ArticleThe Journal of cell biology1987
Microinjection of gelsolin into living cells.
Article in The Journal of cell biology, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
52 citing papers in PubMed, 142 citations in OpenAlex.
- Cytoskeleton-associated gelsolin responds to the midgut distention process in saline meal-fed Aedes aegypti and affects arbovirus dissemination from the midgut.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024Article
- Cytochalasans and Their Impact on Actin Filament Remodeling.Biomolecules · 2023Review
- Mapping the Proximity Interaction Network of STIM1 Reveals New Mechanisms of Cytoskeletal Regulation.Cells · 2021Article
- Role of Plasma Gelsolin Protein in the Final Stage of Erythropoiesis and in Correction of Erythroid Dysplasia In Vitro.International journal of molecular sciences · 2020Article
- Do Skeletal Dynamics Mediate Sugar Uptake and Transport in Human Erythrocytes?Biophysical journal · 2018Article
- Gelsolin dysfunction causes photoreceptor loss in induced pluripotent cell and animal retinitis pigmentosa models.Nature communications · 2017Article
- Dynamin rings: not just for fission.Traffic (Copenhagen, Denmark) · 2013Review
- A llama-derived gelsolin single-domain antibody blocks gelsolin-G-actin interaction.Cellular and molecular life sciences : CMLS · 2010Article
- Rheological characterization of the bundling transition in F-actin solutions induced by methylcellulose.PloS one · 2008Article
- Regulated motion of glycoproteins revealed by direct visualization of a single cargo in the endoplasmic reticulum.The Journal of cell biology · 2008Article
- Glass transition and rheological redundancy in F-actin solutions.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Micro- and macrorheological properties of actin networks effectively cross-linked by depletion forces.Biophysical journal · 2006Article
- Using single-particle tracking to study nuclear trafficking of viral genes.Biophysical journal · 2004Article
- Gelsolin gene expression is upregulated in damaged rat and human livers within non-parenchymal cells and not in hepatocytes.Histochemistry and cell biology · 2003Article
- The optical stretcher: a novel laser tool to micromanipulate cells.Biophysical journal · 2001Article
- A cell-free system to study regulation of focal adhesions and of the connected actin cytoskeleton.Molecular biology of the cell · 1999Article
- Identification of Tyr438 as the major in vitro c-Src phosphorylation site in human gelsolin: a mass spectrometric approach.Protein science : a publication of the Protein Society · 1999Article
- Gelsolin and functionally similar actin-binding proteins are regulated by lysophosphatidic acid.The EMBO journal · 1998Article
- Motile areas of leech neurites are rich in microfilaments and two actin-binding proteins: gelsolin and profilin.Proceedings. Biological sciences · 1997Article
- The actin-severing protein gelsolin modulates calcium channel and NMDA receptor activities and vulnerability to excitotoxicity in hippocampal neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1997Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Gelsolins are actin-binding proteins that cap, nucleate, and sever actin filaments. Microinjection of cytoplasmic or plasma gelsolin into living fibroblasts and macrophages did not affect the shape, actin distribution, deformability, or ruffling activity of the cells. Gelsolin requires calcium for activity, but the NH2-terminal half is active without calcium. Microinjection of this proteolytic fragment had marked effects: the cells rounded up, stopped ruffling, became soft, and stress fibers disappeared. These changes are similar to those seen with cytochalasin, which also caps barbed ends of actin filaments. Attempts to raise the cytoplasmic calcium concentration and thereby activate the injected gelsolin were unsuccessful, but the increases in calcium concentration were minimal or transient and may not have been sufficient. Our interpretation of these results is that at the low calcium concentrations normally found in cells, gelsolin does not express the activities observed in vitro at higher calcium concentrations. We presume that gelsolin may be active at certain times or places if the calcium concentration is elevated to a sufficient level, but we cannot exclude the existence of another molecule that inhibits gelsolin. Microinjection of a 1:1 gelsolin/actin complex had no effect on the cells. This complex is stable in the absence of calcium and has capping activity but no severing and less nucleation activity as compared with either gelsolin in calcium or the NH2-terminal fragment. The NH2-terminal fragment-actin complex also has capping and nucleating activity but no severing activity. On microinjection it had the same effects as the fragment alone. The basis for the difference between the two complexes is unknown. The native molecular weight of rabbit plasma gelsolin is 82,500, and the extinction coefficient at 280 nm is 1.68 cm2/mg. A new simple procedure for purification of plasma gelsolin is described.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.