ArticleScientific reports2016
Amyloid formation of growth hormone in presence of zinc: Relevance to its storage in secretory granules.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 88 citations in OpenAlex.
- Biomimetic Protein Materials for Adjuvant-Free Dermal Penetration.ACS materials letters · 2026Article
- The intrinsically disordered region of the human parathyroid hormone controls functional amyloid properties.The Journal of biological chemistry · 2026Article
- Citrate-Assisted Regulation of Protein Stability and Secretability from Synthetic Amyloids.ACS applied materials & interfaces · 2025Article
- Confinement-Induced Self-Assembly of Protein Nanofibrils Probed by Microfocus X-ray Scattering.The journal of physical chemistry. B · 2025Article
- Protein aggregates and biomolecular condensates: implications for human health and disease.Frontiers in molecular biosciences · 2025Review
- Hybrid Micro-/Nanoprotein Platform Provides Endocrine-like and Extracellular Matrix-like Cell Delivery of Growth Factors.ACS applied materials & interfaces · 2024Article
- Human Platelet Lysate-Derived Nanofibrils as Building Blocks to Produce Free-Standing Membranes for Cell Self-Aggregation.ACS nano · 2024Article
- Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory Amyloids.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Nanoparticle-Based Secretory Granules Induce a Specific and Long-Lasting Immune Response through Prolonged Antigen Release.Nanomaterials (Basel, Switzerland) · 2024Article
- The Amyloid Assembly of the Bacterial Hfq Is Lipid-Driven and Lipid-Specific.International journal of molecular sciences · 2024Article
- Prion protein conversion at two distinct cellular sites precedes fibrillisation.Nature communications · 2023Article
- Efficient Delivery of Antimicrobial Peptides in an Innovative, Slow-Release Pharmacological Formulation.Pharmaceutics · 2023Article
- Resistance exercise stress: theoretical mechanisms for growth hormone processing and release from the anterior pituitary somatotroph.European journal of applied physiology · 2023Review
- Probing the Biosafety of Implantable Artificial Secretory Granules for the Sustained Release of Bioactive Proteins.ACS applied materials & interfaces · 2023Article
- Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative Overview.Pharmaceutics · 2023Article
- Article
- Amyloid-like RIP1/RIP3 RHIM Fragments' Characterization and Application as a Drug Depot.Molecules (Basel, Switzerland) · 2023Article
- Architecture of the two metal-binding sites in prolactin.Biophysical journal · 2022Article
- The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies.Pharmaceutics · 2022Article
- Co-aggregation and secondary nucleation in the life cycle of human prolactin/galanin functional amyloids.eLife · 2022Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloids are cross-β-sheet fibrillar aggregates, associated with various human diseases and native functions such as protein/peptide hormone storage inside secretory granules of neuroendocrine cells. In the current study, using amyloid detecting agents, we show that growth hormone (GH) could be stored as amyloid in the pituitary of rat. Moreover, to demonstrate the formation of GH amyloid in vitro, we studied various conditions (solvents, glycosaminoglycans, salts and metal ions) and found that in presence of zinc metal ions (Zn(II)), GH formed short curvy fibrils. The amyloidogenic nature of these fibrils was examined by Thioflavin T binding, Congo Red binding, transmission electron microscopy and X-ray diffraction. Our biophysical studies also suggest that Zn(II) initiates the early oligomerization of GH that eventually facilitates the fibrillation process. Furthermore, using immunofluorescence study of pituitary tissue, we show that GH in pituitary significantly co-localizes with Zn(II), suggesting the probable role of zinc in GH aggregation within secretory granules. We also found that GH amyloid formed in vitro is capable of releasing monomers. The study will help to understand the possible mechanism of GH storage, its regulation and monomer release from the somatotrophs of anterior pituitary.
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