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      Ursolic acid, a natural pentacyclic triterpenoid, inhibits intracellular trafficking of proteins and induces accumulation of intercellular adhesion molecule-1 linked to high-mannose-type glycans in the endoplasmic reticulum

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          • •

            Ursolic acid inhibits cell-surface expression of ICAM-1.

          • •

            Ursolic acid induces accumulation of high-mannose-type ICAM-1 in ER.

          • •

            Ursolic acid induces morphological changes of Golgi apparatus.

          • •

            Ursolic acid inhibits intracellular trafficking of proteins.

          Abstract

          Ursolic acid (3β-hydroxy-urs-12-en-28-oic acid) is a natural pentacyclic triterpenoid that is present in many plants, including medicinal herbs, and foods. Ursolic acid was initially identified as an inhibitor of the expression of intercellular adhesion molecule-1 (ICAM-1) in response to interleukin-1α (IL-1α). We report here a novel biological activity: ursolic acid inhibits intracellular trafficking of proteins. Ursolic acid markedly inhibited the IL-1α-induced cell-surface ICAM-1 expression in human cancer cell lines and human umbilical vein endothelial cells. By contrast, ursolic acid exerted weak inhibitory effects on the IL-1α-induced ICAM-1 expression at the protein level. Surprisingly, we found that ursolic acid decreased the apparent molecular weight of ICAM-1 and altered the structures of N-linked oligosaccharides bound to ICAM-1. Ursolic acid induced the accumulation of ICAM-1 in the endoplasmic reticulum, which was linked mainly to high-mannose-type glycans. Moreover, in ursolic-acid-treated cells, the Golgi apparatus was fragmented into pieces and distributed over the cells. Thus, our results reveal that ursolic acid inhibits intracellular trafficking of proteins and induces the accumulation of ICAM-1 linked to high-mannose-type glycans in the endoplasmic reticulum.

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          Most cited references49

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          Is NF-kappaB a good target for cancer therapy? Hopes and pitfalls.

          Véronique Baud, Michael Karin (2009)
          Nuclear factor kappaB (NF-kappaB) transcription factors have a key role in many physiological processes such as innate and adaptive immune responses, cell proliferation, cell death, and inflammation. It has become clear that aberrant regulation of NF-kappaB and the signalling pathways that control its activity are involved in cancer development and progression, as well as in resistance to chemotherapy and radiotherapy. This article discusses recent evidence from cancer genetics and cancer genome studies that support the involvement of NF-kappaB in human cancer, particularly in multiple myeloma. The therapeutic potential and benefit of targeting NF-kappaB in cancer, and the possible complications and pitfalls of such an approach, are explored.
          Article 0 comments Cited 309 times – based on 0 reviews     Review now
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            Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway.

            N Perkins (2006)
            The diverse cellular and biological functions of the nuclear factor kappa B (NF-kappaB) pathway, together with the catastrophic consequences of its aberrant regulation, demand specific and highly regulated control of its activity. As described in this review, regulation of the NF-kappaB pathway is brought about through multiple post-translational modifications that control the activity of the core components of NF-kappaB signaling: the IkappaB kinase (IKK) complex, the IkappaB proteins and the NF-kappaB subunits themselves. These regulatory modifications, which include phosphorylation, ubiquitination, acetylation, sumoylation and nitrosylation, can vary, depending on the nature of the NF-kappaB-inducing stimulus. Moreover, they frequently have distinct, sometimes antagonistic, functional consequences and the same modification can have different effects depending on the context. Given the important role of NF-kappaB in human health and disease, understanding these pathways will not only provide valuable insights into mechanism and function, but could also lead to new drug targets and the development of diagnostic and prognostic biomarkers for many pathological conditions.
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              Characterization of a cis-Golgi matrix protein, GM130

              R. Watson, P. Slusarewicz, T. Nilsson … (1995)
              Antisera raised to a detergent- and salt-resistant matrix fraction from rat liver Golgi stacks were used to screen an expression library from rat liver cDNA. A full-length clone was obtained encoding a protein of 130 kD (termed GM130), the COOH-terminal domain of which was highly homologous to a Golgi human auto-antigen, golgin-95 (Fritzler et al., 1993). Biochemical data showed that GM130 is a peripheral cytoplasmic protein that is tightly bound to Golgi membranes and part of a larger oligomeric complex. Predictions from the protein sequence suggest that GM130 is an extended rod-like protein with coiled-coil domains. Immunofluorescence microscopy showed partial overlap with medial- and trans-Golgi markers but almost complete overlap with the cis-Golgi network (CGN) marker, syntaxin5. Immunoelectron microscopy confirmed this location showing that most of the GM130 was located in the CGN and in one or two cisternae on the cis-side of the Golgi stack. GM130 was not re-distributed to the ER in the presence of brefeldin A but maintained its overlap with syntaxin5 and a partial overlap with the ER- Golgi intermediate compartment marker, p53. Together these results suggest that GM130 is part of a cis-Golgi matrix and has a role in maintaining cis-Golgi structure.
              Article 0 comments Cited 197 times – based on 0 reviews     Review now
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                Author and article information

                Contributors
                Takao Kataoka
                Journal
                Journal ID (nlm-ta): FEBS Open Bio
                Journal ID (iso-abbrev): FEBS Open Bio
                Title: FEBS Open Bio
                Publisher: Elsevier
                ISSN (Electronic): 2211-5463
                Publication date PMC-release: 22 February 2014
                Publication date (Electronic): 22 February 2014
                Publication date Collection: 2014
                Volume: 4
                Pages: 229-239
                Affiliations
                Department of Applied Biology, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan
                Author notes
                [* ]Corresponding author. Tel./fax: +81 75 724 7752. takao.kataoka@ 123456kit.ac.jp
                Article
                Publisher ID: S2211-5463(14)00020-5
                DOI: 10.1016/j.fob.2014.02.009
                PMC ID: 3958921
                PubMed ID: 24649404
                SO-VID: 3a4fe901-31d5-4bd3-8ab4-f9382fe5590e
                Copyright © © 2014 The Authors
                History
                Date received : 3 February 2014
                Date revision received : 10 February 2014
                Date accepted : 19 February 2014
                Categories
                Subject: Article

                Keywords: bsa, bovine serum albumin,endo h, endoglycosidase h,er, endoplasmic reticulum,hrp, horseradish peroxidase,huvec, human umbilical vein endothelial cells,icam-1, intercellular adhesion molecule-1,iκb, inhibitor of nuclear factor κb,il-1, interleukin-1,mtt, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide,nf-κb, nuclear factor κb,pbs, phosphate-buffered saline,pngase f, peptide: n-glycosidase f,glycosylation,golgi apparatus,intercellular adhesion molecule-1,intracellular trafficking,ursolic acid
                Data availability:
                Keywords: bsa, bovine serum albumin, endo h, endoglycosidase h, er, endoplasmic reticulum, hrp, horseradish peroxidase, huvec, human umbilical vein endothelial cells, icam-1, intercellular adhesion molecule-1, iκb, inhibitor of nuclear factor κb, il-1, interleukin-1, mtt, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide, nf-κb, nuclear factor κb, pbs, phosphate-buffered saline, pngase f, peptide: n-glycosidase f, glycosylation, golgi apparatus, intercellular adhesion molecule-1, intracellular trafficking, ursolic acid

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