1983
DOI: 10.1111/j.1471-4159.1983.tb08119.x
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Isolation of a Ca2+‐Dependent Actin‐Fragmenting Protein from Brain, Spinal Cord, and Cultured Neurones

Abstract: Extracts of ox spinal cord and chicken brain were fractionated by ion-exchange chromatography and assayed for their ability to reduce the viscosity of muscle F-actin solutions. Two distinct peaks of activity were obtained, one of which was further purified by affinity chromatography on a DNAase-actin Sepharose column. Following molecular exclusion chromatography, the actin component appeared as a complex of 1 molecule of a protein with molecular weight 90,000 and 2 molecules of actin (42,000). This tightly bou… Show more

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Cited by 49 publications
(23 citation statements)
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“…Colocalization of gelsolin and micro¢laments has been observed in growth cones of PC12 cells, but is less clear in dorsal root ganglion neurons (Tanaka et al 1993). Gelsolin is also present in neurites and growth cones of cultured sympathetic neurons (Petrucci et al 1983). This 1704 M. D. Neely and E. Macaluso Gelsolin and pro¢lin in leech neurites Proc.…”
Section: Discussionmentioning
confidence: 99%
“…Colocalization of gelsolin and micro¢laments has been observed in growth cones of PC12 cells, but is less clear in dorsal root ganglion neurons (Tanaka et al 1993). Gelsolin is also present in neurites and growth cones of cultured sympathetic neurons (Petrucci et al 1983). This 1704 M. D. Neely and E. Macaluso Gelsolin and pro¢lin in leech neurites Proc.…”
Section: Discussionmentioning
confidence: 99%
“…Probably, the 'cap 90' binds to DNase-I as a 1: 1 complex with actin [8], from which the pure 'cap 90' is released during elution from the DNase-I column with 8.8 M formamide.…”
Section: Discussionmentioning
confidence: 99%
“…Our search for capping proteins in the nervous system led to the discovery of a first capping protein, which was isolated from bovine brain cortex [7], This protein has a native MX-value of 63 kDa, consists of two polypeptides of 36 kDa and 3 1 kDa and caps the fast-growing end of actin filaments in a Caz+-insensitive manner. Recently, the isolation of a 90-kDa Ca2+-dependent actin fragmenting protein from neuronal tissue was reported [8]. This protein, however, in its native form could only be isolated as a 1: 1 complex with another protein of 42 kDa.…”
Section: Introductionmentioning
confidence: 99%
“…As formamide exerts a powerful actin-depolymerizing activity, this finding is in favor of the possibility that the supernatants contain actin-ADF complexes rather than actin oligomers. Such complexes are apparently resistent to the dissociating effect of formamide [33]. Another argument supporting the formation of actin-ADF complexes derives from the results of the experiment in which G-actin and ADF were mixed under ionic conditions favoring actin depolymerization (Table 1) ; here the addition of increasing proportions of ADF progressively decreased the DNase-inhibiting activity of G-actin; at a G-actin:ADF molar ratio of 1:1, the inhibition of DNase activity was only 7% of that exerted by the same amount of G-actin alone.…”
Section: Discussionmentioning
confidence: 99%
“…These data suggest that ADF treatment before immunofluorescent staining for actin represents a useful tool for the evaluation of the state of actin polymerization and/or stability during different pathological or experimental conditions. Our antibody against ADF gives a positive immunofluorescent stain when incubated with human platelets, polymorphonuclear neutrophils and other leukocytes, but does not stain cells such as fibroblasts where gelsolin, an actinfragmenting protein isolated from macrophages [39 -421 but present in many cells and tissues [33,[43][44][45][46], has been localized. Immunoblotting further confirms that ADF antibody recognizes a 90-kDa protein in platelets and polymorphonuclear neutrophils but not in fibroblasts.…”
Section: Discussionmentioning
confidence: 99%