High-level expression and characterization of a glycosylated human cementum protein 1 with lectin activity
| Autor: | Enrique Romo-Arévalo, Higinio Arzate, Gonzalo Montoya-Ayala, Adela Rodríguez-Romero |
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| Rok vydání: | 2016 |
| Předmět: |
Erythrocyte Aggregation
0301 basic medicine Circular dichroism Glycosylation Hot Temperature Protein Conformation Recombinant Fusion Proteins Biophysics Biochemistry Pichia Protein Structure Secondary Pichia pastoris 03 medical and health sciences chemistry.chemical_compound Protein structure Structural Biology Gene Expression Regulation Fungal Lectins Genetics Animals Humans Molecular Biology Protein secondary structure Molecular mass biology Protein Stability Chemistry Circular Dichroism Proteins Biological activity Cell Biology biology.organism_classification Molecular Weight 030104 developmental biology Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Microscopy Electron Scanning Hydroxyapatites Rabbits Mannose Protein Processing Post-Translational |
| Zdroj: | FEBS Letters. 590:129-138 |
| ISSN: | 0014-5793 |
| Popis: | This work aims to contribute to the knowledge of human cementum protein 1 (CEMP1), its conformational characteristics and influence during the biomineralization process. The results revealed that hrCEMP1 expressed in Pichia pastoris is a 2.4% glycosylated, thermostable protein which possesses a molecular mass of 28,770 Da. The circular dichroism spectrum indicated a secondary structure content of 28.6% of alpha-helix, 9.9% of beta-sheet and 61.5% of random-coil forms. Biological activity assays demonstrated that hrCEMP1 nucleates and regulates hydroxyapatite crystal growth. Hereby, it is demonstrated for the first time that CEMP1 has a (C-type) lectin-like activity and specifically recognizes mannopyranoside. The information produced by this biochemical and structural characterization may contribute to understand more fully the biological functions of CEMP1. |
| Databáze: | OpenAIRE |
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