Comparison of Haptoglobin and Alpha1-Acid Glycoprotein Glycosylation in the Sera of Small Cell and Non-Small Cell Lung Cancer Patients

Ferens-Sieczkowska, Mirosława; Kratz, Ewa Maria; Kossowska, Barbara; Passowicz−Muszyńska, Ewa; Jankowska, Renata

doi:10.5604/17322693.1061788

Cited by 24 publications

(21 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Total expression of carbohydrate epitopes was measured with the direct lectin-ELISA method as described by us previously for fucose [ 25 , 26 ]. The glycoproteins sialylation was determined using two biotinylated lectins: Maackia amurensis agglutinin, MAA and Sambucus nigra agglutinin, SNA, recognizing sialic acid α 2,3- and α 2,6-linked, respectively (Vector Laboratories Inc., Burlingame, CA, USA).…”

Section: Methodsmentioning

confidence: 99%

The Analysis of Sialylation,N-Glycan Branching, and Expression ofO-Glycans in Seminal Plasma of Infertile Men

et al. 2015

Self Cite

View full text Add to dashboard Cite

Carbohydrates are known to mediate some events involved in successful fertilization. Although some studies on the glycosylation of seminal plasma proteins are available, the total glycan profile was rarely analyzed as a feature influencing fertilization potential. In this work we aimed to compare some glycosylation traits in seminal plasma glycoproteins of fertile and infertile men. The following findings emerge from our studies: (1) in human seminal plasma the presence and alterations of O-linked glycans were observed; (2) the expression of SNA-reactive sialic acid significantly differs between asthenozoospermia and both normozoospermic (fertile and infertile) groups; (3) the expression of PHA-L-reactive highly branched N-glycans was significantly lower in oligozoospermic patients than in both normozoospermic groups. Indication of the appropriate lectins that would enable the possibly precise determination of the glycan profile seems to be a good supplement to mass spectrum analysis. Extension of the lectin panel is useful for the further research.

show abstract

Section: Methodsmentioning

confidence: 99%

The Analysis of Sialylation,N-Glycan Branching, and Expression ofO-Glycans in Seminal Plasma of Infertile Men

et al. 2015

Self Cite

View full text Add to dashboard Cite

show abstract

“…Employing this method, approximately 130 sialylated glycoproteins were identified and sialylated plasma protease C1 inhibitor was found to be down-regulated in pancreatic cancer serum, which may serve as a marker for cancer [ 96 ]. Another study in small cell and non-small cell lung cancer patients showed different glycosylation profiles including α2–3-sialylation and expression of sialyl Lewis X (SLX) epitopes on acute phase proteins of α-1-acid glycoprotein and haptoglobin [ 97 ] .…”

Section: Protein-specific Sialylation Changes As Serum Markers In Spementioning

confidence: 99%

Serum sialylation changes in cancer

2018

View full text Add to dashboard Cite

Cancer is a major cause of death in both developing and developed countries. Early detection and efficient therapy can greatly enhance survival. Aberrant glycosylation has been recognized to be one of the hallmarks of cancer as glycans participate in many cancer-associated events. Cancer-associated glycosylation changes often involve sialic acids which play important roles in cell-cell interaction, recognition and immunological response. This review aims at giving a comprehensive overview of the literature on changes of sialylation in serum of cancer patients. Furthermore, the methods available to measure serum and plasma sialic acids as well as possible underlying biochemical mechanisms involved in the serum sialylation changes are surveyed. In general, total serum sialylation levels appear to be increased with various malignancies and show a potential for clinical applications, especially for disease monitoring and prognosis. In addition to overall sialic acid levels and the amount of sialic acid per total protein, glycoprofiling of specific cancer-associated glycoproteins, acute phase proteins and immunoglobulins in serum as well as the measurements of sialylation-related enzymes such as sialidases and sialyltransferases have been reported for early detection of cancer, assessing cancer progression and improving prognosis of cancer patients. Moreover, sialic-acid containing glycan antigens such as CA19–9, sialyl Lewis X and sialyl Tn on serum proteins have also displayed their value in cancer diagnosis and management whereby increased levels of these factors positively correlated with metastasis or poor prognosis.

show abstract

“…STn neo- or over-expression has been described in many types of epithelial cancer including pancreas 24 , 30 , 31 , colorectal 26 , 32 , ovarian 20 and breast cancers 33 . Similarly, increased fucosylation of Hp has also been reported in cancers of pancreas 34 , prostate 11 , lung 35 , ovarian 36 and colon 37 . Therefore, it is necessary to combine clinically used biomarker AFP with ELISA Index or fucosylated Hp /Hp ratio for HCC diagnosis.…”

Section: Discussionmentioning

confidence: 68%

Aided Diagnosis of Hepatocellular Carcinoma Using Serum Fucosylated Haptoglobin Ratios

Shang¹,

Li²,

Qin³

et al. 2017

J. Cancer

View full text Add to dashboard Cite

Aberrant fucosylation plays a functional role in regulating ontogeny and celluar differentiation and are differentially regulated in cancerous condition, which could provide hallmarks for cancer diagnostics and surveillance. We previously developed a magnetic beads-based lectin ELISA system to measure fucosylated haptoglobin (Hp), which has been reported to be a cancer biomarker through a series of glycoproteomic analysis. In this study, serum fucosylated Hp ratios were measured using our ELISA kit in a separate cohort of 260 patients independently, including 130 healthy controls and 130 patients with hepatocellular carcinoma (HCC). Fucosylated Hp /Hp ratio (levels of fucosylated Hp /levels of protein Hp) and ELISA Index (OD value of fucosylated Hp /OD value of protein Hp) were calculated respectively to reflect Hp fucosylation level on its protein level. Our data showed that fucosylated Hp /Hp ratio (AUC=0.8449) and ELISA Index (AUC=0.8581) had better performance in distinguishing HCC from controls, which indicated that fucosylated Hp ratios could improve the diagnosis and prediction of HCC even with a low level of alpha-fetoprotein (AFP). Additionally, the combination analysis of AFP and fucosylated Hp ratios increased the AUC value for HCC diagnosis.

show abstract

Comparison of Haptoglobin and Alpha1-Acid Glycoprotein Glycosylation in the Sera of Small Cell and Non-Small Cell Lung Cancer Patients

Cited by 24 publications

References 24 publications

The Analysis of Sialylation,N-Glycan Branching, and Expression ofO-Glycans in Seminal Plasma of Infertile Men

The Analysis of Sialylation,N-Glycan Branching, and Expression ofO-Glycans in Seminal Plasma of Infertile Men

Serum sialylation changes in cancer

Aided Diagnosis of Hepatocellular Carcinoma Using Serum Fucosylated Haptoglobin Ratios

Contact Info

Product

Resources

About