Protein-mediated surface structuring in biomembranes
| Autor: | Bruno Maggio, M. Del Boca, Carla M. Rosetti, Graciela A. Borioli, Maria Laura Fanani |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2005 |
| Předmět: |
Surface (mathematics)
Proteolipid protein 1 Proto-Oncogene Proteins c-jun Surface Properties Physiology Lipid monolayers Proteolipids Immunology Biophysics Context (language use) Biochemistry Anphitropic proteins Phase (matter) Humans General Pharmacology Toxicology and Pharmaceutics lcsh:QH301-705.5 c-Fos lcsh:R5-920 Membranes biology Chemistry General Neuroscience Membrane Proteins Cell Biology General Medicine Segregated lipid domains Electrostatics Myelin basic protein Membrane lcsh:Biology (General) biology.protein Thermodynamics Sphingomyelinase Sphingomyelin Lipid-protein interaction lcsh:Medicine (General) Proto-Oncogene Proteins c-fos Myelin Proteins |
| Zdroj: | Brazilian Journal of Medical and Biological Research, Vol 38, Iss 12, Pp 1735-1748 (2005) Brazilian Journal of Medical and Biological Research, Volume: 38, Issue: 12, Pages: 1735-1748, Published: DEC 2005 Brazilian Journal of Medical and Biological Research v.38 n.12 2005 Brazilian Journal of Medical and Biological Research Associação Brasileira de Divulgação Científica (ABDC) instacron:ABDC |
| ISSN: | 0034-7310 |
| Popis: | The lipids and proteins of biomembranes exhibit highly dissimilar conformations, geometrical shapes, amphipathicity, and thermodynamic properties which constrain their two-dimensional molecular packing, electrostatics, and interaction preferences. This causes inevitable development of large local tensions that frequently relax into phase or compositional immiscibility along lateral and transverse planes of the membrane. On the other hand, these effects constitute the very codes that mediate molecular and structural changes determining and controlling the possibilities for enzymatic activity, apposition and recombination in biomembranes. The presence of proteins constitutes a major perturbing factor for the membrane sculpturing both in terms of its surface topography and dynamics. We will focus on some results from our group within this context and summarize some recent evidence for the active involvement of extrinsic (myelin basic protein), integral (Folch-Lees proteolipid protein) and amphitropic (c-Fos and c-Jun) proteins, as well as a membrane-active amphitropic phosphohydrolytic enzyme (neutral sphingomyelinase), in the process of lateral segregation and dynamics of phase domains, sculpturing of the surface topography, and the bi-directional modulation of the membrane biochemical reactivity. |
| Databáze: | OpenAIRE |
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