Ubiquitin and Ubiquitination in Cells from the Marine Sponge<i>Geodia cydonium</i>

Müller, Wernér E.G.; Gamulin, Vera; Rinkevich, Baruch; Spreitzer, Ingo; Weinblum, D.; Schröder, Heinz C.

doi:10.1515/bchm3.1994.375.1.53

Cited by 14 publications

(6 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The two NF-B-inhibiting marine natural products macrolide bryostatin 1 isolated from a bryozoan [56] and salinosporamide A isolated from a bacterium [24] are currently in clinical trials [58]. Several ecological reasons why marine natural products may inhibit NF-B have been established [20,21,[59][60][61][62][63][64][65][66][67][68][69].…”

Section: Discussionmentioning

confidence: 99%

The inhibition of TNF-α-induced NF-κB activation by marine natural products

Folmer

Jaspars

Solano

et al. 2009

Biochemical Pharmacology

View full text Add to dashboard Cite

, et al.. The inhibition of TNF-α induced NF-κB activation by marine natural products. Biochemical Pharmacology, Elsevier, 2009, 78 (6) This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A c c e p t e d M a n u s c r i p t 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 65 AbstractThe deregulated activation of NF-B is associated with cancer development and inflammatory diseases. With the aim to find new NF-B inhibitors, we purified and characterized compounds from extracts of the Fijian sponge Rhabdastrella globostellata, the crinoid Comanthus parvicirrus, the soft corals Sarcophyton sp. nov. and Sinularia sp., and the gorgonian Subergorgia sp. after an initial screening of 266 extracts from different marine origins.Results obtained show that selected purified compounds had a cytotoxic effect on the human leukaemia cell line K562, inhibited both TNF--induced NF-B-DNA binding as well as TNF- induced IB degradation and nuclear translocation of p50/p65. Furthermore, we observed inhibition of NF-B activation induced by an overexpression of TNFR1, TRAF2, TRADD, or IKK Interestingly, natural products inhibited IKK kinase as well as the 26S proteasome proteolytic activity.

show abstract

Section: Discussionmentioning

confidence: 99%

The inhibition of TNF-α-induced NF-κB activation by marine natural products

Folmer

Jaspars

Solano

et al. 2009

Biochemical Pharmacology

View full text Add to dashboard Cite

show abstract

“…Müller et al [184] observed that after the addition of purified AF to primary G. cydonium cell aggregates, DNA, RNA, and protein synthesis increased, and that the cells exhibited a high mitotic activity. Transcription of polyubiquitin mRNA was greatly increased when the dissociated cells were incubated with AF [185,186]. Binding of AF to the cells triggered protein phosphorylation [187] and ras gene expression [188,189].…”

Section: Involvement Of Spongicans In Signal Transduction Processesmentioning

confidence: 99%

Circular proteoglycans from sponges: first members of the spongican family

Fernàndez‐Busquets

Burger

2003

Cellular and Molecular Life Sciences (CMLS)

View full text Add to dashboard Cite

Species-specific cell adhesion in marine sponges is mediated by a new family of modular proteoglycans whose general supramolecular structure resembles that of hyalectans. However, neither their protein nor their glycan moieties have significant sequence homology to other proteoglycans, despite having protein subunits equivalent to link proteins and to proteoglycan monomer core proteins, and glycan subunits equivalent to hyaluronan and to the glycosaminoglycans of hyalectans. In some species, these molecular components are assembled into a structure with a circular core formed by the link protein- and hyaluronan-like subunits. Besides their involvement in cell adhesion, these sponge proteoglycans, for which we propose the term spongicans, participate in signal transduction processes and are suspected to play a role in sponge self-nonself recognition. Their in vivo roles and the mild methods used to purify large amounts of functionally active spongicans make them ideal models to study the functions and possible new applications of proteoglycans in biomedical research.

show abstract

“…The addition of purified AF to primary cell aggregates of the marine sponge Geodia cydonium resulted in increased DNA, RNA, and protein synthesis, as well as in a higher mitotic activity (Mü ller et al, 1976(Mü ller et al, , 1994Pfeifer et al, 1993). Binding of AF to the cells also triggered protein phosphorylation (Rottmann et al, 1987) and ras gene expression (Schröder et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

Supramolecular Structure of a New Family of Circular Proteoglycans Mediating Cell Adhesion in Sponges

Jarchow

Fritz²,

Anselmetti

et al. 2000

Journal of Structural Biology

100

View full text Add to dashboard Cite

Aggregation factors are the molecules responsible for species-specific cell adhesion in sponges. Here, we present the structure of the aggregation factor from the marine sponge Microciona prolifera, which constitutes the first description of a circular proteoglycan. We have analyzed chemically dissociated and enzymatically digested aggregation factor with atomic force microscopy, agarose gel electrophoresis, and Western blots using antibodies against the protein and carbohydrate moieties. Twenty units from each of two N-glycosylated proteins, MAFp3 and MAFp4, form the central ring and radiating arms, respectively, stabilized by a hyaluronidase-sensitive component. MAFp3 carries a 200-kDa glycan involved in homologous self-interactions between aggregation factor molecules, whereas MAFp4 carries a 6-kDa glycan that binds cell surface receptors. A 68-kDa lectin found in cell membranes of several sponge species binds the aggregation factor and its protein-free glycans, as well as chondroitin sulfate and hyaluronan. Here, we show that despite their lack of clear sequence homologies with other known proteoglycan structures, the protein and carbohydrate components of sponge aggregation factors assemble to form a supramolecular complex remarkably similar to classical proteoglycans.

show abstract

Ubiquitin and Ubiquitination in Cells from the Marine SpongeGeodia cydonium

Cited by 14 publications

References 14 publications

The inhibition of TNF-α-induced NF-κB activation by marine natural products

The inhibition of TNF-α-induced NF-κB activation by marine natural products

Circular proteoglycans from sponges: first members of the spongican family

Supramolecular Structure of a New Family of Circular Proteoglycans Mediating Cell Adhesion in Sponges

Contact Info

Product

Resources

About