CROSS-LINKER DYNAMICS DETERMINE THE MECHANICAL-PROPERTIES OF ACTIN GELS

CROSS-LINKER DYNAMICS DETERMINE THE MECHANICAL-PROPERTIES OF ACTIN GELS
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DOI:
10.1016/s0006-3495(94)80856-2
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发表时间:
1994-03-01
影响因子:
3.4
通讯作者:
POLLARD, TD
POLLARD, TD
中科院分区:
生物学3区
文献类型:
--
作者:
WACHSSTOCK, DH;SCHWARZ, WH;POLLARD, TD

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To evaluate the contributions of cross-linker dynamics and polymer deformation to the frequency-dependent stiffness of actin filament gels, we compared the rheological properties of actin gels with three types of cross-linkers: a weak one, Acanthamoeba alpha-actinin (dissociation rate constant 5.2 s(-1), association rate constant 1.1 x 10(6) M(-1) s(-1)); a strong one, chicken smooth muscle alpha-actinin (dissociation rate constant 0.66 s(-1), association rate constant 1.20 x 10(6) M(-1) s(-1)); and an extremely strong one, biotin/avidin (dissociation rate constant approximately zero). The biotin/avidin cross-linked gel, whose behavior is determined by polymer bending alone, behaves like a solid and shows no frequency dependence. The amoeba alpha-actinin cross-linked gel behaves like a viscoelastic fluid, and the frequency dependence of the stiffness can be explained by a mathematical model for dynamically cross-linked gels. The stiffness of the chicken alpha-actinin cross-linked gel is independent of frequency, and has viscoelastic properties intermediate between the two. The two alpha-actinins have similar association rate constants for binding to actin filaments, consistent with a diffusion-limited reaction. Rigid cross-links make the gel stiff, but make it elastic without the ability to deform permanently. Dynamically cross-linked actin filaments should allow the cell to react passively to various outside forces without any sort of signaling. Slower, signal-mediated pathways, such as severing filaments or changing the affinity of cross-linkers, could alter the nature of these passive reactions.