ACL-I, a lectin from the marine sponge Axinella corrugata: Isolation, characterization and chemotactic activity

Dresch, Roger Remy; Zanetti, Gilberto Dolejal; Lerner, Cléa; Mothes, Beatriz; Trindade, Vera Maria Treis; Henriques, Amélia T.; Vozari-Hampe, Magdolna M.

doi:10.1016/j.cbpc.2008.03.003

Cited by 24 publications

(31 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Furthermore, similar to other lectins from marine invertebrates (Moura et al 2006, Dresch et al 2008, optimal activity of CvL-2 was observed in neutral pH, probably because that pH represents the natural environment of sponges.…”

Section: Discussionmentioning

confidence: 84%

See 1 more Smart Citation

Hemagglutinating/Hemolytic activities in extracts of marine invertebrates from the Brazilian coast and isolation of two lectins from the marine sponge Cliona varians and the sea cucumber Holothuria grisea

Moura

Melo

Carneiro

et al. 2015

An. Acad. Bras. Ciênc.

View full text Add to dashboard Cite

Twenty species of marine invertebrates from the Brazilian coast were screened for hemagglutinating/ hemolytic activity. In at least twelve tested species, hemagglutinating activity was different for different blood types, suggesting the presence of lectins. Extracts from four species showed hemolytic activity. Two new lectins were purified from the marine sponge Cliona varians (CvL-2) and sea cucumber Holothuria grisea (HGL). CvL-2 was able to agglutinate rabbit erythrocytes and was inhibited by galactosides. The hemagglutinating activity was optimal in pH neutral and temperatures below 70 °C. CvL-2 is a trimeric protein with subunits of 175 kDa. On the other hand, HGL showed both hemagglutinating and hemolytic activity in human and rabbit erythrocytes, but hemolysis could be inhibited by osmotic protection, and agglutination was inhibited by mucin. HGL was stable in pH values ranging from 4 to 10 and temperatures up to 90 °C. In electrophoresis and gel filtration, HGL was a monomeric protein with 15 kDa. CvL-2 and HGL showed different levels of toxicity to Artemia naplii. CvL-2 showed LC 50 of 850.1 μg/mL, whereas HGL showed LC 50 of 9.5 µg/mL.

show abstract

Section: Discussionmentioning

confidence: 84%

“…Like CvL-2, a considerable number of lectins isolated from marine sponges, agglutinate proteasetreated rabbit erythrocytes (Miarrons and Fresno 2000, Pajic et al 2002, Dresch et al 2008). CvL-2 was inhibited by diverse galactosides and PSM.…”

Section: Discussionmentioning

confidence: 99%

Hemagglutinating/Hemolytic activities in extracts of marine invertebrates from the Brazilian coast and isolation of two lectins from the marine sponge Cliona varians and the sea cucumber Holothuria grisea

Moura

Melo

Carneiro

et al. 2015

An. Acad. Bras. Ciênc.

View full text Add to dashboard Cite

show abstract

“…Another method used for lectin isolation, based on immobilized glycoprotein ligands, is affinity chromatography on agarose-immobilized porcine (Sus scrofa) blood plasma proteins (Kajiya et al, 2003) or on stroma (Alpuche et al, 2010;Dresch et al, 2008;Vazquez et al, 1993;Veau et al, 1999) or membranes (Castillo-Villanueva et al, 2007) of various erythrocytes, fixed with 1 % glutaraldehyde and physically entrapped in various matrices.…”

Section: Glycoproteinsmentioning

confidence: 99%

“…Several authors have purified lectins from a variety of sources using serial carbohydrate affinity chromatography (Chen et al, 1999;Kato et al, 2011;Lavanya Latha et al, 2006;Moreira et al, 1998;Ooi et al, 2002;Pohleven et al, 2011;Trindade et al, 2006) or Ultrogel-A4 agarose beads to remove non-specific agarose-binding proteins from the extract prior to subjecting it to carbohydrate affinity chromatography (Kvennefors et al, 2008). In contrast, nonpolysaccharide matrices, such as silica carriers (Synsorb) (Kaur et al, 2006;Mo et al, 2000;Naeem et al, 2007b;Shangary et al, 1995), poly(2-hydroxyethyl methacrylate) matrix of Spheron 300 (Nahálková et al, 2001), fractogel affinity matrix (Guzmán-Partida et al, 2004) or polyacrylamide beads (Dresch et al, 2008;Hořejší & Kocourek, 1978;Veau et al, 1999), can be used to avoid non-specific binding of lectins to the polysaccharide matrix.…”

Section: Adsorbent Matricesmentioning

confidence: 99%

Affinity Chromatography of Lectins

Pohleven¹,

Štrukelj²,

Kos³

2012

Affinity Chromatography

View full text Add to dashboard Cite

“…Sea worm Serpula vermicularis GlcNAc binding lectin was determined to be effective in inhibiting HIV-1 infection [20]. Marine sponge Axinella corrugate-1 is a GlcNAc binding lectin showing chemotactic effect on rat neutrophil [21], and was utilized in staining various cancer cells [22]. Abnormal GlcNAc glycosylation has been identified as a cancer maker [23], and utilized in bladder cancer targeting drug delivery [24] and cancer cell staining [22].…”

Section: Introductionmentioning

confidence: 99%

Ulva pertusa lectin 1 delivery through adenovirus vector affects multiple signaling pathways in cancer cells

Zhao

et al. 2017

Glycoconj J

View full text Add to dashboard Cite

Ulva pertusa lectin 1 (UPL1) is a N-acetyl-D-glucosamine (GlcNAc) binding lectin in marine green alga Ulva pertusa. Exogenous UPL1 colocalized with protein arginine methyltransferase 5 (PRMT5), methylosome protein 50 (MEP50), β-actin and β-tubulin, indicating the interaction of UPL1 with the methylosome and cytoskeleton. UPL1 delivery through adenovirus vector (Ad-UPL1) dramatically induced extracellularly regulated protein kinases 1/2 (ERK1/2) phosphorylation in liver cancer cell lines BEL-7404 and Huh7. Signaling pathways including p38 mitogen-activated protein kinase (MAPK), and Akt were also affected by Ad-UPL1 in a cell type dependent manner. MEK1/2 inhibitor U0126, as well as to a lesser extent p38 MAPK inhibitor SB203580 and phosphoinositide 3-kinase (PI3K) inhibitor LY294002, completely eliminated a higher molecular weight isoform of β-tubulin induced by Ad-UPL1, and significantly enhanced the cytotoxicity of Ad-UPL1 in Huh7 cells, suggesting that the inhibition of MEK1/2, p38 MAPK, and PI3K enhanced antiproliferative effect of Ad-UPL1 possibly through regulating the modification of β-tubulin. Ad-UPL1 completely inhibited the expression of autophagy-related factor Beclin1, but induced LC3-II expression in Huh7 cells. In addition, Ad-UPL1 significantly enhanced starvation induced survival suppression in Huh7 cells. Our data elucidated intracellular signaling pathways affected by exogenous UPL1, and may provide insights into a novel way of UPL1 delivery through adenovirus vectors combined with survival signaling inhibitors for cancer treatment.

show abstract

ACL-I, a lectin from the marine sponge Axinella corrugata: Isolation, characterization and chemotactic activity

Cited by 24 publications

References 40 publications

Hemagglutinating/Hemolytic activities in extracts of marine invertebrates from the Brazilian coast and isolation of two lectins from the marine sponge Cliona varians and the sea cucumber Holothuria grisea

Hemagglutinating/Hemolytic activities in extracts of marine invertebrates from the Brazilian coast and isolation of two lectins from the marine sponge Cliona varians and the sea cucumber Holothuria grisea

Affinity Chromatography of Lectins

Ulva pertusa lectin 1 delivery through adenovirus vector affects multiple signaling pathways in cancer cells

Contact Info

Product

Resources

About