PMID- 9780008
OWN - NLM
STAT- MEDLINE
DCOM- 19981123
LR  - 20131121
IS  - 0950-9232 (Print)
IS  - 0950-9232 (Linking)
VI  - 17
IP  - 7
DP  - 1998 Aug 20
TI  - Emodin (3-methyl-1,6,8-trihydroxyanthraquinone) inhibits TNF-induced NF-kappaB 
      activation, IkappaB degradation, and expression of cell surface adhesion proteins 
      in human vascular endothelial cells.
PG  - 913-8
AB  - Most inflammatory agents activate nuclear transcription factor-kappaB (NF-kappaB) 
      which results in expression of genes for cytokines, adhesion molecules, and 
      enzymes involved in amplification and perpetuation of inflammation. Emodin 
      (3-methyl-1,6,8-trihydroxyanthraquinone) is an active component from the roots of 
      Polygonum cuspidatum that has been reported to exhibit antiinflammatory 
      properties but the mechanism is not known. In the present study we investigated 
      the effects of emodin on the activation of NF-kappaB in human umbelical vein 
      endothelial cells (EC). Treatment of EC with TNF activated NF-kappaB; 
      preincubation with emodin inhibited this activation in a dose- and time-dependent 
      manner. Emodin did not chemically modify NF-kappaB subunits but rather inhibited 
      degradation of IkappaB, an inhibitory subunit of NF-kappaB. Since the promoter 
      regions of ICAM-1, VCAM-1, and ELAM-1 contain NF-kappaB binding sites and these 
      adhesion molecules are involved in the attachment of leukocytes to EC, the effect 
      of emodin on the adhesion of monocytes to EC and the expression of these adhesion 
      molecules was also studied. Treatment of EC with TNF for 6 h increased the 
      adhesion of monocytes to EC, which correlated with increases in cell surface 
      expression of ICAM-1, VCAM-1 and ELAM-1. Pretreatment of EC for 1 h with emodin 
      inhibited both monocyte-EC attachment and expression of ICAM-1, ELAM-1 and 
      VCAM-1. These results indicate that emodin is a potent inhibitor of NF-kappaB 
      activation and expression of adhesion molecules and thus could be useful in 
      treating various inflammatory diseases.
FAU - Kumar, A
AU  - Kumar A
AD  - Department of Molecular Oncology, The University of Texas MD Anderson Cancer 
      Center, Houston 77030, USA.
FAU - Dhawan, S
AU  - Dhawan S
FAU - Aggarwal, B B
AU  - Aggarwal BB
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Oncogene
JT  - Oncogene
JID - 8711562
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (E-Selectin)
RN  - 0 (I-kappa B Proteins)
RN  - 0 (NF-kappa B)
RN  - 0 (Oligodeoxyribonucleotides)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - 0 (Vascular Cell Adhesion Molecule-1)
RN  - 126547-89-5 (Intercellular Adhesion Molecule-1)
RN  - KA46RNI6HN (Emodin)
SB  - IM
MH  - Base Sequence
MH  - Binding Sites
MH  - Cell Adhesion/drug effects/physiology
MH  - Cell Adhesion Molecules/*genetics
MH  - Cells, Cultured
MH  - DNA-Binding Proteins/*metabolism
MH  - E-Selectin/genetics
MH  - Emodin/*pharmacology
MH  - Endothelium, Vascular/cytology/drug effects/*metabolism
MH  - Gene Expression Regulation/*drug effects/physiology
MH  - HIV Long Terminal Repeat
MH  - Humans
MH  - I-kappa B Proteins
MH  - Intercellular Adhesion Molecule-1/genetics
MH  - Molecular Sequence Data
MH  - NF-kappa B/antagonists & inhibitors/*metabolism
MH  - Oligodeoxyribonucleotides/chemistry/metabolism
MH  - Plant Roots
MH  - Promoter Regions, Genetic
MH  - Tumor Necrosis Factor-alpha/*pharmacology/physiology
MH  - Vascular Cell Adhesion Molecule-1/genetics
EDAT- 1998/10/21 00:00
MHDA- 1998/10/21 00:01
CRDT- 1998/10/21 00:00
PHST- 1998/10/21 00:00 [pubmed]
PHST- 1998/10/21 00:01 [medline]
PHST- 1998/10/21 00:00 [entrez]
AID - 10.1038/sj.onc.1201998 [doi]
PST - ppublish
SO  - Oncogene. 1998 Aug 20;17(7):913-8. doi: 10.1038/sj.onc.1201998.