Iga binding lectins isolated from distinct artocarpus species demonstrate differential specificity

Hashim, Onn Haji; Ng, Chee Liang; Gendeh, G.; Jaafar, Mohd Iskandar Nik

doi:10.1016/0161-5890(91)90152-a

Cited by 28 publications

(19 citation statements)

References 15 publications

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“…Champedak lectin-C is a plant lectin that binds to the O -glycans of IgA1 similar to jacalin [8, 9]. In this study, we have demonstrated that the affinity of the champedak lectin-C to serum IgA1 was significantly weaker in patients with IgAN as compared to normal controls.…”

Section: Discussionmentioning

confidence: 48%

Neuraminidase Treatment Abrogates the Binding Abnormality of IgA1 from IgA Nephropathy Patients and the Differential Charge Distribution of Its α-Heavy Chains

Hashim¹,

Shuib²,

Chua³

2001

Nephron

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We have studied the interaction of the Gal-GalNAc-reactive champedak lectin-C with neuraminidase-treated and untreated IgA1 from IgA nephropathy patients. The binding ability of the lectin to untreated IgA1 from IgA nephropathy patients was significantly lower as compared to the untreated IgA1 from normal controls. This differential lectin-binding capacity was abrogated when the experiment was performed on neuraminidase-treated sera. Treatment of the serum IgA1 with neuraminidase also abrogated the differential charge distribution between the α-heavy chains of IgA nephropathy patients and normal controls.

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Section: Discussionmentioning

confidence: 48%

Neuraminidase Treatment Abrogates the Binding Abnormality of IgA1 from IgA Nephropathy Patients and the Differential Charge Distribution of Its α-Heavy Chains

Hashim¹,

Shuib²,

Chua³

2001

Nephron

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“…The lectin was chosen based on its specific interaction with O-glycans of glycoproteins [18]. Purity and specificity of the lectin were confirmed using previously described biochemical and immunochemical analyses [18][19][20]. Blots were developed using 3,3 0 -diaminobenzidine (BioRad Laboratories, Hercules, CA, USA).…”

Section: Western Blotting and Lectin Detectionmentioning

confidence: 99%

Expression of high‐abundance proteins in sera of patients with endometrial and cervical cancers: Analysis using 2‐DE with silver staining and lectin detection methods

2007

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The expression of high-abundance serum proteins in newly diagnosed patients with endometrial adenocarcinoma (EACa), squamous cell cervical carcinoma (SCCa) and cervical adenocarcinoma (ACCa), relative to control female subjects, was analyzed by subjecting serum samples to 2-DE followed by image analysis of the silver-stained protein profiles. The three cohorts of cancer patients demonstrated different altered expression of serum high-abundance proteins compared to negative control women. The expression of alpha1-antitrypsin, alpha1-B glycoprotein, cleaved high-molecular-weight kininogen (light chain) and antithrombin III were consistently altered in all the patients. However, clusterin was upregulated only in the patients with EACa, while those with SCCa and ACCa were typically characterized by the upregulated expression of zinc alpha-2-glycoprotein. The aberrant expression of selective serum proteins in the various cohorts of cancer patients was validated by competitive ELISA as well as by lectin detection. Analysis by using the champedak galactose binding lectin further highlighted an unidentified protein that may be differently glycosylated in the sera of the EACa patients that were studied.

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“…Champedak galactose-binding (CGB) lectin is a plant lectin that recognizes the core Galb1-3GalNAc structure of O-glycans of glycoproteins [7][8][9]. In our recent report, we have used the CGB lectin to detect O-glycosylated serum proteins that were separated by 2-DE and Western blotted onto NC membrane [10].…”

Section: Introductionmentioning

confidence: 99%

Lectin‐based electrophoretic analysis of the expression of the 35 kDa inter‐α‐trypsin inhibitor heavy chain H4 fragment in sera of patients with five different malignancies

et al. 2008

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A 35 kDa glycoprotein whose abundance was previously demonstrated to be enhanced in sera of patients with endometrial adenocarcinoma (n = 12), was isolated from pooled sera of three of the cancer patients using champedak galactose-binding lectin affinity chromatography in the present study. Subjecting it to 2-DE and MS/MS, the glycoprotein was identified as the O-glycosylated fragment of inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4). When compared to control sera (n = 17), expression of the 35 kDa ITIH4 cleavage fragment was demonstrated to be significantly enhanced in sera of patients with breast carcinoma (n = 10), epithelial ovarian carcinoma (n = 10), and germ cell ovarian carcinoma (n = 10) but not in patients with nasopharyngeal carcinoma (n = 13) and osteosarcoma (n = 7). The lectin-based electrophoretic bioanalytical method adopted in the present study may be used to assess the physiological relevance of ITIH4 fragmentation and its correlation with different malignancies, their stages and progression.

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Iga binding lectins isolated from distinct artocarpus species demonstrate differential specificity

Cited by 28 publications

References 15 publications

Neuraminidase Treatment Abrogates the Binding Abnormality of IgA1 from IgA Nephropathy Patients and the Differential Charge Distribution of Its α-Heavy Chains

Neuraminidase Treatment Abrogates the Binding Abnormality of IgA1 from IgA Nephropathy Patients and the Differential Charge Distribution of Its α-Heavy Chains

Expression of high‐abundance proteins in sera of patients with endometrial and cervical cancers: Analysis using 2‐DE with silver staining and lectin detection methods

Lectin‐based electrophoretic analysis of the expression of the 35 kDa inter‐α‐trypsin inhibitor heavy chain H4 fragment in sera of patients with five different malignancies

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