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LL-37

Cathelicidin, hCAP-18, FALL-39, CAP-18

Quick Stats
Studies 2230
Trials 95
Score 1
2017 pubmed 14 citations

Histones bundle F-actin filaments and affect actin structure.

Blotnick. Edna E; Sol. Asaf A; Muhlrad. Andras A

Key Findings

  • Histone mixtures and the H2A histone can bundle F‑actin, increasing solution viscosity and promoting actin polymerization.
  • These histone‑actin bundles are unusually resistant to salt (only break apart at 300‑400 mM NaCl) and can be disrupted by DNA.
  • Enzymes like DNase 1 and proteins like cofilin can partially unwind the bundles, indicating both electrostatic and hydrophobic forces hold them together.

Practical Outcomes

  • For biohackers, this research doesn’t provide a new supplement or protocol to try. It mainly highlights a potential harmful effect of extracellular histones on mucus thickness, which is relevant for disease contexts like cystic fibrosis but not for general longevity or performance optimization.

Summary

The study shows that histone proteins released from dying cells can stick to actin filaments outside the cell, forming thick bundles that make fluids thicker. These bundles are very stable unless a lot of salt or DNA is present, and they may contribute to the thick mucus seen in cystic fibrosis. The findings are mostly basic science and don’t suggest any direct health‑boosting actions for everyday use.

Abstract

Histones are small polycationic proteins complexed with DNA located in the cell nucleus. Upon apoptosis they are secreted from the cells and react with extracellular polyanionic compounds. Actin which is a polyanionic protein, is also secreted from necrotic cells and interacts with histones. We showed that both histone mixture (histone type III) and the recombinant H2A histone bundles F-actin, increases the viscosity of the F-actin containing solution and polymerizes G-actin. The histone-actin bundles are relatively insensitive to increase of ionic strength, unlike other polycation, histatin, lysozyme, spermine and LL-37 induced F-actin bundles. The histone-actin bundles dissociate completely only in the presence of 300-400 mM NaCl. DNA, which competes with F-actin for histones, disassembles histone induced actin bundles. DNase1, which depolymerizes F- to G-actin, actively unbundles the H2A histone induced but slightly affects the histone mixture induced actin bundles. Cofilin decreases the amount of F-actin sedimented by low speed centrifugation, increases light scattering and viscosity of F-actin-histone mixture containing solutions and forms star like superstructures by copolymerizing G-actin with H2A histone. The results indicate that histones are tightly attached to F-actin by strong electrostatic and hydrophobic forces. Since both histones and F-actin are present in the sputum of patients with cystic fibrosis, therefore, the formation of the stable histone-actin bundles can contribute to the pathology of this disease by increasing the viscosity of the sputum. The actin-histone interaction in the nucleus might affect gene expression.

Study Information

Provider

pubmed

Year

2017

Date

2017-08-28T00:00:00.000Z

DOI

10.1371/journal.pone.0183760

Citations

14

References

60