Proteomic knowledge of human aquaporins
| Autor: | Niccolò Bosso, Fulvio Magni, Marzia Galli Kienle, Davide Ticozzi, Cecilia Sarto, Monica Soldi, Paolo Mocarelli |
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| Přispěvatelé: | Magni, F, Sarto, C, Ticozzi, D, Soldi, M, Bosso, N, Mocarelli, P, Kienle, M |
| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Proteomics BIO/12 - BIOCHIMICA CLINICA E BIOLOGIA MOLECOLARE CLINICA Molecular Sequence Data Aquaporin Computational biology Biology MED/46 - SCIENZE TECNICHE DI MEDICINA DI LABORATORIO Aquaporins Bioinformatics Biochemistry Genome Humans Electrophoresis Gel Two-Dimensional Amino Acid Sequence Spettrometria di massa carcinoma renale rene proteomica tumore Molecular Biology Peptide sequence Aquaporin 1 Sequence Homology Amino Acid Genome Human MED/04 - PATOLOGIA GENERALE Ms analysis Proteins Hydrogen-Ion Concentration BIO/10 - BIOCHIMICA Genetic translation Post translational Aquaporin 2 MED/24 - UROLOGIA Protein Processing Post-Translational |
| Zdroj: | PROTEOMICS. 6:5637-5649 |
| ISSN: | 1615-9861 1615-9853 |
| Popis: | Aquaporins (AQPs) are an ubiquitous family of proteins characterized by sequence similarity and the presence of two NPA (Asp-Pro-Ala) motifs. At present, 13 human AQPs are known and they are divided into two subgroups according to their ability to transport only water molecules (AQPO, AQP1, AQP2, AQP4, AQP5, AQP6, and AQP8), or also glycerol and other small solutes (AQP3, AQP7, AQP9, AQP10, AQP12). The genomic, structural, and functional aspects of this family are briefly described. In particular, proteomic approaches to identify and characterize the most studied AQPs, mainly through SDS-PAGE followed by MS analysis, are discussed. Moreover, the clinical importance of the best studied aquaporin (AQP1) in human diseases is also provided. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA. |
| Databáze: | OpenAIRE |
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