Lectin-enzyme immunoassay of transferrin sialovariants using immobilized antitransferrin and enzyme-labeled galactose-binding lectin from Ricinus communis

Pekelharing, J.M.; Vissers, P.M.A.M.; Peters, Hannelore; Leijnse, B.

doi:10.1016/0003-2697(87)90275-2

Cited by 17 publications

(5 citation statements)

References 11 publications

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“…A further potential problem is that it is possible that the lectin itself can bind to carbohydrate on the side chain Fc region of immunoglobulin using either configuration and give rise to even higher non specific binding. Various techniques have been proposed to overcome this problem including the use of affinity purified antibodies (Pekelharing et al, 1987;Suzuki et al, 1990) and chemical or enzymatic deglycosylation of the solid phase antibody (Kinoshita et Kottgen et al, 1988).…”

Section: Discussf Onmentioning

confidence: 99%

The development of a sialic acid specific lectin‐immunoassay for the measurement of human chorionic gonadotrophin glycoforms in serum and its application in normal and Down's syndrome pregnancies

Abushoufa¹,

Talbot²,

Brownbill³

et al. 2000

Clinical Endocrinology

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Section: Discussf Onmentioning

confidence: 99%

The development of a sialic acid specific lectin‐immunoassay for the measurement of human chorionic gonadotrophin glycoforms in serum and its application in normal and Down's syndrome pregnancies

Abushoufa¹,

Talbot²,

Brownbill³

et al. 2000

Clinical Endocrinology

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“…Lectin affinity chromatography was used to analyze these altered glycosylation patterns and the clinical use of this methodology was proposed in detecting changes in the carbohydrate structures of IgG resulting from diseases (38). An assay using antibodies to human transferrin and Ricinus communis agglutinin for detecting transferrin sialovariants has been reported (39). We sought a relationship between 0-glycosidic linkages and tumor-associated epitopes in serum IgAl and the utilization of lectins to discriminate between the altered IgAl carbohydrate structure and its normal structure.…”

Section: Discussionmentioning

confidence: 99%

IgA With altered carbohydrate structure as a tumor‐associated marker in serum of cancer patients

Henslee

Rittenhouse

Matias

et al. 1988

Clinical Laboratory Analysis

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Serum lgAl contains 0-linked carbohydrate structures, whereas other immunoglobulins contain only N-linked structures. An assay was developed which detects lgAl by measuring the DGalP(1-3) DGalNAc structures 0-linked to the lgAl hinge region. Fifty percent of the serum specimens from cancer patients tested were elevated compared to 1% of the total normal serum specimens tested by this assay. The assay combines antibody (antihuman IgA) and lectin and measures the DGalp(1-3)DGalNAc structure in the lgAl molecule accessible to lectin binding. Three lectins were compared-the lectins from Bauhinia purpurea alba, Maclura pomifera, and peanut agglutinin (PNA). PNA in the assay discriminated best between serum specimens from normal subjects and cancer patients and was chosen as the lectin component in the assay. The anti-lgA-PNA enzyme immunoassay was evaluated in a retrospective study of cancer patients. A panel of 845 serum specimens was tested and the results analyzed at three cutoff R values. The R value of a specimen is the ratio of the assay absorbance obtained for that test specimen with respect to the assay absorbance obtained for a pool of normal human sera. At a cutoff R value of 2.38, 1% normals and 26% benigns were elevated. The following cancer specimens had elevated R values: 52% lung, 60% colon, 43% head and neck, 35% breast, 64% kidney, 38% bladder, 43% prostate, 8% ovarian, and 67% pancreas. Further testing showed a significant percentage of serum specimens from patients with cirrhosis, pancreatitis, or ulcerative colitis also had elevated R values. No correlation of this assay was observed with CEA levels. The results suggest that the carbohydrate structure of serum lgAl is altered by malignancies and that measurement of this altered IgA may supplement CEA testing.

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“…Lectins, especially fucose‐specific lectins due to their sugar recognition property have been commonly used to monitor changes in fucosylation of plasma glycoproteins such as AFP, the most reliable and widely used tumour marker for the diagnosis of hepatocellular carcinoma. Enzyme‐linked immunosorbent assay (ELISA) employing an anti‐AFP antibody and a fucose‐specific lectin is a powerful tool for quantifying elevated levels of aberrantly glycosylated AFP in the serum, for clinical purposes 8,9 . Hence, fucose‐specific lectins such as Lens culinaris agglutinin (LCA), Aspergillus oryzae lectin (AOL) and Cephalosporium curvulum (CSL) are gaining clinical significance 10 .…”

Section: Introductionmentioning

confidence: 99%

The fucose‐specific lectin ANL from Aspergillus niger possesses anti‐cancer activity by inducing the intrinsic apoptosis pathway in hepatocellular and colon cancer cells

Jagadeesh

Belur

Campbell

2021

Cell Biochemistry & Function

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The L‐fucose‐specific lectin from Aspergillus niger (ANL), isolated from the corneal smears of a keratitis patient was reported earlier. Here, we examined the interaction of ANL with human hepatocellular and colon cancer cells, evaluated its anti‐cancer activity and diagnostic potential to detect aberrantly glycosylated tumour‐associated serum glycoproteins such as alpha‐fetoprotein (AFP). We observed that ANL strongly bound to both HepG2 and HT‐29 cell‐lines and this interaction was effectively blocked with L‐fucose and mucin in a dose and time‐dependent manner with an IC50 of 1.25 and 5 μg/mL for HepG2 and HT‐29 cells respectively at 48 hours. ANL treatment increased hypodiploidy and decreased the number of HepG2 cell in G0‐G1 phase at both 24 and 48 hours. Furthermore, ANL increased the level of apoptosis in both HepG2 and HT‐29 cells in a time‐dependent manner via enhanced production of reactive oxygen species and altered mitochondrial membrane potential, indicative of intrinsic apoptotis pathway activation. Immunoblot analysis confirmed the time‐dependent elevation of levels of cytochrome c, initiator caspase‐9 and activation of caspase‐3. ANL immunohistochemistry on colon cancer tissue and quantification of AFP in HCC patient serum samples by developing an ANL‐anti‐AFP antibody sandwich enzyme‐linked immunosorbent assay confirmed the diagnostic potential of ANL. Here, interaction of ANL with AFP could be effectively blocked in the presence of competing fucose‐bearing glycans. We found ANL to be more sensitive than Lens culinaris lectin, a well‐known fucose‐specific lectin and currently used diagnostic agent. ANL can be further explored as a diagnostic and anti‐cancer agent.

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Lectin-enzyme immunoassay of transferrin sialovariants using immobilized antitransferrin and enzyme-labeled galactose-binding lectin from Ricinus communis

Cited by 17 publications

References 11 publications

The development of a sialic acid specific lectin‐immunoassay for the measurement of human chorionic gonadotrophin glycoforms in serum and its application in normal and Down's syndrome pregnancies

The development of a sialic acid specific lectin‐immunoassay for the measurement of human chorionic gonadotrophin glycoforms in serum and its application in normal and Down's syndrome pregnancies

IgA With altered carbohydrate structure as a tumor‐associated marker in serum of cancer patients

The fucose‐specific lectin ANL from Aspergillus niger possesses anti‐cancer activity by inducing the intrinsic apoptosis pathway in hepatocellular and colon cancer cells

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