F-Actin-Depolymerizing Activity of Human Serum

Norberg, Renée; Thorstensson, Rigmor; Utter, Göran; Fagræus, Astrid

doi:10.1111/j.1432-1033.1979.tb04204.x

Cited by 112 publications

(52 citation statements)

References 10 publications

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“…By contrast the ADF activity of human serum is reported to be abolished by Ca*+ chelators [2]; this may be due to an effect on factor stability rather than on the depolymerizing reaction itself.…”

Section: Discussionmentioning

confidence: 79%

An actin depolymerizing protein from pig plasma

Harris

Gooch

1981

FEBS Letters

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Section: Discussionmentioning

confidence: 79%

An actin depolymerizing protein from pig plasma

Harris

Gooch

1981

FEBS Letters

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“…The existence of a thermolabile factor with an inhib-the same 22 AAA-positive sera in 1:160 dilution (Table 1) is strong evidence that there are no false-positive iting activity against actin-containing structures was first proposed in 1979, by Norberg et al 34 At the same results in lower dilutions in techniques D and E. This conclusion is emphasized by the absence of AAA in time, Chaponnier et al 44 characterized an actin-depolymerizing factor present in human serum. Harris et control samples from SMA-negative sera that were tested by technique D.…”

Section: Techniques Techniquesmentioning

confidence: 94%

“…Their best preparations were obtained when the polymerizing factor). 34,44 In 1982, Thorstensson et al…”

Section: Techniques Techniquesmentioning

confidence: 99%

Heat serum inactivation as a mandatory procedure for antiactin antibody detection in cell culture

et al. 1996

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In autoimmune hepatitis (AIH), the smooth-muscle an-The determination of antiactin antibody (AAA) is of tibody is specific for polymerized actin. Detection of paramount importance to better characterize the antiantiactin antibody (AAA) has been hampered by techni-smooth muscle antibody (SMA), one of the most imcal problems. We have investigated AAA in 30 sera from portant autoantibodies for the diagnosis of autoimpatients with liver diseases and smooth-muscle anti-mune hepatitis (AIH).1-4 However, the best technique body. AAA was detected by indirect immunofluores-for its determination remains a challenge. Perhaps this

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“…The first recognized function of DBP was the plasma transport of vitamin D and other related derivatives [4]. In addition, other previous studies [5] have shown that the serum affords actin-depolymerizing activity. This property was further ascribed to the conjugate effects of gelsolin and DBP [6].…”

mentioning

confidence: 99%

Localization of a vitamin‐D‐binding protein interaction site in the COOH‐terminal sequence of actin

Houmeida

Hanin

Constans

et al. 1992

European Journal of Biochemistry

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The serum vitamin D binding protein is the carrier of vitamin D and its derivatives in the plasma. One of the known roles of this protein is to sequester monomeric actin in the blood, therefore implicating this protein in actin elimination. However, its binding site at the surface of actin is poorly delimited. We report here the results of a study which locates, using several actin fragments together with immunological probes, a vitamin D binding protein site near the COOH-terminal extremity.Thus, the interface is delimited by the sequence 360-372 in subdomain I of actin.The vitamin D binding protein (DBP), also called Gc (group component), is a plasma protein found in humans and other mammalian species [l]. It is a monomeric protein with an a2-globulin mobility, secreted by the liver [2, 31 and has a relative molecular mass (M,) of 52000 [3]. The first recognized function of DBP was the plasma transport of vitamin D and other related derivatives [4]. In addition, other previous studies [5] have shown that the serum affords actin-depolymerizing activity. This property was further ascribed to the conjugate effects of gelsolin and DBP [6]. However, whereas gelsolin can cause severing of actin filaments, DBP can sequester actin monomers in a 1 : l complex and thereby leads to actin depolymerization. The in vivo occurrence of a DBP-actin complex was detectcd, at a very low level, in the serum of healthy patients [7]. A drastic increase in the amount of actin and its DBP complex following tissue injury (hepatic necrosis for example) or trauma have also been reported [7, 81. Thus, one of the physiological roles of DBP would be to avoid actin filament formation, which would occur at normal salinity of the serum, and thus accelerate clearing of actin from the circulation [9, 101.In vitru, studies have clearly shown the existence of a very tight G-actin -DBP complex without interaction with F-actin [6]. Other studies have also suggested that the interaction site is restricted to the 227-375 segment of actin [ll], the Cterminal extremity being excluded. Another actin-sequestering protein, profilin, binds with a relatively low affinity at or near the C-terminal extremity of actin [12]. Thus, the two proteins would have different binding sites on actin. In fact, other actin-associated proteins have been shown to be directed to the C-terminal part of the actin sequence. This is true, not only for proteins which prevent actin polymerization, but also for crosslinking proteins such as a-actinin [13], for severing proteins such as gelsolin which interact with the 305 -326 actin sequence [14] and for the myosin subfragment-1 (SI)In view of the potential importance of DBP in the elimination of actin from plasma, we have begun a study aimed at defining the location of the DBP interface in the actin sequence. We located an interaction site of DBP precisely in subdomain I of actin. ~5 1 . MATERIALS AND METHODS Materials7-Chloro-4-nitrobenzo-2-oxa-I ,3,diazole (Nbd-C1) and Niodoacetyl-N-(5-sulfo-l-naphthyl) ethylenediamine (1,5-I-AED...

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F-Actin-Depolymerizing Activity of Human Serum

Cited by 112 publications

References 10 publications

An actin depolymerizing protein from pig plasma

An actin depolymerizing protein from pig plasma

Heat serum inactivation as a mandatory procedure for antiactin antibody detection in cell culture

Localization of a vitamin‐D‐binding protein interaction site in the COOH‐terminal sequence of actin

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