Purification and distribution of a lectin in sea urchin (Anthocidaris crassispina) egg before and after fertilization

Sasaki, Hajime; Aketa, Kenji

doi:10.1016/0014-4827(81)90294-9

Cited by 23 publications

(15 citation statements)

References 9 publications

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“…Serial 2-fold dilutions of 25 ml of the humoral fluids were made in V-bottom 96 well microtiter plates using 10 mM PBS (pH 7.4). Haemagglutinating activity against the fixed rabbit and human A, B and O erythrocytes was assayed using 1% erythrocyte suspensions [20]. Haemagglutination was scored after the microtiter plates were kept at room temperature for 1 h. The activity was expressed by titer defined as the reciprocal of the highest dilution giving positive haemagglutination.…”

Section: Haemagglutination Assaymentioning

confidence: 99%

Humoral immune responses of amphioxus Branchiostoma belcheri to challenge with Escherichia coli

Pang

Zhang

Liu

et al. 2006

Fish & Shellfish Immunology

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Section: Haemagglutination Assaymentioning

confidence: 99%

Humoral immune responses of amphioxus Branchiostoma belcheri to challenge with Escherichia coli

Pang

Zhang

Liu

et al. 2006

Fish & Shellfish Immunology

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“…A galactose-specific lectin has been described in the egg of the sea urchin Anthocidaris Crassispina (Sasaki and Aketa 1981). This molecule is composed of two monomers with a relative molecular weight of 11 500, which aggregate to form a dimer of 23 000.…”

Section: Fertilizationmentioning

confidence: 99%

On the possible role of endogenous lectins in early animal development

Zalik

1991

Anat Embryol

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In this review I have tried to summarize the information available on the lectins of developing embryos. The emerging evidence indicates that during fertilization carbohydrate-binding proteins play a role in sperm adhesion and in the reorganization of the extracellular matrix of the fertilized egg. Results also indicate that in adult tissues lectins participate in cell recognition and adhesion, and that several galactose-binding lectins function as receptors for laminin and, in principle could also interact with polylactosamine groups of other extracellular matrix glycoproteins. Since in developing embryos lectins are located at the cell surface, and colocalize with extracellular matrix glycoproteins, they could play a role in transitory adhesive interactions and in the segregation of organ primordia. On the basis of experiments in cultured cell lines, it has been suggested that lectins are involved in lysosomal and nuclear glycoprotein transport. These carbohydrate-binding proteins could also regulate development by modulating these processes in the embryo. Since galactose-binding lectins are mitogenic, and are present in high concentration in the chick yolk sac, these proteins could be released into the embryonic circulation, bind to cells expressing appropriate receptors, and act as growth regulators, by modulating cell division of specific cell lineages.

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“…However, the first RBL described, the sea urchin eggs lectin, or SUEL, was purified from eggs of the sea urchin Anthocidaris crassispina [13,14]. Also bivalves [12,15].…”

Section: Introductionmentioning

confidence: 99%

l-rhamnose-binding lectin from eggs of the Echinometra lucunter: Amino acid sequence and molecular modeling

Carneiro

Teixeira

Melo

et al. 2015

International Journal of Biological Macromolecules

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An L-rhamnose-binding lectin named ELEL was isolated from eggs of the rock boring sea urchin Echinometra lucunter by affinity chromatography on lactosyl-agarose. ELEL is a homodimer linked by a disulfide bond with subunits of 11 kDa each. The new lectin was inhibited by saccharides possessing the same configuration of hydroxyl groups at C-2 and C-4, such as L-rhamnose, melibiose, galactose and lactose. The amino acid sequence of ELEL was determined by tandem mass spectrometry. The ELEL subunit has 103 amino acids, including nine cysteine residues involved in four conserved intrachain disulfide bonds and one interchain disulfide bond. The full sequence of ELEL presents conserved motifs commonly found in rhamnose-binding lectins, including YGR, DPC and KYL. A three-dimensional model of ELEL was created, and molecular docking revealed favorable binding energies for interactions between ELEL and rhamnose, melibiose and Gb3 (Galα1-4Galβ1-4Glcβ1-Cer). Furthermore, ELEL was able to agglutinate Gram-positive bacterial cells, suggesting its ability to recognize pathogens.

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Purification and distribution of a lectin in sea urchin (Anthocidaris crassispina) egg before and after fertilization

Cited by 23 publications

References 9 publications

Humoral immune responses of amphioxus Branchiostoma belcheri to challenge with Escherichia coli

Humoral immune responses of amphioxus Branchiostoma belcheri to challenge with Escherichia coli

On the possible role of endogenous lectins in early animal development

l-rhamnose-binding lectin from eggs of the Echinometra lucunter: Amino acid sequence and molecular modeling

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