The present study was designed to investigate the presence of mannose binding lectin (ManBL) in the sera and tissue samples of patients with tumoral (benign & malignant) kidney in addition to patients with non tumoral kidney affection, in order to establish the possibility of using serum and tissue ManBL test for diagnosis and epidemiological testing of kidney cancers. Participants of the present study were 96 patients at the age range 12-80 years; they were attending by different hospitals in Najaf (basically) and Karbala, and 46 healthy individuals within the same age range of the studying patients groups. Specific hemagglutination activity levels were revealed a significant increased (p < 0.001) in the sera and tissues of the patients with the malignant tumors specimens in comparison to that of pathological controls and healthy individuals. Serum and tissue hemagglutination activity levels were significantly higher (p < 0.001) in patients with metastatic disease compared with patients with localized tumors. While, the levels of the hemagglutination activity were approximate at patients with the end malignant kidney tumors stages. Upon electrophoresis of the study samples, the results reflected presence of changes in some proteins and glycoproteins bands presents in these samples. Using hydrophobic affinity chromatography, ManBLs were purified from sera of malignant, benign kidney tumors and non tumoral kidney diseases in addition to healthy individuals groups. The purified lectins were found to be glycoprotein with 77.45 KD as an approximate molecular weight and its sugar content was equal to13.5%. The maximum concentration of purified ManBL was found at patients with malignant kidney tumors.The results revealed that the highest hemagglutination activity of purified ManBL occurred with O + RBCs, at pH 7.4, and 37˚C. ManBL (regardless of its origin) lost the hemagglutination activity, completely, in the presence of EDTA. A result that indicates that the present purified the human ManBLs is a calcium dependent type. EXPERIMENTAL Patient and Control IndividualsThe present study involved 96 patients (55 cases with malignant kidney tumors, 23 cases with benign kidney tumors, and 18 cases with non tumoral kidney diseases) with the age range 10-80 years, in addition to 46 healthy individuals, at the same age range.

The present study was designed to investigate lectins in sera of patients with kidney tumors, in addition to non tumoral kidney disease patients. Fifty five patients of malignant kidney tumors were enrolled in addition to 23 patients of benign kidney tumors, and 18 patients of non tumoral kidney diseases used as control groups, in addition to 46 healthy individuals were also investigated. The age of patients and healthy individuals were 10-90 years. The measurement of total serum proteins revealed significant (p < 0.001) decrease in patients of malignant tumors when compared with those of benign, non tumoral diseases, and healthy individuals. The conditions of the hemagglutination assay of serum lectin activity were optimized. They were Tris buffer of 20 mM and pH 7.4, 60 mM CaCl2, 800 µg of defatted serum, 30 ˚C for serum samples, 60 minutes for serum samples, and human blood of group A+ suspension with 1.4 optical density. The measurement of the specific hemagglutination activity of lectins demonstrated significant (p < 0.001) elevation in patients of malignant tumors when compared with those of other patients and healthy individuals. Lectin activity was pointed out to be significantly (r = 0.767 at p < 0.0005) positively correlated with stage of malignancies. The cutoff value of the specific hemagglutination activity was found to equal 6 SHU for discriminatory malignant kidney tumors. Serum lectins activity were indicated to be inhibited by galactose, mannose, lactose, and N-acetyl galactosamine. Purification of lectin from sera of patients with malignant kidney tumors by affinity chromatography with the use of silver stain revealed N-Acetyl Galactosamine Binding Lectin (GalNAcBL). The purified folds and the yield was 178 with 32.4%. The polyacrylamide gel electrophoresis (PAGE) of purified lectin demonstrated one band consisted lectin activity. The approximate molecular weight of GalNAcBL was determined and found to be 63.83. Purified lectin was characterized through the assessment of the capability to agglutinate RBCs, inhibition by EDTA, pH dependency, thermal dependent, and carbohydrate contents. GalNAcBL were observed to be calcium dependence lectins (C-type). These results suggest that the diagnosis of the specific hemagglutination activity of lectin is promising biomarker for discrimination of malignant kidney tumor patients and the purified lectin could be introduced in the field of biomarkers.

The present study was designed to investigate lectins in sera of patients with kidney tumors, in addition to non tumoral kidney disease patients. Fifty five patients of malignant kidney tumors were enrolled in addition to 23 patients of benign kidney tumors, and 18 patients of non tumoral kidney diseases used as control groups, in addition to 46 healthy individuals were also investigated. The age of patients and healthy individuals were 10-90 years. The measurement of total serum proteins revealed significant (p < 0.001) decrease in patients of malignant tumors when compared with those of benign, non tumoral diseases, and healthy individuals. The conditions of the hemagglutination assay of serum lectin activity were optimized. They were Tris buffer of 20 mM and pH 7.4, 60 mM CaCl2, 800 µg of defatted serum, 30 ˚C for serum samples, 60 minutes for serum samples, and human blood of group A+ suspension with 1.4 optical density. The measurement of the specific hemagglutination activity of lectins demonstrated significant (p < 0.001) elevation in patients of malignant tumors when compared with those of other patients and healthy individuals. Lectin activity was pointed out to be significantly (r = 0.767 at p < 0.0005) positively correlated with stage of malignancies. The cutoff value of the specific hemagglutination activity was found to equal 6 SHU for discriminatory malignant kidney tumors. Serum lectins activity were indicated to be inhibited by galactose, mannose, lactose, and N-acetyl galactosamine. Purification of lectin from sera of patients with malignant kidney tumors by affinity chromatography with the use of silver stain revealed N-Acetyl Galactosamine Binding Lectin (GalNAcBL). The purified folds and the yield was 178 with 32.4%. The polyacrylamide gel electrophoresis (PAGE) of purified lectin demonstrated one band consisted lectin activity. The approximate molecular weight of GalNAcBL was determined and found to be 63.83. Purified lectin was characterized through the assessment of the capability to agglutinate RBCs, inhibition by EDTA, pH dependency, thermal dependent, and carbohydrate contents. GalNAcBL were observed to be calcium dependence lectins (C-type). These results suggest that the diagnosis of the specific hemagglutination activity of lectin is promising biomarker for discrimination of malignant kidney tumor patients and the purified lectin could be introduced in the field of biomarkers.