Poly(ADP-ribosyl)ation of mannose-binding lectin out of human kidney cells

• Published in: Molecular and cellular biochemistry Vol. 352; no. 1-2; pp. 231 - 238
• Main Authors: Sidorova, Natalie N., Kurchashova, Svetlana Yu, Yarahmedov, Tural Ya, Ziganshin, Rustam H., Kuimov, Alexander N.
• Format: Journal Article
• Language: English
• Published: Boston Springer US 01.06.2011; Springer Nature B.V
• Subjects: Adenosine diphosphate; Binding sites; Biochemistry; Biomedical and Life Sciences; Blotting, Western; Cardiology; Cell Line; Chromatography, Affinity - methods; Cytoplasm; Electrophoresis, Polyacrylamide Gel; Humans; Kidney - cytology; Kidney - metabolism; Kidneys; Life Sciences; Mannose-Binding Lectin - metabolism; Mass Spectrometry; Medical Biochemistry; Oncology; Poly Adenosine Diphosphate Ribose - metabolism; Proteins; Posttranslational modification; Tankyrase 2; Keratin 1; Poly(ADP-ribosyl)ation; Mannose-binding lectin
• ISSN: 0300-8177; 1573-4919
• DOI: 10.1007/s11010-011-0758-9

Mannose-binding lectin was identified as a substrate of tankyrase 2, an enzyme that catalyzes poly(ADP-ribosyl)ation. The endogenous tankyrase 2 was isolated out of cytoplasm of human embryonic kidney cells. It was bound to a soluble complex of at least two other proteins; they were identified using specific antibodies and other approaches as keratin 1 and mannose-binding lectin. Using immunoblot analysis and radioactive labeling, we detected tankyrase-2-dependent poly(ADP-ribosyl)ation of mannose-binding lectin. In the presence of NAD + , the complex of keratin 1 and lectin was dissociated, what was recorded during elution of its separate components out of affinity columns and by decrease of their apparent molecular masses during gel-filtration. Tankyrase 2 also inhibited the carbohydrate-binding function of the lectin. The latter effect was observed using mannose-binding lectin out of human serum, which is free from keratin 1. As a result of tankyrase-2 activity, the lectin lost its affinity to mannan-agarose. The discovery of this new biochemical mechanism justifies further analysis of its physiological and medical significance.