Chicken‐Gizzard Actin: Polymerization and Stability

Strzelecka‐Gołaszewska, Hanna; Próchniewicz, Ewa; Nowak, Ewa; Zmorzyñski, S.; Drabikowski, W.

doi:10.1111/j.1432-1033.1980.tb04397.x

Cited by 89 publications

(39 citation statements)

References 29 publications

(23 reference statements)

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“…Avian smooth muscle actin was purified according to [27]. Rabbit skeletal muscle myosin was prepared by a procedure modified from [28], and HMM made from fresh myosin according to [29].…”

Section: In Vitro Motility Assaysmentioning

confidence: 99%

Calponin reduces shortening velocity in skinned taenia coli smooth muscle fibres

et al. 1995

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Calponin (4.1-5.9/.tM, pig stomach) inhibited maximal shortening velocity (Vm,x) by 20-25% with only minor influence on force in skinned smooth muscle from guinea-pig taenia coli activated at different Ca 2+ levels and with thiophosphorylation. Similar results were obtained with a fragment of the Nterminal 1-228 amino acids engineered using a mouse cDNA construct (5.4 pM). Both the native calponin and the fragment inhibited actin filament sliding in a graded manner in an in vitro motility assay. We conclude that calponin influences the kinetics of the actin-myosin interaction in the organised smooth muscle contractile system and that engineered fragments of calponin can be used to probe its action in muscle fibres. The effects can be due to an introduction of an internal load during filament sliding, possibly by decreasing the detachment rates and increasing the cross-bridge time spent in the attached state.

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“…Avian smooth muscle actin was purified according to [27]. Rabbit skeletal muscle myosin was prepared by a procedure modified from [28], and HMM made from fresh myosin according to [29].…”

Section: In Vitro Motility Assaysmentioning

confidence: 99%

Calponin reduces shortening velocity in skinned taenia coli smooth muscle fibres

et al. 1995

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“…Preparation of chicken gizzard actin was essentially as in [26]. After 3 cycles of polymerization and depolymerization, G-actin thus prepared was used either with or without the further purification by column chromatography, the preparations being referred to as column purified G-actin preparation and depolymerized actin preparation, respectively.…”

Section: Methodsmentioning

confidence: 99%

Actin polymerization induced by calspectin, a calmodulin‐binding spectrinlike protein

et al. 1982

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We have purified from a membrane fraction of bovine brain a calmodulin-binding protein (calspectin) that shares a number of properties with erythrocyte spectrin: It has a heterodimeric structure with M, 240 000 and 235 000 and binds to (dimeric form) or crosslinks (tetrameric form) F-actin. We show that calspectin (tetramer) is capable of inducing the polymerization of G-actin to actin filaments by increasing nucleation under conditions where actin alone polymerizes at a much slower rate. Thus, brain calspectin behaves in the same manner as erythrocyte spectrin, supporting the idea that, in conjunction with actin oligomers it comprises the cytoskeletal meshwork underlying the cytoplasmic surface of the nerve cell.

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“…Actomyosin pellets obtained from turkey gizzards (24) were further extracted for purification of smooth muscle actin (26). Purified smooth muscle F-actin was collected by centrifugation at 100,000 ϫ g after two cycles of polymerization-depolymerization (26). Purification of myosin light chain kinases was performed at 4°C if not specified.…”

Section: Expression Of Full-length and Truncated Smooth Muscle Myosinmentioning

confidence: 99%

“…Regulatory light chain was purified from turkey gizzards (24) and from Escherichia coli expressing human regulatory light chain (25). Actomyosin pellets obtained from turkey gizzards (24) were further extracted for purification of smooth muscle actin (26). Purified smooth muscle F-actin was collected by centrifugation at 100,000 ϫ g after two cycles of polymerization-depolymerization (26).…”

Section: Expression Of Full-length and Truncated Smooth Muscle Myosinmentioning

confidence: 99%

Binding of Myosin Light Chain Kinase to Cellular Actin-Myosin Filaments

Lin

Luby-Phelps²,

Stull

1997

Journal of Biological Chemistry

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Myosin light chain kinase binds to the actomyosincontaining filaments in smooth and nonmuscle cells. However, the region of the kinase necessary for this high affinity binding in vivo is not known, although it has been proposed that the N and C termini bind to actin and myosin in vitro, respectively. Truncated myosin light chain kinases containing the catalytic core and calmodulin-binding domain but lacking N (amino acids 1-655) and/or C (amino acids 1004 -1147) termini were expressed in the baculovirus system and purified. All enzymes were catalytically active and Ca 2؉ /calmodulindependent. The C-terminal truncated myosin light chain kinase bound to detergent-washed smooth muscle contractile proteins similar to recombinant full-length myosin light chain kinase or enzyme purified from smooth muscle. The apparent affinity of the full-length kinase was greater for the actomyosin-containing filaments with associated proteins than for purified smooth muscle F-actin or actomyosin filaments from skeletal muscle. In contrast, truncations at the N terminus alone or at both N and C termini resulted in no significant binding. Similar effects were observed by two other assays: binding of fluorescently labeled myosin light chain kinases to actin-containing stress fibers in detergenttreated fibroblasts and localization of fluorescently labeled kinases after microinjection into primary smooth muscle cells in culture. The full-length and the C-terminal truncated myosin light chain kinases, but not myosin light chain kinases truncated at the N terminus or both N and C termini, associated with filaments in cells. Thus, the N terminus and not the C terminus of myosin light chain kinase is necessary for high affinity binding to actomyosin-containing filaments in smooth and nonmuscle cells.

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Chicken‐Gizzard Actin: Polymerization and Stability

Cited by 89 publications

References 29 publications

Calponin reduces shortening velocity in skinned taenia coli smooth muscle fibres

Calponin reduces shortening velocity in skinned taenia coli smooth muscle fibres

Actin polymerization induced by calspectin, a calmodulin‐binding spectrinlike protein

Binding of Myosin Light Chain Kinase to Cellular Actin-Myosin Filaments

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