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Main Authors: Bonar, Sophia E, Mattos, Daphne R, Yu, Xinhui, Neuhaus, George F, Youssef, Diaa T A, Shaala, Lamiaa A, Gerwick, William H, McPhail, Kerry L, Ishmael, Jane E
Format: Artículo científico
Language:en
Published: Journal of natural products 2026
Subjects:
Online Access:https://pubmed.ncbi.nlm.nih.gov/42080225/
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author Bonar, Sophia E
Mattos, Daphne R
Yu, Xinhui
Neuhaus, George F
Youssef, Diaa T A
Shaala, Lamiaa A
Gerwick, William H
McPhail, Kerry L
Ishmael, Jane E
author_facet Bonar, Sophia E
Mattos, Daphne R
Yu, Xinhui
Neuhaus, George F
Youssef, Diaa T A
Shaala, Lamiaa A
Gerwick, William H
McPhail, Kerry L
Ishmael, Jane E
Bonar, Sophia E
Mattos, Daphne R
Yu, Xinhui
Neuhaus, George F
Youssef, Diaa T A
Shaala, Lamiaa A
Gerwick, William H
McPhail, Kerry L
Ishmael, Jane E
collection PubMed - marine biology
contents Identification of Hoiamide A as an Inducer of Oxidative and Endoplasmic Reticulum Secretory Pathway Stress. Bonar, Sophia E Mattos, Daphne R Yu, Xinhui Neuhaus, George F Youssef, Diaa T A Shaala, Lamiaa A Gerwick, William H McPhail, Kerry L Ishmael, Jane E Humans Endoplasmic Reticulum Stress Oxidative Stress Endoplasmic Reticulum Depsipeptides Molecular Structure Secretory Pathway Superoxide Dismutase-1 Cell Line, Tumor Transcription Factor CHOP Cyanobacteria The endoplasmic reticulum (ER) to Golgi secretory compartment of eukaryotic cells is highly sensitive to changes in intracellular homeostasis. Using a primary screening assay that monitors the function of this pathway, we prioritized a cyanobacterial extract from the Red Sea that decreased secretion of a bioluminescent reporter, luciferase (GLuc), in living cells. A comparison of LCMS2 data against the GNPS database revealed a match for macrocyclic depsipeptide hoiamide A (). Biological testing confirmed the ability of to induce a mixed, non-lethal stress response in human U87-MG glioblastoma cells; analysis of stress markers by qRT-PCR revealed early upregulation of superoxide dismutase 1 (SOD1) and C/EBP-homologous protein (CHOP) relative to the control. Co-treatment of cells with (100 nM to 3 μM) and antioxidant -acetylcysteine afforded full protection from -induced decreases in GLuc secretion. We report that terminally differentiated human SH-SY5Y neuroblastoma cells, with a neuron-like phenotype, are highly sensitive to nanomolar concentrations of , whereas undifferentiated cells remained viable at 3 μM. These results expand the known biology of hoiamides and suggest that neurotoxic potential of is likely due to an inherent failure of neurons to adapt to the loss of redox homeostasis and sustained ER stress.
format Artículo científico
id pubmed_42080225
institution PubMed
language en
publishDate 2026
publisher Journal of natural products
record_format pubmed
spellingShingle Identification of Hoiamide A as an Inducer of Oxidative and Endoplasmic Reticulum Secretory Pathway Stress.
Bonar, Sophia E
Mattos, Daphne R
Yu, Xinhui
Neuhaus, George F
Youssef, Diaa T A
Shaala, Lamiaa A
Gerwick, William H
McPhail, Kerry L
Ishmael, Jane E
Humans
Endoplasmic Reticulum Stress
Oxidative Stress
Endoplasmic Reticulum
Depsipeptides
Molecular Structure
Secretory Pathway
Superoxide Dismutase-1
Cell Line, Tumor
Transcription Factor CHOP
Cyanobacteria
Identification of Hoiamide A as an Inducer of Oxidative and Endoplasmic Reticulum Secretory Pathway Stress. Bonar, Sophia E Mattos, Daphne R Yu, Xinhui Neuhaus, George F Youssef, Diaa T A Shaala, Lamiaa A Gerwick, William H McPhail, Kerry L Ishmael, Jane E Humans Endoplasmic Reticulum Stress Oxidative Stress Endoplasmic Reticulum Depsipeptides Molecular Structure Secretory Pathway Superoxide Dismutase-1 Cell Line, Tumor Transcription Factor CHOP Cyanobacteria The endoplasmic reticulum (ER) to Golgi secretory compartment of eukaryotic cells is highly sensitive to changes in intracellular homeostasis. Using a primary screening assay that monitors the function of this pathway, we prioritized a cyanobacterial extract from the Red Sea that decreased secretion of a bioluminescent reporter, luciferase (GLuc), in living cells. A comparison of LCMS2 data against the GNPS database revealed a match for macrocyclic depsipeptide hoiamide A (). Biological testing confirmed the ability of to induce a mixed, non-lethal stress response in human U87-MG glioblastoma cells; analysis of stress markers by qRT-PCR revealed early upregulation of superoxide dismutase 1 (SOD1) and C/EBP-homologous protein (CHOP) relative to the control. Co-treatment of cells with (100 nM to 3 μM) and antioxidant -acetylcysteine afforded full protection from -induced decreases in GLuc secretion. We report that terminally differentiated human SH-SY5Y neuroblastoma cells, with a neuron-like phenotype, are highly sensitive to nanomolar concentrations of , whereas undifferentiated cells remained viable at 3 μM. These results expand the known biology of hoiamides and suggest that neurotoxic potential of is likely due to an inherent failure of neurons to adapt to the loss of redox homeostasis and sustained ER stress.
title Identification of Hoiamide A as an Inducer of Oxidative and Endoplasmic Reticulum Secretory Pathway Stress.
topic Humans
Endoplasmic Reticulum Stress
Oxidative Stress
Endoplasmic Reticulum
Depsipeptides
Molecular Structure
Secretory Pathway
Superoxide Dismutase-1
Cell Line, Tumor
Transcription Factor CHOP
Cyanobacteria
url https://pubmed.ncbi.nlm.nih.gov/42080225/