| Autor: |
Maggio B; Departamento de Química Biológica, CIQUIBIC, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ciudad Universitaria, 5000 Córdoba, Argentina. bmaggio@dqb.icq.unc.edu.ar, Rosetti CM, Borioli GA, Fanani ML, Del Boca M |
| Jazyk: |
angličtina |
| Zdroj: |
Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas [Braz J Med Biol Res] 2005 Dec; Vol. 38 (12), pp. 1735-48. Date of Electronic Publication: 2005 Nov 09. |
| DOI: |
10.1590/s0100-879x2005001200002 |
| Abstrakt: |
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: |
MEDLINE |
| Externí odkaz: |
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