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Poly(ADP-ribosyl)ation of Mannose-Binding Lectin Out of Human Kidney Cells

Poly(ADP-ribosyl)ation of Mannose-Binding Lectin Out of Human Kidney Cells

Natalie N Sidorova, Svetlana Yu Kurchashova, Tural Ya Yarahmedov, Rustam H Ziganshin, Alexander N Kuimov

Mol Cell Biochem. 2011 Jun;352(1-2):231-8.

PMID: 21380727

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42410968	Mannan−Agarose			Price

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