5f2q

Structural highlights

Function

[LECG_BOTJR] Galactose-binding lectin which recognizes specific carbohydrate structures and agglutinates a variety of animal cells by binding to cell-surface glycoproteins and glycolipids. Calcium-dependent lectin. Shows high hemagglutinating activity. When injected into mouse hind paws, (10-100 ug/paw) causes edema and increases vascular permeability. In anesthetized rats, decreases the blood pressure by approximately 15%, with a rapid return to the resting level (PubMed:16309723). Is an effective inhibitor of cell growth in some cancer cell lines, especially against renal and pancreatic cancer cell lines, human breast and ovarian carcinoma, glioblastoma and a bovine brain microvascular endothelial cell line (PubMed:10628348, PubMed:11478954).^{[1] [2] [3] [4]}

References

1. ↑ Pereira-Bittencourt M, Carvalho DD, Gagliardi AR, Collins DC. The effect of a lectin from the venom of the snake, Bothrops jararacussu, on tumor cell proliferation. Anticancer Res. 1999 Sep-Oct;19(5B):4023-5. PMID:10628348
2. ↑ de Carvalho DD, Schmitmeier S, Novello JC, Markland FS. Effect of BJcuL (a lectin from the venom of the snake Bothrops jararacussu) on adhesion and growth of tumor and endothelial cells. Toxicon. 2001 Oct;39(10):1471-6. PMID:11478954
3. ↑ Panunto PC, da Silva MA, Linardi A, Buzin MP, Melo SE, Mello SM, Prado-Franceschi J, Hyslop S. Biological activities of a lectin from Bothrops jararacussu snake venom. Toxicon. 2006 Jan;47(1):21-31. Epub 2005 Nov 23. PMID:16309723 doi:http://dx.doi.org/10.1016/j.toxicon.2005.08.012
4. ↑ de Carvalho DD, Marangoni S, Novello JC. Primary structure characterization of Bothrops jararacussu snake venom lectin. J Protein Chem. 2002 Jan;21(1):43-50. PMID:11902666