 6 of these peptides from insulin-like growth factor-binding protein 2 (IBP2), sex hormone-binding globulin (SHBG), and TIMP metalloproteinase inhibitor 1 (TIMP1) were quantified in sera from a cohort of 69 patients with early-stage HGSOC, late-stage HGSOC, benign ovarian conditions, and healthy (non-cancer) controls. Confirming the results from previously published studies using orthogonal analytical approaches, IBP2 was identified as a diagnostic biomarker candidate based on its significantly increased abundance in the late-stage HGSOC patient sera compared to the healthy controls and patients with benign ovarian conditions. Conclusions A multiplexed targeted PRM MS assay was applied to detect candidate diagnostic biomarkers in HGSOC sera. To evaluate the clinical utility of the IBP2 PRM assay for HGSOC detection, further studies need to be performed using a larger patient cohort.

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Diagnostic accuracy of serum insulin-like growth factor-binding protein 2 for ovarian cancer

Cited by 4 publications

References 23 publications

Role of increased IGFBP2 in trophoblast cell proliferation and recurrent spontaneous abortion development: A pilot study

Role of increased IGFBP2 in trophoblast cell proliferation and recurrent spontaneous abortion development: A pilot study

The Use of Stable Isotope Labeling with Amino Acids in Cell Culture (SILAC) to Study Ivermectin-Mediated Molecular Pathway Changes in Human Ovarian Cancer Cells

Quantification of putative ovarian cancer serum protein biomarkers using a multiplexed targeted mass spectrometry assay

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