actin

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actin,

a protein abundantly present in many cells, especially muscle cells, that significantly contributes to the cell's structure and motility. Actin can very quickly assemble into long polymer rods called microfilaments. These microfilaments have a variety of roles—they form part of the cell's cytoskeleton, they interact with myosinmyosin
, one of the two major protein constituents responsible for contraction of muscle. In muscle cells myosin is arranged in long filaments called thick filaments that lie parallel to the microfilaments of actin.
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 to permit movement of the cell, and they pinch the cell into two during cell division. In muscle contraction, filaments of actin and myosin alternately unlink and chemically link in a sliding action. The energy for this reaction is supplied by adenosine triphosphateadenosine triphosphate
(ATP) , organic compound composed of adenine, the sugar ribose, and three phosphate groups. ATP serves as the major energy source within the cell to drive a number of biological processes such as photosynthesis, muscle contraction, and the synthesis of
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.

actin

[′ak·tən]
(biochemistry)
A muscle protein that is the chief constituent of the Z-band myofilaments of each sarcomere.
References in periodicals archive ?
Ueno, "Acceleration of actin polymerization and rapid microfilament reorganization in cultured hepatocytes by cyclochlorotin, a hepatotoxic cyclic peptide," Toxicon, vol.
Stoll et al., "Hepatocyte swelling leads to rapid decrease of the G-/total actin ratio and increases actin mRNA levels," FEBS Letters, vol.
The present report describes the isolation of actin gene (partial sequence) from T.
The plasmid pTZ57R/T (Fermentas) containing ampicillin resistance gene and was used for cloning of actin gene.
In the presence of [Ca.sup.2+], gelsolin severs and caps polymeric actin filaments (F-actin) (21): after binding of domain G1 and partly domain G2 to the actin filament (F-actin), gelsolin rapidly severs F-actin and then remains bound to the barbed end of one of the newly formed filaments, forming a stable cap, thus inhibiting addition of further monomers.
The concentration of gelsolin seems to be rate limiting in the actin removal system and depends on the rates of formation, dissociation, and clearance of the actin-gelsolin complex.
The thin filaments (~10 nm of diameter) are composed mainly by actin, tropomyosin, the troponin complex with its three subunits, tropomodulin and nebulin (Gordon et al.).
Actin. Actin (42 kDa) is the most abundant protein in almost all types of cells and the regulation of its architecture is essential for proper muscle function (Hopkins; Pappas et al., 2010).
To visualize actin filaments, after the secondary antibody incubation, the zygotes were treated with a 200-fold dilution of rhodamine phalloidin (R415; Molecular Probes) by DW for 2 h at room temperature and then rinsed in rinse solution three times.