epipolythiodioxopiperazine / epipolythiopiperazine-2,5-dione / HSP90 Cancer Research Results

HDN-1, epipolythiodioxopiperazine / epipolythiopiperazine-2,5-dione: Click to Expand ⟱
Features:

HDN-1 is a naturally occurring fungal epipolythiodioxopiperazine / epipolythiopiperazine-2,5-dione (ETP) isolated from the Antarctic fungus Oidiodendron truncatum GW3-13. HDN-1 has demonstrated preclinical anticancer activity and acts as a direct Hsp90 inhibitor, binding the C-terminal region of Hsp90α. Hsp90 inhibition by HDN-1 promotes degradation of multiple oncogenic client proteins, enhances downregulation of wild-type and mutant EGFR and suppresses tumour-cell proliferation. HDN-1 has also induced differentiation followed by apoptosis in selected promyelocytic leukemia cell lines. Its mechanism overlaps with that of the structurally related ETP chaetocin, which also inhibits Hsp90, but HDN-1 and chaetocin are chemically distinct compounds and should be maintained as separate products. HDN-1 should be classified as an experimental natural fungal metabolite / epipolythiodioxopiperazine / Hsp90 inhibitor, with current anticancer evidence predominantly preclinical.
HDN-1 is an analogue of chaetocin, which is a fungal mycotoxin with histone methyltransferase SUV39H1 inhibitory activity
HSP90, HSP90: Click to Expand ⟱
Source: HalifaxProj(inhibit)
Type:
Heat shock protein 90 (Hsp90) is a molecular chaperone that plays a critical role in the proper folding, stabilization, and function of many proteins, including those involved in cell signaling, cell cycle regulation, and stress responses.
-Hsp90 interacts with a variety of client proteins that are often mutated or overexpressed in cancer. These include oncogenes (like HER2, BRAF, and AKT) and tumor suppressor proteins (like p53).
-Hsp90 is often overexpressed in cancer cells, which can help them survive under stressful conditions, such as those found in the tumor microenvironment. This overexpression is associated with poor prognosis in several types of cancer.
-HSPs, particularly HSP90, are known to stabilize many proteins that drive cancer progression (oncoproteins).
Scientific Papers found: Click to Expand⟱
7169- HDN-1,  CHA,    Identification of epipolythiodioxopiperazines HDN-1 and chaetocin as novel inhibitor of heat shock protein 90
- in-vitro, Lung, H1975 - in-vitro, Lung, HCC827 - in-vitro, Lung, A549
HSP90↓, TumCP↓, EGFR↓, STAT3↓, Akt↓, ERK↓, Raf↓, cycD1/CCND1↓, SUV39H↓,

Showing Research Papers: 1 to 1 of 1

* indicates research on normal cells as opposed to diseased cells
Total Research Paper Matches: 1

Pathway results for Effect on Cancer / Diseased Cells:


NA, unassigned(tgid=0) ⓘ

SUV39H↓, 1,  

Mitochondria & Bioenergetics(tgid=3) ⓘ

Raf↓, 1,  

Cell Death(tgid=5) ⓘ

Akt↓, 1,  

Protein Folding & ER Stress(tgid=8) ⓘ

HSP90↓, 1,  

Cell Cycle & Senescence(tgid=11) ⓘ

cycD1/CCND1↓, 1,  

Proliferation, Differentiation & Cell State(tgid=12) ⓘ

ERK↓, 1,   STAT3↓, 1,  

Migration(tgid=13) ⓘ

TumCP↓, 1,  

Angiogenesis & Vasculature(tgid=14) ⓘ

EGFR↓, 1,  

Clinical Biomarkers(tgid=22) ⓘ

EGFR↓, 1,  
Total Targets: 10

Pathway results for Effect on Normal Cells:


Total Targets: 0

Scientific Paper Hit Count for: HSP90, HSP90
Query results interpretion may depend on "conditions" listed in the research papers.
Such Conditions may include : 
  -low or high Dose
  -format for product, such as nano of lipid formations
  -different cell line effects
  -synergies with other products 
  -if effect was for normal or cancerous cells

Filter Conditions: Pro/AntiFlg:%  IllCat:%  CanType:%  Cells:%  prod#:434  Target#:149  State#:%  Dir#:1
  wNotes=0  sortOrder:rid,rpid

 

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