Diversified Biomineralization Roles of Pteria penguin Pearl Shell Lectins as Matrix Proteins
| Autor: | Kayeu Liu, Koji Muramoto, Takako Naganuma, Shizuka Sakaue, Tomohisa Ogawa, Rie Sato, Kyosuke Yoshimi, Makoto Osada, Saho Sato |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Carbohydrates Matrix (biology) chitin Oligomer Catalysis Homology (biology) Article Calcium Carbonate Inorganic Chemistry lcsh:Chemistry 03 medical and health sciences chemistry.chemical_compound Affinity chromatography Chitin Animal Shells Lectins Animals Protein Isoforms Physical and Theoretical Chemistry Amino Acids Molecular Biology lcsh:QH301-705.5 Spectroscopy pearl shell 030102 biochemistry & molecular biology biology Organic Chemistry Lectin General Medicine biology.organism_classification biomineralization Computer Science Applications Bivalvia 030104 developmental biology Phenotype chemistry Biochemistry lcsh:Biology (General) lcsh:QD1-999 Pteria penguin carbohydrate biology.protein lectin Plant Lectins Crystallization Biomineralization |
| Zdroj: | International Journal of Molecular Sciences Volume 22 Issue 3 International Journal of Molecular Sciences, Vol 22, Iss 1081, p 1081 (2021) |
| ISSN: | 1422-0067 |
| DOI: | 10.3390/ijms22031081 |
| Popis: | 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 &beta prism fold lectins (JRLs). While PPL3s and PPL4 shared only 35%&ndash 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. |
| Databáze: | OpenAIRE |
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