Abstract
A concise review is presented on the nature, possible origin and functional significance of cell surface receptor patterns in the plasma membrane of lymphoid cells. A special emphasize has been laid on the available methodological approaches, their individual virtues and sources of errors. Fluorescence energy transfer is one of the oldest available means for studying non-randomized co-distribution patterns of cell surface receptors. A detailed and critical description is given on the generation of two-dimensional cell surface receptor patterns based on pair-wise energy transfer measurements. A second hierarchical-level of receptor clusters have been described by electron and scanning force microscopies after immuno-gold-labeling of distinct receptor kinds. The origin of these receptor islands at a nanometer scale and island groups at a higher hierarchical (μm) level, has been explained mostly by detergent insoluble glycolipid-enriched complexes known as rafts, or detergent insoluble glycolipids (DIGs). These rafts are the most-likely organizational forces behind at least some kind of receptor clustering [K. Simons et al., Nature 387 (1997) 569]. These models, which have great significance in trans-membrane signaling and intra-membrane and intracellular trafficking, are accentuating the necessity to revisit the Singer-Nicolson fluid mosaic membrane model and substitute the free protein diffusion with a restricted diffusion concept [S.J. Singer et al., Science 175 (1972) 720]. Copyright (C) 1999 Elsevier Science B.V.
| Original language | English |
|---|---|
| Pages (from-to) | 99-108 |
| Number of pages | 10 |
| Journal | Biophysical Chemistry |
| Volume | 82 |
| Issue number | 2-3 |
| DOIs | |
| Publication status | Published - Dec 13 1999 |
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Keywords
- Cell-surface organization
- Electron microscopy
- Fluorescence energy transfer
- Receptor patterns
- Scanning force microscopy
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Physical and Theoretical Chemistry
Cite this
Two-dimensional receptor patterns in the plasma membrane of cells. A critical evaluation of their identification, origin and information content. / Damjanovich, S.; Bene, L.; Matkó, J.; Mátyus, L.; Krasznai, Z.; Szabó, Gábor; Pieri, Carlo; Gáspár, R.; Szöllősi, J.
In: Biophysical Chemistry, Vol. 82, No. 2-3, 13.12.1999, p. 99-108.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Two-dimensional receptor patterns in the plasma membrane of cells. A critical evaluation of their identification, origin and information content
AU - Damjanovich, S.
AU - Bene, L.
AU - Matkó, J.
AU - Mátyus, L.
AU - Krasznai, Z.
AU - Szabó, Gábor
AU - Pieri, Carlo
AU - Gáspár, R.
AU - Szöllősi, J.
PY - 1999/12/13
Y1 - 1999/12/13
N2 - A concise review is presented on the nature, possible origin and functional significance of cell surface receptor patterns in the plasma membrane of lymphoid cells. A special emphasize has been laid on the available methodological approaches, their individual virtues and sources of errors. Fluorescence energy transfer is one of the oldest available means for studying non-randomized co-distribution patterns of cell surface receptors. A detailed and critical description is given on the generation of two-dimensional cell surface receptor patterns based on pair-wise energy transfer measurements. A second hierarchical-level of receptor clusters have been described by electron and scanning force microscopies after immuno-gold-labeling of distinct receptor kinds. The origin of these receptor islands at a nanometer scale and island groups at a higher hierarchical (μm) level, has been explained mostly by detergent insoluble glycolipid-enriched complexes known as rafts, or detergent insoluble glycolipids (DIGs). These rafts are the most-likely organizational forces behind at least some kind of receptor clustering [K. Simons et al., Nature 387 (1997) 569]. These models, which have great significance in trans-membrane signaling and intra-membrane and intracellular trafficking, are accentuating the necessity to revisit the Singer-Nicolson fluid mosaic membrane model and substitute the free protein diffusion with a restricted diffusion concept [S.J. Singer et al., Science 175 (1972) 720]. Copyright (C) 1999 Elsevier Science B.V.
AB - A concise review is presented on the nature, possible origin and functional significance of cell surface receptor patterns in the plasma membrane of lymphoid cells. A special emphasize has been laid on the available methodological approaches, their individual virtues and sources of errors. Fluorescence energy transfer is one of the oldest available means for studying non-randomized co-distribution patterns of cell surface receptors. A detailed and critical description is given on the generation of two-dimensional cell surface receptor patterns based on pair-wise energy transfer measurements. A second hierarchical-level of receptor clusters have been described by electron and scanning force microscopies after immuno-gold-labeling of distinct receptor kinds. The origin of these receptor islands at a nanometer scale and island groups at a higher hierarchical (μm) level, has been explained mostly by detergent insoluble glycolipid-enriched complexes known as rafts, or detergent insoluble glycolipids (DIGs). These rafts are the most-likely organizational forces behind at least some kind of receptor clustering [K. Simons et al., Nature 387 (1997) 569]. These models, which have great significance in trans-membrane signaling and intra-membrane and intracellular trafficking, are accentuating the necessity to revisit the Singer-Nicolson fluid mosaic membrane model and substitute the free protein diffusion with a restricted diffusion concept [S.J. Singer et al., Science 175 (1972) 720]. Copyright (C) 1999 Elsevier Science B.V.
KW - Cell-surface organization
KW - Electron microscopy
KW - Fluorescence energy transfer
KW - Receptor patterns
KW - Scanning force microscopy
UR - http://www.scopus.com/inward/record.url?scp=0033552675&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033552675&partnerID=8YFLogxK
U2 - 10.1016/S0301-4622(99)00109-X
DO - 10.1016/S0301-4622(99)00109-X
M3 - Article
C2 - 17030342
AN - SCOPUS:0033552675
VL - 82
SP - 99
EP - 108
JO - Biophysical Chemistry
JF - Biophysical Chemistry
SN - 0301-4622
IS - 2-3
ER -