Dynamics of F-actin and F-actin/filamin networks as studied by photon correlation spectroscopy. 1990

J Seils, and B M Jockusch, and T Dorfmuller
Faculty of Chemistry, University of Bielefeld, Federal Republic of Germany.

Photon correlation spectroscopy was used to study both F-actin and F-actin/filamin networks in solution. The measured autocorrelation functions were analyzed with the inverse Laplace transform CONTIN. The resulting frequency distributions consist of maximal five relatively narrow peaks. This rather unexpected finding disagrees with the frequency spectra calculated for an entangled rigid rod model. For this model, we expect spectra consisting of a single broad peak. Factors like flexibility, deviation from an experimental length distribution, interference with chemical reactions, and translation-rotation coupling that would influence the profile of the frequency distribution could be excluded by comparison of the data with model calculations or qualitative estimates. We conclude that our data for F-actin are consistent with the dynamics of an infinite network stable on the time scale of the observed modes. Further support for this interpretation is provided by a comparison with frequency spectra of actin/filamin networks. These appear to be very similar in shape. The main peak of these spectra that corresponds to the slow motions shifts to lower frequencies with increasing cross-link density. It appears that higher frequency modes of the gel are more efficiently damped with progressive cross-link density, resulting in a predominance of the slow motions in the spectra. This behavior has been already found in other systems and seems to be a general feature of cross-linked systems.

UI MeSH Term Description Entries
D008433 Mathematics The deductive study of shape, quantity, and dependence. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed) Mathematic
D008840 Microfilament Proteins Monomeric subunits of primarily globular ACTIN and found in the cytoplasmic matrix of almost all cells. They are often associated with microtubules and may play a role in cytoskeletal function and/or mediate movement of the cell or the organelles within the cell. Actin Binding Protein,Actin-Binding Protein,Actin-Binding Proteins,Microfilament Protein,Actin Binding Proteins,Binding Protein, Actin,Protein, Actin Binding,Protein, Actin-Binding,Protein, Microfilament,Proteins, Actin-Binding,Proteins, Microfilament
D011827 Radiation Emission or propagation of acoustic waves (SOUND), ELECTROMAGNETIC ENERGY waves (such as LIGHT; RADIO WAVES; GAMMA RAYS; or X-RAYS), or a stream of subatomic particles (such as ELECTRONS; NEUTRONS; PROTONS; or ALPHA PARTICLES). Radiations
D003285 Contractile Proteins Proteins which participate in contractile processes. They include MUSCLE PROTEINS as well as those found in other cells and tissues. In the latter, these proteins participate in localized contractile events in the cytoplasm, in motile activity, and in cell aggregation phenomena. Contractile Protein,Protein, Contractile,Proteins, Contractile
D000199 Actins Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle. F-Actin,G-Actin,Actin,Isoactin,N-Actin,alpha-Actin,alpha-Isoactin,beta-Actin,gamma-Actin,F Actin,G Actin,N Actin,alpha Actin,alpha Isoactin,beta Actin,gamma Actin
D013057 Spectrum Analysis The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed) Spectroscopy,Analysis, Spectrum,Spectrometry
D064448 Filamins A family of crosslinking filament proteins encoded by distinct FLN genes. Filamins are involved in cell adhesion, spreading, and migration, acting as scaffolds for over 90 binding partners including channels, receptors, intracellular signaling molecules and transcription factors. Due to the range of molecular interactions, mutations in FLN genes result in anomalies with moderate to lethal consequences. 280 kDa Actin-Binding Protein,Filamin,Filamin 1,Filamin 1-Like Protein,Filamin A,Filamin B,Filamin C,Merofilamins,alpha-Filamin,beta-Filamin,1-Like Protein, Filamin,1-Like Proteins, Filamin,280 kDa Actin Binding Protein,Cs, Filamin,Filamin 1 Like Protein,Filamin 1-Like Proteins,Filamin Cs,Merofilamin,Protein, Filamin 1-Like,Proteins, Filamin 1-Like,alpha Filamin,alpha-Filamins,beta Filamin,beta-Filamins

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