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Pavlova E.V.

Surgut Clinical Dermatovenerologic Dispensary, Surgut, Russia, 628403

Mihailov R.V.

Anterix, Moscow region, Russia

Kazakov A.S.

GKB #50, Moskva

Development of recombinant antibodies specific to galectin-3 by the phage display method for diagnostics and research purposes

Authors:

Pavlova E.V., Mihailov R.V., Kazakov A.S.

More about the authors

Journal: Laboratory Service. 2019;8(1): 81‑85

DOI: 10.17116/labs2019801181

Views: 999

Downloaded: 27

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To cite this article:

Pavlova EV, Mihailov RV, Kazakov AS. Development of recombinant antibodies specific to galectin-3 by the phage display method for diagnostics and research purposes. Laboratory Service. 2019;8(1):81‑85. (In Russ.)
https://doi.org/10.17116/labs2019801181

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ABSTRACT Galectin-3 (Gal-3) is 26 kDa galactoside-binding protein which found both inside the cell and in the extracellular space. Rise of Gal-3 level in serum significantly correlated with various pathologies, such as cancer, cardiac insufficiency and fibrosis. Despite the proven prognostic significance, the widespread measurement of the level of galectin-3 in the serum of patients in clinical practice is not yet been achieved. The purpose of this study was development of recombinant human antibodies specific to galectin-3 by phage display method. As a result four antibodies to gal-3 were obtained by the phage display method. Affinity of antibodies is from 9 nM to 120 pM. The presence of the sandwich-pair in obtained antibodies allows determining the concentration of galectin-3 in the solution by the method of enzyme immunoassay (ELISA).

Keywords:

galectin-3
antibodies
phage display
malignant tumors
fibrosis

Authors:

Pavlova E.V.

Surgut Clinical Dermatovenerologic Dispensary, Surgut, Russia, 628403

Mihailov R.V.

Anterix, Moscow region, Russia

Kazakov A.S.

GKB #50, Moskva

List of references:

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  2. Houzelstein D, Goncalves IR, Fadden AJ, Sidhu SS, Cooper DN, Drickamer K, Leffler H, Poirier. Phylogenetic analysis of the vertebrate galectin family. Mol Biol Evol. 2004 Jul;21(7):1177-1187. https://doi.org/10.1093/molbev/msh082
  3. Dumic J, Dabelic S, Flogel M. Galectin-3: an open-ended story. Biochemica and biophysica Acta. 2006 Apr;1760(4):616-635. https://doi.org/10.1016/j.bbagen.2005.12.020
  4. Shimura T, Shibata M, Gonda K, Nakajima T, Chida S, Noda M, Suzuki S, Nakamura I, Ohki S, Takenoshita S. Association between circulating galectin-3 levels and the immunological, inflammatory and nutritional parameters in patients with colorectal cancer. Biomed Rep. 2016 Aug;5(2):203-207. https://doi.org/10.3892/br.2016.696
  5. Traber P, Chou H, Zomer E, Hong F, Klyosov K, Frel MI, Friedman SL. Regression of fibrosis and reversal of cirrhosis in rats by galectin inhibitors in thioacetamide-induced liver disease. PLOS One. 2013 Oct 9;8(10):e75361. https://doi.org/10.1371/journal.pone.0075361
  6. Kramer F. Galectin-3: clinical utility and prognostic value in patients with heart failure. Research reports in Clinical Cardiology. 2013;4:13-22. https://doi.org/10.2147/RRCC.S28562
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  9. Connie Arthur M, Cataldi Rodrigues L, Dias Baruffi M, Harold Sullivan C, Heimburg-Molinaro J, Dave Smith F, Richard Cummings D, Sean Stowell R. Examining Galectin Binding Specificity Using Glycan Microarrays. Methods Mol Biol. 2015;1207:115-131. https://doi.org/10.1007/978-1-4939-1396-1_8
  10. Barbas CFI, Burton DR, Silverman GJ. Phage Display: A Laboratory Manual. New York, NY: Cold Spring Harbor. 2001.
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