Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain
- PMID: 3020431
- DOI: 10.1038/323455a0
Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain
Abstract
Gelsolin is representative of a class of actin-modulating proteins found in lower eukaryotes to mammals, which sever actin filaments. Gelsolin found in the cytoplasm of cells is functionally similar to a mammalian plasma protein of similar size, originally called ADF or brevin. Human plasma and rabbit macrophage gelsolins differ by the presence of a 25-amino-acid residue extension on plasma gelsolin which appears to account for the difference in relative molecular mass (Mr) between the proteins as assessed by SDS-polyacrylamide gel electrophoresis (PAGE), 93,000 (93K) and 90K, respectively. Here we report the isolation of full-length human plasma gelsolin complementary DNA clones from a HepG2 library. The inferred amino-acid sequence reveals the presence of a signal peptide, a long tandem repeat that matches the actin-binding domains of gelsolin, a tetrapeptide present in actin and extended regions of identical sequence with rabbit macrophage gelsolin. Southern blot analysis indicates that a single gene in the haploid genome encodes both protein forms.
Similar articles
-
Cloning of a secretory gelsolin from Drosophila melanogaster.J Mol Biol. 1993 Apr 5;230(3):709-16. doi: 10.1006/jmbi.1993.1191. J Mol Biol. 1993. PMID: 8386771
-
The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure.Biochemistry. 1996 Jul 30;35(30):9700-9. doi: 10.1021/bi960920n. Biochemistry. 1996. PMID: 8703941
-
Differential effects of gelsolins on tissue culture cells.Cell Motil Cytoskeleton. 1990;16(4):229-38. doi: 10.1002/cm.970160403. Cell Motil Cytoskeleton. 1990. PMID: 2168294
-
Evolution of the gelsolin family of actin-binding proteins as novel transcriptional coactivators.Bioessays. 2005 Apr;27(4):388-96. doi: 10.1002/bies.20200. Bioessays. 2005. PMID: 15770676 Review.
-
Human plasma gelsolin binds adenosine triphosphate.J Biochem. 1990 Oct;108(4):505-6. doi: 10.1093/oxfordjournals.jbchem.a123229. J Biochem. 1990. PMID: 1963427 Review.
Cited by
-
Plasma gelsolin modulates the production and fate of IL-1β-containing microparticles following high-pressure exposure and decompression.J Appl Physiol (1985). 2021 May 1;130(5):1604-1613. doi: 10.1152/japplphysiol.01062.2020. Epub 2021 Mar 25. J Appl Physiol (1985). 2021. PMID: 33764168 Free PMC article.
-
Comparative two-dimensional gel analysis and microsequencing identifies gelsolin as one of the most prominent downregulated markers of transformed human fibroblast and epithelial cells.J Cell Biol. 1990 Jul;111(1):95-102. doi: 10.1083/jcb.111.1.95. J Cell Biol. 1990. PMID: 2164032 Free PMC article.
-
Identification of a region in segment 1 of gelsolin critical for actin binding.EMBO J. 1990 Dec;9(12):4103-9. doi: 10.1002/j.1460-2075.1990.tb07632.x. EMBO J. 1990. PMID: 2174356 Free PMC article.
-
Gelsolin has three actin-binding sites.J Cell Biol. 1988 May;106(5):1553-62. doi: 10.1083/jcb.106.5.1553. J Cell Biol. 1988. PMID: 2836434 Free PMC article.
-
Steered molecular dynamics simulations on the "tail helix latch" hypothesis in the gelsolin activation process.Biophys J. 2002 Aug;83(2):753-62. doi: 10.1016/S0006-3495(02)75206-5. Biophys J. 2002. PMID: 12124262 Free PMC article.
Publication types
MeSH terms
Substances
Associated data
- Actions
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials