Literature DB >> 2836420

Muscle is the major source of plasma gelsolin.

D J Kwiatkowski1, R Mehl, S Izumo, B Nadal-Ginard, H L Yin.   

Abstract

Gelsolin, a Ca2+- and polyphosphoinositide-regulated actin-binding protein, is unique among vertebrate proteins in being both cytoplasmic and secreted. Plasma gelsolin, present at greater than 200 micrograms/ml in human plasma, may have a protective function by promoting the clearance of actin filaments released during tissue injury. Although there is evidence that smooth muscle tissues and HepG2 cells synthesize plasma gelsolin, the predominant secretory source is hitherto unknown. We report here that skeletal, cardiac, and smooth muscles have large amounts of plasma gelsolin mRNA and devote 0.5-3% of their biosynthetic activity to plasma gelsolin, whereas liver makes relatively little. Since skeletal muscle accounts for a large fraction of body mass and total protein synthesis, it is the major source of plasma gelsolin.

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Year:  1988        PMID: 2836420

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  59 in total

1.  Metalloendoprotease cleavage triggers gelsolin amyloidogenesis.

Authors:  Lesley J Page; Ji Young Suk; Mary E Huff; Hee-Jong Lim; John Venable; John Yates; Jeffery W Kelly; William E Balch
Journal:  EMBO J       Date:  2005-11-10       Impact factor: 11.598

Review 2.  Mechanisms of exercise-induced muscle fibre injury.

Authors:  R B Armstrong; G L Warren; J A Warren
Journal:  Sports Med       Date:  1991-09       Impact factor: 11.136

3.  Plasma gelsolin and circulating actin correlate with hemodialysis mortality.

Authors:  Po-Shun Lee; Kartik Sampath; S Ananth Karumanchi; Hector Tamez; Ishir Bhan; Tamara Isakova; Orlando M Gutierrez; Myles Wolf; Yuchiao Chang; Thomas P Stossel; Ravi Thadhani
Journal:  J Am Soc Nephrol       Date:  2009-04-23       Impact factor: 10.121

4.  Phototactic migration of Dictyostelium cells is linked to a new type of gelsolin-related protein.

Authors:  S Stocker; M Hiery; G Marriott
Journal:  Mol Biol Cell       Date:  1999-01       Impact factor: 4.138

5.  Depletion of plasma gelsolin in patients with tick-borne encephalitis and Lyme neuroborreliosis.

Authors:  Alina Kułakowska; Joanna M Zajkowska; Nicholas J Ciccarelli; Barbara Mroczko; Wiesław Drozdowski; Robert Bucki
Journal:  Neurodegener Dis       Date:  2011-03-10       Impact factor: 2.977

6.  Filamin and gelsolin influence Ca(2+)-sensitivity of smooth muscle thin filaments.

Authors:  N B Gusev; K Pritchard; J L Hodgkinson; S B Marston
Journal:  J Muscle Res Cell Motil       Date:  1994-12       Impact factor: 2.698

7.  The 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenic.

Authors:  James P Solomon; Isaac T Yonemoto; Amber N Murray; Joshua L Price; Evan T Powers; William E Balch; Jeffery W Kelly
Journal:  Biochemistry       Date:  2009-12-08       Impact factor: 3.162

8.  Definition of a Ca2(+)-sensitive interface in the plasma gelsolin-actin complex.

Authors:  A Houmeida; V Hanin; J Feinberg; Y Benyamin; C Roustan
Journal:  Biochem J       Date:  1991-03-15       Impact factor: 3.857

9.  Gelsolin is depleted in post-shock mesenteric lymph.

Authors:  Janeen R Jordan; Ernest E Moore; Sagar S Damle; Phillip Eckels; Jeffrey L Johnson; Jonathan P Roach; Jasmina S Redzic; Kirk C Hansen; Anirban Banerjee
Journal:  J Surg Res       Date:  2007-11       Impact factor: 2.192

10.  A direct interaction with calponin inhibits the actin-nucleating activity of gelsolin.

Authors:  Imen Ferjani; Abdellatif Fattoum; Sutherland K Maciver; Christine Bénistant; Anne Chahinian; Mohamed Manai; Yves Benyamin; Claude Roustan
Journal:  Biochem J       Date:  2006-06-15       Impact factor: 3.857

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