scholarly journals Diversified Biomineralization Roles of Pteria penguin Pearl Shell Lectins as Matrix Proteins

2021 ◽  
Vol 22 (3) ◽  
pp. 1081
Author(s):  
Tomohisa Ogawa ◽  
Rie Sato ◽  
Takako Naganuma ◽  
Kayeu Liu ◽  
Saho Sato ◽  
...  
Keyword(s):  
Matrix Proteins ◽  
Carbohydrate Binding ◽  
Data Sets ◽  
Shell Formation ◽  
Binding Properties ◽  
Chromatography Analysis ◽  
Pteria Penguin ◽  
Lectin Family ◽  
Chitin Oligomer ◽  
Mollusk Shell

Previously, we isolated jacalin-related lectins termed PPL2, PPL3 (PPL3A, 3B and 3C) and PPL4 from the mantle secretory fluid of Pteria penguin (Mabe) pearl shell. They showed the sequence homology with the plant lectin family, jacalin-related β-prism fold lectins (JRLs). While PPL3s and PPL4 shared only 35%–50% homology to PPL2A, respectively, they exhibited unique carbohydrate binding properties based on the multiple glycan-binding profiling data sets from frontal affinity chromatography analysis. In this paper, we investigated biomineralization properties of these lectins and compared their biomineral functions. It was found that these lectins showed different effects on CaCO3 crystalization, respectively, although PPL3 and PPL2A showed similar carbohydrate binding specificities. PPL3 suppressed the crystal growth of CaCO3 calcite, while PPL2A increased the number of contact polycrystalline calcite composed of more than one crystal with various orientations. Furthermore, PPL4 alone showed no effect on CaCO3 crystalization; however, PPL4 regulated the size of crystals collaborated with N-acetyl-D-glucosamine and chitin oligomer, which are specific in recognizing carbohydrates for PPL4. These observations highlight the unique functions and molecular evolution of this lectin family involved in the mollusk shell formation.

scholarly journals Glycan Binding Profiling of Jacalin-Related Lectins from the Pteria Penguin Pearl Shell

2019 ◽  
Vol 20 (18) ◽  
pp. 4629
Author(s):  
Tomohisa Ogawa ◽  
Rie Sato ◽  
Takako Naganuma ◽  
Kayeu Liu ◽  
Agness Ethel Lakudzala ◽  
...  
Keyword(s):  
Matrix Protein ◽  
Binding Specificity ◽  
The Other ◽  
Carbohydrate Binding ◽  
Sequence Variants ◽  
Data Sets ◽  
Binding Properties ◽  
Chromatography Analysis ◽  
Pteria Penguin ◽  
High Mannose

We determined the primary structures of jacalin-related lectins termed PPL3s (PPL3A, 3B, and 3C, which are dimers consisting of sequence variants α + α, α + β, β + β, respectively) and PPL4, which is heterodimer consisting of α + β subunits, isolated from mantle secretory fluid of Pteria penguin (Mabe) pearl shell. Their carbohydrate-binding properties were analyzed, in addition to that of PPL2A, which was previously reported as a matrix protein. PPL3s and PPL4 shared only 35–50% homology to PPL2A, respectively; they exhibited significantly different carbohydrate-binding specificities based on the multiple glycan binding profiling data sets from frontal affinity chromatography analysis. The carbohydrate-binding specificity of PPL3s was similar to that of PPL2A, except only for Man3Fuc1Xyl1GlcNAc2 oligosaccharide, while PPL4 showed different carbohydrate-binding specificity compared with PPL2A and PPL3s. PPL2A and PPL3s mainly recognize agalactosylated- and galactosylated-type glycans. On the other hand, PPL4 binds to high-mannose-and hybrid-type N-linked glycans but not agalactosylated- and galactosylated-type glycans.

scholarly journals Galectin-3 as a Potential Target to Prevent Cancer Metastasis

2015 ◽  
Vol 9 ◽  
pp. CMO.S29462 ◽  
Author(s):  
Hafiz Ahmed ◽  
Dina M. M. Alsadek
Keyword(s):  
Cancer Progression ◽  
Growth Regulation ◽  
Cancer Metastasis ◽  
Carbohydrate Binding ◽  
Biological Processes ◽  
Binding Properties ◽  
Galectin 3 ◽  
Carbohydrate Ligands ◽  
Lectin Family ◽  
Binding Lectin

Interactions between two cells or between cell and extracellular matrix mediated by protein–carbohydrate interactions play pivotal roles in modulating various biological processes such as growth regulation, immune function, cancer metastasis, and apoptosis. Galectin-3, a member of the β-galactoside-binding lectin family, is involved in fibrosis as well as cancer progression and metastasis, but the detailed mechanisms of its functions remain elusive. This review discusses its structure, carbohydrate-binding properties, and involvement in various aspects of tumorigenesis and some potential carbohydrate ligands that are currently investigated to block galectin-3 activity.

scholarly journals Activity Dependence of a Novel Lectin Family on Structure and Carbohydrate-Binding Properties

Molecules ◽  
2019 ◽  
Vol 25 (1) ◽  
pp. 150 ◽  
Author(s):  
Irina Chikalovets ◽  
Alina Filshtein ◽  
Valentina Molchanova ◽  
Tatyana Mizgina ◽  
Pavel Lukyanov ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Diagnostic Tools ◽  
Carbohydrate Binding ◽  
Mytilus Trossulus ◽  
Amino Acid Sequence Analysis ◽  
Binding Properties ◽  
Lectin Family ◽  
Activity Dependence ◽  
Antiproliferative Activities

A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus. Amino acid sequence analysis of these lectins showed that they, together with another lectin MytiLec-1, formed a novel lectin family, adopting β-trefoil fold. In this mini review we discuss the structure, oligomerization, and carbohydrate-binding properties of a novel lectin family. We describe also the antibacterial, antifungal, and antiproliferative activities of these lectins and report about dependence of activities on molecular properties. Summarizing, CGL, MTL, and MytiLec-1 could be involved in the immunity in mollusks and may become a basis for the elaboration of new diagnostic tools or treatments for a variety of cancers.

scholarly journals Carbohydrate binding properties of complex-type oligosaccharides on immobilized Datura stramonium lectin.

1987 ◽  
Vol 262 (4) ◽  
pp. 1602-1607 ◽  
Author(s):  
K Yamashita ◽  
K Totani ◽  
T Ohkura ◽  
S Takasaki ◽  
I J Goldstein ◽  
...  
Keyword(s):  
Datura Stramonium ◽  
Carbohydrate Binding ◽  
Complex Type ◽  
Binding Properties

scholarly journals The chitin synthase involved in marine bivalve mollusk shell formation contains a myosin domain

FEBS Letters ◽  
2006 ◽  
Vol 580 (7) ◽  
pp. 1846-1852 ◽  
Author(s):  
Ingrid M. Weiss ◽  
Veronika Schönitzer ◽  
Norbert Eichner ◽  
Manfred Sumper
Keyword(s):  
Bivalve Mollusk ◽  
Chitin Synthase ◽  
Marine Bivalve ◽  
Shell Formation ◽  
Mollusk Shell

Expression of Winged Bean Basic Agglutinin in Spodoptera frugiperda Insect Cell Expression System

2001 ◽  
Vol 21 (3) ◽  
pp. 361-367 ◽  
Author(s):  
V. R. Srinivas ◽  
Kiran Bachhawat-Sikder ◽  
Saman Habib ◽  
Seyed E. Hasnain ◽  
Avadhesha Surolia
Keyword(s):  
Spodoptera Frugiperda ◽  
Expression System ◽  
Recombinant Baculovirus ◽  
Winged Bean ◽  
Carbohydrate Binding ◽  
Binding Properties ◽  
Insect Cell Expression System ◽  
Cell Expression ◽  
Insect Cell Expression ◽  
Cell Expression System

In this paper we report the successful expression of the winged bean basic agglutinin (WBA I) in insect cells infected with a recombinant baculovirus carrying the WBA I gene and its characterization in terms of its carbohydrate binding properties. The expressed protein appears to have a lower molecular weight than the native counterpart which is consistent with the lack of glycosylation of the former. Moreover, the expressed protein maintains its dimeric nature. Hence, a role for glycosylation in modulation of dimerization of WBA I is ruled out unlike Erythrina corallodendron (EcorL). Despite this the protein is active, with its sugar specificity unaltered.

scholarly journals Shell matrix proteins of the clam, Mya truncata: Roles beyond shell formation through proteomic study

2016 ◽  
Vol 27 ◽  
pp. 69-74 ◽  
Author(s):  
Jaison Arivalagan ◽  
Benjamin Marie ◽  
Victoria A. Sleight ◽  
Melody S. Clark ◽  
Sophie Berland ◽  
...  
Keyword(s):  
Matrix Proteins ◽  
Shell Formation ◽  
Shell Matrix ◽  
Proteomic Study ◽  
Shell Matrix Proteins
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