Interaction of plasma gelsolin with tropomyosin.
Abstract: Horse plasma gelsolin labelled with benzophenone-4-isothiocyanate can be photochemically cross-linked to rabbit cardiac tropomyosin. The cross-linking proceeds with greater efficiency in calcium-containing buffers. Further evidence for interaction between these proteins is provided by retention of fluorescently labelled gelsolin on tropomyosin-agarose affinity columns and by the ability of tropomyosin to cause an increase in the fluorescence intensity of gelsolin labelled with fluorescein-5-isothiocyanate. Both of these effects require the presence of calcium ions.
Publication Date: 1992-08-31 PubMed ID: 1324850DOI: 10.1016/0014-5793(92)80738-3Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This research reveals that plasma gelsolin from horses can be chemically linked to cardiac tropomyosin from rabbits, a process that works better in calcium-containing environments. Further experiments demonstrated these proteins interact by binding to each other, an interaction dependent on the presence of calcium ions.
Plasma Gelsolin and Tropomyosin Interaction
- The research established a relationship between two proteins, plasma gelsolin and cardiac tropomyosin. The authors used horse plasma gelsolin labeled with a certain chemical compound (benzophenone-4-isothiocyanate) and were able to cross-link it photochemically to rabbit cardiac tropomyosin. This means that, under certain conditions, these two proteins can form bonds and interact with each other.
- This process of cross-linking was found to be more efficient in buffers containing calcium. Buffers are solutions used to maintain a constant pH level. The fact that calcium enhances this process indicates that calcium ions play a vital role in the interaction between these proteins.
Demonstration of Protein Interaction
- The researchers provided additional evidence of interaction between these proteins. They did this by retaining fluorescently labelled gelsolin on tropomyosin-agarose affinity columns. Agarose affinity columns are used in protein purification and the retention of gelsolin indicates that it has a strong affinity for tropomyosin, which supports the idea of interaction between these proteins.
- Further evidence was provided by the ability of tropomyosin to induce an increase in the fluorescence intensity of gelsolin labeled with fluorescein-5-isothiocyanate. This suggests a close interaction between the two proteins, as the fluorescence intensity of a molecule can increase when it interacts closely with another molecule.
- Both of these interactions (retention on affinity columns and increase in fluorescence) also required the presence of calcium ions, reinforcing the initial findings that calcium appears to be a critical factor in these protein interactions.
Cite This Article
APA
Koepf EK, Burtnick LD.
(1992).
Interaction of plasma gelsolin with tropomyosin.
FEBS Lett, 309(1), 56-58.
https://doi.org/10.1016/0014-5793(92)80738-3 Publication
Researcher Affiliations
- Department of Chemistry, University of British Columbia, Vancouver, Canada.
MeSH Terms
- Animals
- Calcium-Binding Proteins / blood
- Calcium-Binding Proteins / isolation & purification
- Chromatography, Affinity
- Electrophoresis, Polyacrylamide Gel
- Fluorescent Dyes
- Gelsolin
- Horses
- Kinetics
- Microfilament Proteins / blood
- Microfilament Proteins / isolation & purification
- Muscles / metabolism
- Myocardium / metabolism
- Protein Binding
- Rabbits
- Tropomyosin / isolation & purification
- Tropomyosin / metabolism
Citations
This article has been cited 6 times.- Kis-Bicskei N, Bécsi B, Erdődi F, Robinson RC, Bugyi B, Huber T, Nyitrai M, Talián GC. Tropomyosins Regulate the Severing Activity of Gelsolin in Isoform-Dependent and Independent Manners.. Biophys J 2018 Feb 27;114(4):777-787.
- Wawro B, Greenfield NJ, Wear MA, Cooper JA, Higgs HN, Hitchcock-DeGregori SE. Tropomyosin regulates elongation by formin at the fast-growing end of the actin filament.. Biochemistry 2007 Jul 10;46(27):8146-55.
- Ferjani I, Fattoum A, Maciver SK, Bénistant C, Chahinian A, Manai M, Benyamin Y, Roustan C. A direct interaction with calponin inhibits the actin-nucleating activity of gelsolin.. Biochem J 2006 Jun 15;396(3):461-8.
- Goosney DL, DeVinney R, Finlay BB. Recruitment of cytoskeletal and signaling proteins to enteropathogenic and enterohemorrhagic Escherichia coli pedestals.. Infect Immun 2001 May;69(5):3315-22.
- Dabrowska R, Hinssen H, Gałazkiewicz B, Nowak E. Modulation of gelsolin-induced actin-filament severing by caldesmon and tropomyosin and the effect of these proteins on the actin activation of myosin Mg(2+)-ATPase activity.. Biochem J 1996 May 1;315 ( Pt 3)(Pt 3):753-9.
- Teubner A, Sobek-Klocke I, Hinssen H, Eichenlaub-Ritter U. Distribution of gelsolin in mouse ovary.. Cell Tissue Res 1994 Jun;276(3):535-44.
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