Study on FcγRn Electrochemical Receptor Sensor and Its Kinetics
Neonatal γ-immunoglobulin (IgG) Fc receptor (FcγRn) is a receptor that transports IgG across the intestinal mucosa, placenta, and mammary gland, ensuring the balance of IgG and albumin in the body. These functions of FcγRn depend on the intracellular signal transduction and activation caused by the...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-07-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/25/14/3206 |
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| author | Dandan Peng Dingqiang Lu Guangchang Pang |
| author_facet | Dandan Peng Dingqiang Lu Guangchang Pang |
| author_sort | Dandan Peng |
| collection | DOAJ |
| description | Neonatal γ-immunoglobulin (IgG) Fc receptor (FcγRn) is a receptor that transports IgG across the intestinal mucosa, placenta, and mammary gland, ensuring the balance of IgG and albumin in the body. These functions of FcγRn depend on the intracellular signal transduction and activation caused by the combination of its extracellular domain and IgG Fc domain. Nevertheless, there are still no kinetic studies on this interaction. Consequently, in the present study, we successfully constructed the human FcγRn (hFcγRn) electrochemical receptor sensor. The signal amplification system formed by chitosan nanogold-hFcγRn protein and horseradish peroxidase was used to simulate the cell signal amplification system in vivo, and the kinetic effects between seven IgG and hFcγRn receptors from different species were quantitatively measured. The results showed that the interaction of these seven IgGs with hFcγRn was similar to the catalytic kinetics of enzyme and substrate, and there was a ligand-receptor saturation effect. The order of the interconnect allosteric constants (K<sub>a</sub>), which is similar to the Michaelis constant (K<sub>m</sub>), was human IgG < bovine IgG < horse IgG < rabbit IgG < sheep IgG < donkey IgG < quail IgY. The results showed that hFcγRn had the strongest ability to transport human IgG, which was consistent with the evolution of the system. Therefore, our hFcγRn electrochemical receptor sensor can be used to measure and evaluate the interconnected allosteric network. It is also an essential parameter of the interaction between hFcγRn and different IgGs and, thus, provides a new detection and evaluation method for immunoemulsion, therapeutic monoclonal antibody therapy, heteroantibody treatment, and half-life research. |
| first_indexed | 2024-03-10T18:29:29Z |
| format | Article |
| id | doaj.art-4334b6b3d717497097c9ddc7bd6bd327 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T18:29:29Z |
| publishDate | 2020-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-4334b6b3d717497097c9ddc7bd6bd3272023-11-20T06:43:41ZengMDPI AGMolecules1420-30492020-07-012514320610.3390/molecules25143206Study on FcγRn Electrochemical Receptor Sensor and Its KineticsDandan Peng0Dingqiang Lu1Guangchang Pang2College of Biotechnology & Food Science, Tianjin University of Commerce, Tianjin 300314, ChinaCollege of Biotechnology & Food Science, Tianjin University of Commerce, Tianjin 300314, ChinaCollege of Biotechnology & Food Science, Tianjin University of Commerce, Tianjin 300314, ChinaNeonatal γ-immunoglobulin (IgG) Fc receptor (FcγRn) is a receptor that transports IgG across the intestinal mucosa, placenta, and mammary gland, ensuring the balance of IgG and albumin in the body. These functions of FcγRn depend on the intracellular signal transduction and activation caused by the combination of its extracellular domain and IgG Fc domain. Nevertheless, there are still no kinetic studies on this interaction. Consequently, in the present study, we successfully constructed the human FcγRn (hFcγRn) electrochemical receptor sensor. The signal amplification system formed by chitosan nanogold-hFcγRn protein and horseradish peroxidase was used to simulate the cell signal amplification system in vivo, and the kinetic effects between seven IgG and hFcγRn receptors from different species were quantitatively measured. The results showed that the interaction of these seven IgGs with hFcγRn was similar to the catalytic kinetics of enzyme and substrate, and there was a ligand-receptor saturation effect. The order of the interconnect allosteric constants (K<sub>a</sub>), which is similar to the Michaelis constant (K<sub>m</sub>), was human IgG < bovine IgG < horse IgG < rabbit IgG < sheep IgG < donkey IgG < quail IgY. The results showed that hFcγRn had the strongest ability to transport human IgG, which was consistent with the evolution of the system. Therefore, our hFcγRn electrochemical receptor sensor can be used to measure and evaluate the interconnected allosteric network. It is also an essential parameter of the interaction between hFcγRn and different IgGs and, thus, provides a new detection and evaluation method for immunoemulsion, therapeutic monoclonal antibody therapy, heteroantibody treatment, and half-life research.https://www.mdpi.com/1420-3049/25/14/3206γ-immunoglobulin (IgG)neonatal IgG Fc receptor (FcγRn)human FcγRn (hFcγRn) electrochemical receptor sensorinterconnected allosteric constants (Ka) |
| spellingShingle | Dandan Peng Dingqiang Lu Guangchang Pang Study on FcγRn Electrochemical Receptor Sensor and Its Kinetics Molecules γ-immunoglobulin (IgG) neonatal IgG Fc receptor (FcγRn) human FcγRn (hFcγRn) electrochemical receptor sensor interconnected allosteric constants (Ka) |
| title | Study on FcγRn Electrochemical Receptor Sensor and Its Kinetics |
| title_full | Study on FcγRn Electrochemical Receptor Sensor and Its Kinetics |
| title_fullStr | Study on FcγRn Electrochemical Receptor Sensor and Its Kinetics |
| title_full_unstemmed | Study on FcγRn Electrochemical Receptor Sensor and Its Kinetics |
| title_short | Study on FcγRn Electrochemical Receptor Sensor and Its Kinetics |
| title_sort | study on fcγrn electrochemical receptor sensor and its kinetics |
| topic | γ-immunoglobulin (IgG) neonatal IgG Fc receptor (FcγRn) human FcγRn (hFcγRn) electrochemical receptor sensor interconnected allosteric constants (Ka) |
| url | https://www.mdpi.com/1420-3049/25/14/3206 |
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