Preparation and characterization of bovine aortic actin

Cavadore, Jean‐Claude; Axelrud-Cavadore, Claude; Berta, Philippe; Harricane, Marie-Cécile; Haiech, Jacques

doi:10.1042/bj2280433

Cited by 22 publications

(17 citation statements)

References 38 publications

(26 reference statements)

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“…CPBPs include proteins of an apparent Mr of about 70 kDa that are probably identical and of several proteins in the 3 W O kDa range that are not yet fully distinguishable. This group of [30][31][32][33][34][35][36][37][38][39][40] kDa proteins share common properties and can be differentiated from one another essentially by their amino acid sequence [ 1,2,[11][12][13]24,30] or by their characteristic migration on twodimensional electrophoresis [9]. Four have been clearly identified: lipocortin I (identical to calpactin 11), lipocortin I1 (identical to calpactin I heavy chain), protein I1 (similar to endonexin and chromobindin 4), and endonexin 11, which is identical to the coagulation inhibitor (PAP or IBC) and to lipocortin V [30].…”

Section: Jcbmentioning

confidence: 99%

Further characterization of four lipocortins from human peripheral blood mononuclear cells

Coméra

Rothhut

Cavadore

et al. 1989

J of Cellular Biochemistry

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Four calcium and phospholipid binding proteins purified from mononuclear cells were characterized for PKC and EGF phosphorylation, actin binding capacity, and partial tissue distribution. Those named 35K, 32K, and 73K are equivalent, respectively, to lipocortin III, endonexin II and the 67 kDa calelectrin; 36K is a fragment of 73K. After purification, 35K and 73K were phosphorylated by protein kinase C in vitro but 36K nor 32K were not. None were phosphorylated by the epidermal growth factor receptor kinase in vitro; 73K bound F-actin in a calcium-dependent manner, whereas 35K, 36K, and 32K did not. Using Western blotting analysis, 32K and 73K were detected in high amounts in human lymphocytes, monocytes, liver, and placenta and in rat adrenal medulla; but 32K was not detected in polymorphonuclear cells, and 36K and 35K were detected in high amounts only, respectively, in human blood lymphocytes and polymorphonuclear cells. Thus, 32K and 73K appear to have a wide tissue distribution, whereas 35K has a much more restricted distribution.

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Section: Jcbmentioning

confidence: 99%

Further characterization of four lipocortins from human peripheral blood mononuclear cells

Coméra

Rothhut

Cavadore

et al. 1989

J of Cellular Biochemistry

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“…Smooth muscle a-actinin was obtained from chicken gizzard as described by Craig et al (1 982). Tropomyosin was obtained from rabbit skeletal muscle according to Cavadore et al (1985). Rabbit skeletal muscle actin was extracted from acetone powder (Spudich and Watt, 1971) and further purified on Sephacryl S300 as previously described (Lebart et al, 1990).…”

Section: Preparation Of Protein and Peptidesmentioning

confidence: 99%

Localization and identification of actin structures involved in the filamin – actin interaction

Méjean

Lebart

Boyer

et al. 1992

European Journal of Biochemistry

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The interface between gizzard filamin and skeletal muscle actin was located on the actin monomer. Conserved sequences 105 -120 and 360 -372, in the actin subdomain 1 near the myosin binding sites, were involved in this interaction. The corresponding peptides for these sequences were each found to bind filamin and compete in the actin-filamin interaction. When these two peptides were used together in the presence of filamin and filamentous actin, they dissociated sedimentable complexes formed by these two proteins.

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“…Bovine aortic-muscle actin was prepared as previously described by Cavadore et al (1985). Glutaraldehydestabilized aortic F-actin (Herman & Pollard, 1979) was coupled to CNBr-activated Sepharose 4B (Pharmacia) as indicated by the manufacturer.…”

Section: Methodsmentioning

confidence: 99%

A 36 kDa monomeric protein and its complex with a 10 kDa protein both isolated from bovine aorta are calpactin-like proteins that differ in their Ca2+-dependent calmodulin-binding and actin-severing properties

Martin

Derancourt

Capony

et al. 1988

Biochemical Journal

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Interaction of plasma membrane with the cytoskeleton involves a large number of proteins, among them a 36 kDa protein that was found to be involved in the interaction with actin filaments. We have isolated a 36 kDa protein from bovine aorta as a monomer and in a complex with a 10 kDa protein. Partial amino acid sequence determinations show that the 36 kDa and 10 kDa proteins isolated from bovine aorta are analogous to or identical with corresponding proteins purified from bovine intestine already described by Kristensen, Saris, Hunter, Hicks, Noonan, Glenney & Tack [(1986) Biochemistry 25, 4497-4503]. We report here that the association of the 10 kDa protein with the 36 kDa protein confers specific calmodulin-binding and actin-severing properties on the complex that are not possessed by the 36 kDa monomer alone. These findings suggest that the protein complex could be involved in thin-filament-related structures or could modulate some Ca2+-regulated events mediated by calmodulin.

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Preparation and characterization of bovine aortic actin

Cited by 22 publications

References 38 publications

Further characterization of four lipocortins from human peripheral blood mononuclear cells

Further characterization of four lipocortins from human peripheral blood mononuclear cells

Localization and identification of actin structures involved in the filamin – actin interaction

A 36 kDa monomeric protein and its complex with a 10 kDa protein both isolated from bovine aorta are calpactin-like proteins that differ in their Ca2+-dependent calmodulin-binding and actin-severing properties

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