Molecular Characterization and Mitogenic Activity of a Lectin from Purse Crab Philyra Pisum

Na, Jong Cheon; Park, Byung Tae; Chung, Woo Hyuk; Kim, Ha Hyung

doi:10.4196/kjpp.2011.15.4.241

Cited by 7 publications

(2 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Hemolymph was prepared from P. pisum and the PPL was purified from this hemolymph as described previously [ 13 , 14 ]. The concentration of the purified lectin was determined by the Bradford assay [ 15 ] using bovine serum albumin (Bio-Rad, Hercules, CA, USA) as the standard.…”

Section: Methodsmentioning

confidence: 99%

“…Our previous investigation indicated that P. pisum lectin (PPL), which has a molecular mass of 24,060 Da and is obtained from the hemolymph of P. pisum , exhibits hemagglutination and antiproliferative activities in human lung cancer cells [ 13 ]. The molecular characterization of PPL including its molecular mass, p I value, amino acid sequences, amino acid composition, and effects of pH, temperature, and metal ions on its activity as well as mitogenic activities on human lymphocytes were also investigated [ 14 ].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Binding Specificity ofPhilyra pisumLectin to Pathogen-Associated Molecular Patterns, and Its Secondary Structure

Park

Kim

Park

et al. 2013

Korean J Physiol Pharmacol

Self Cite

View full text Add to dashboard Cite

We recently reported a Philyra pisum lectin (PPL) that exerts mitogenic effects on human lymphocytes, and its molecular characterization. The present study provides a more detailed characterization of PPL based on the results from a monosaccharide analysis indicating that PPL is a glycoprotein, and circular dichroism spectra revealing its estimated α-helix, β-sheet, β-turn, and random coil contents to be 14.0%, 39.6%, 15.8%, and 30.6%, respectively. These contents are quite similar to those of deglycosylated PPL, indicating that glycans do not affect its intact structure. The binding properties to different pathogen-associated molecular patterns were investigated with hemagglutination inhibition assays using lipoteichoic acid from Gram-positive bacteria, lipopolysaccharide from Gram-negative bacteria, and both mannan and β-1,3-glucan from fungi. PPL binds to lipoteichoic acids and mannan, but not to lipopolysaccharides or β-1,3-glucan. PPL exerted no significant antiproliferative effects against human breast or bladder cancer cells. These results indicate that PPL is a glycoprotein with a lipoteichoic acid or mannan-binding specificity and which contains low and high proportions of α-helix and β-structures, respectively. These properties are inherent to the innate immune system of P. pisum and indicate that PPL could be involved in signal transmission into Gram-positive bacteria or fungi.

show abstract

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Binding Specificity ofPhilyra pisumLectin to Pathogen-Associated Molecular Patterns, and Its Secondary Structure

Park

Kim

Park

et al. 2013

Korean J Physiol Pharmacol

Self Cite

View full text Add to dashboard Cite

show abstract

Investigation of Lectins from Anomuran and Brachyuran Crabs

Silvester¹,

Adimy²,

Chellappa³

et al. 2022

Aquatic Lectins

View full text Add to dashboard Cite

Internalization of a novel, huge lectin from Ibacus novemdentatus (slipper lobster) induces apoptosis of mammalian cancer cells

et al. 2016

View full text Add to dashboard Cite

An N-acetyl sugar-binding lectin (termed iNoL) displaying cytotoxic activity against human cancer cells was isolated from the slipper lobster Ibacus novemdentatus (family Scyllaridae). iNoL recognized monosaccharides containing N-acetyl group, and glycoproteins (e.g., BSM) containing oligosaccharides with N-acetyl sugar. iNoL was composed of five subunits (330, 260, 200, 140, and 30 kDa), which in turn consisted of 70-, 40-, and 30-kDa polypeptides held together by disulfide bonds. Electron microscopic observations and gel permeation chromatography indicated that iNoL was a huge (500-kDa) molecule and had a polygonal structure under physiological conditions. iNoL displayed cytotoxic (apoptotic) effects against human cancer cell lines MCF7 and T47D (breast), HeLa (ovarian), and Caco2 (colonic), through incorporation (internalization) into cells. The lectin was transported into lysosomes via endosomes. Its cytotoxic effect and incorporation into cells were inhibited by the co-presence of N-acetyl-D-mannosamine (ManNAc). Treatment of HeLa cells with iNoL resulted in DNA fragmentation and chromatin condensation, through activation of caspase-9 and -3. In summary, the novel crustacean lectin iNoL is incorporated into mammalian cancer cells through glycoconjugate interaction, and has cytotoxic (apoptotic) effects.

show abstract

Molecular Characterization and Mitogenic Activity of a Lectin from Purse Crab Philyra Pisum

Cited by 7 publications

References 18 publications

Binding Specificity ofPhilyra pisumLectin to Pathogen-Associated Molecular Patterns, and Its Secondary Structure

Binding Specificity ofPhilyra pisumLectin to Pathogen-Associated Molecular Patterns, and Its Secondary Structure

Investigation of Lectins from Anomuran and Brachyuran Crabs

Internalization of a novel, huge lectin from Ibacus novemdentatus (slipper lobster) induces apoptosis of mammalian cancer cells

Contact Info

Product

Resources

About