Ebulitins: A new family of type 1 ribosome-inactivating proteins (rRNAN-glycosidases) from leaves ofSambucus ebulusL. that coexist with the type 2 ribosome-inactivating protein ebulin 1

FEBS Letters ◽  
1995 ◽  
Vol 360 (3) ◽  
pp. 299-302 ◽  
Keyword(s):  
Ribosome Inactivating Protein ◽  
Ribosome Inactivating Proteins ◽  
New Family

scholarly journals Sensitivity of Translation byBrevibacterium lactofermentumRibosomes to Type 1 and Type 2 Ribosome-inactivating Proteins

1994 ◽  
Vol 58 (8) ◽  
pp. 1458-1462 ◽  
Author(s):  
José Miguel Ferreras ◽  
Carlos Alegre ◽  
Rosario Iglesias ◽  
Tomás Girbes
Keyword(s):  
Ribosome Inactivating Proteins

scholarly journals Production of Active Nonglycosylated Recombinant B-Chain of Type-2 Ribosome-Inactivating Protein fromViscum articulatumand Its Biological Effects on Peripheral Blood Mononuclear Cells

2011 ◽  
Vol 2011 ◽  
pp. 1-9
Author(s):  
Tzu-Li Lu ◽  
Jing-Yuan Chuang ◽  
Jai-Sing Yang ◽  
Shau-Ting Chiu ◽  
Nai-Wan Hsiao ◽  
...  
Keyword(s):  
Mononuclear Cells ◽  
Biological Effects ◽  
Ribosome Inactivating Protein ◽  
Peripheral Blood Mononuclear ◽  
Ribosome Inactivating Proteins ◽  
Preferential Binding ◽  
A Chain ◽  
Low Ionic Strength

Type-2 ribosome-inactivating proteins, composed of a toxic A-chain and lectin-like B-chain, display various biological functions, including cytotoxicity and immunomodulation. We here cloned the lectin-like B-chain encoding fragment of a newly identified type-2 RIP gene,articulatingene, fromViscum articulatum, into a bacterial expression vector to obtain nonglycosylated recombinant protein expressed in inclusion bodies. After purification and protein refolding, soluble refolded recombinant articulatin B-chain (rATB) showed lectin activity specific toward galactoside moiety and was stably maintained while stored in low ionic strength solution. Despite lacking glycosylation, rATB actively bound leukocytes with preferential binding to monocytes andin vitrostimulated PBMCs to release cytokines without obvious cytotoxicity. These results implicated such a B-chain fragment as a potential immunomodulator.

scholarly journals Cytotoxicity Effect of Quinoin, Type 1 Ribosome-Inactivating Protein from Quinoa Seeds, on Glioblastoma Cells

Toxins ◽  
2021 ◽  
Vol 13 (10) ◽  
pp. 684
Author(s):  
Rossella Rotondo ◽  
Sara Ragucci ◽  
Salvatore Castaldo ◽  
Maria Antonietta Oliva ◽  
Nicola Landi ◽  
...  
Keyword(s):  
Cell Lines ◽  
Chemotherapeutic Agent ◽  
Primary Cells ◽  
Glioblastoma Cells ◽  
Ribosome Inactivating Protein ◽  
Primary Glioblastoma ◽  
Ribosome Inactivating Proteins ◽  
Primary Cell Lines ◽  
Target Cancer

Ribosome-inactivating proteins (RIPs) are found in several edible plants and are well characterized. Many studies highlight their use in cancer therapy, alone or as immunoconjugates, linked to monoclonal antibodies directed against target cancer cells. In this context, we investigate the cytotoxicity of quinoin, a novel type 1 RIP from quinoa seeds, on human continuous and primary glioblastoma cell lines. The cytotoxic effect of quinoin was assayed on human continuous glioblastoma U87Mg cells. Moreover, considering that common conventional glioblastoma multiforme (GBM) cell lines are genetically different from the tumors from which they derive, the cytotoxicity of quinoin was subsequently tested towards primary cells NULU and ZAR (two cell lines established from patients’ gliomas), also in combination with the chemotherapeutic agent temozolomide (TMZ), currently used in glioblastoma treatment. The present study demonstrated that quinoin (2.5 and 5.0 nM) strongly reduced glioblastoma cells’ growth. The mechanisms responsible for the inhibitory action of quinoin are different in the tested primary cell lines, reproducing the heterogeneous response of glioblastoma cells. Interestingly, primary cells treated with quinoin in combination with TMZ were more sensitive to the treatment. Overall, our data highlight that quinoin could represent a novel tool for glioblastoma therapy and a possible adjuvant for the treatment of the disease in combination with TMZ, alone or as possible immunoconjugates/nanoconstructs.

scholarly journals KMT2C/D COMPASS complex-associated diseases [KCDCOM-ADs]: an emerging class of congenital regulopathies

2020 ◽  
Vol 12 (1) ◽  
Author(s):  
William J. Lavery ◽  
Artem Barski ◽  
Susan Wiley ◽  
Elizabeth K. Schorry ◽  
Andrew W. Lindsley
Keyword(s):  
System Development ◽  
Cell Types ◽  
Nervous System Development ◽  
Syndrome Type ◽  
New Family ◽  
Histone 3 ◽  
Kleefstra Syndrome ◽  
Evolutionarily Conserved

AbstractThe type 2 lysine methyltransferases KMT2C and KMT2D are large, enzymatically active scaffold proteins that form the core of nuclear regulatory structures known as KMT2C/D COMPASS complexes (complex of proteins associating with Set1). These evolutionarily conserved proteins regulate DNA promoter and enhancer elements, modulating the activity of diverse cell types critical for embryonic morphogenesis, central nervous system development, and post-natal survival. KMT2C/D COMPASS complexes and their binding partners enhance active gene expression of specific loci via the targeted modification of histone-3 tail residues, in general promoting active euchromatic conformations. Over the last 20 years, mutations in five key COMPASS complex genes have been linked to three human congenital syndromes: Kabuki syndrome (type 1 [KMT2D] and 2 [KDM6A]), Rubinstein-Taybi syndrome (type 1 [CBP] and 2 [EP300]), and Kleefstra syndrome type 2 (KMT2C). Here, we review the composition and biochemical function of the KMT2 complexes. The specific cellular and embryonic roles of the KMT2C/D COMPASS complex are highlight with a focus on clinically relevant mechanisms sensitive to haploinsufficiency. The phenotypic similarities and differences between the members of this new family of disorders are outlined and emerging therapeutic strategies are detailed.

The type-1 and type-2 ribosome-inactivating proteins from Iris confer transgenic tobacco plants local but not systemic protection against viruses

Planta ◽  
2004 ◽  
Vol 220 (2) ◽  
pp. 211-221 ◽  
Author(s):  
Frank Vandenbussche ◽  
Willy J. Peumans ◽  
Stijn Desmyter ◽  
Paul Proost ◽  
Marialibera Ciani ◽  
...  
Keyword(s):  
Transgenic Tobacco ◽  
Transgenic Tobacco Plants ◽  
Tobacco Plants ◽  
Ribosome Inactivating Proteins

scholarly journals Iris Bulbs Express Type 1 and Type 2 Ribosome-Inactivating Proteins with Unusual Properties

2001 ◽  
Vol 125 (2) ◽  
pp. 866-876 ◽  
Author(s):  
Qiang Hao ◽  
Els J.M. Van Damme ◽  
Bettina Hause ◽  
Annick Barre ◽  
Ying Chen ◽  
...  
Keyword(s):  
Ribosome Inactivating Proteins

scholarly journals Type 1 ribosome-inactivating proteins are the most abundant proteins in iris (Iris hollandica var. Professor Blaauw) bulbs: characterization and molecular cloning

1997 ◽  
Vol 324 (3) ◽  
pp. 963-970 ◽  
Author(s):  
Els J. M. VAN DAMME ◽  
Annick BARRE ◽  
Luigi BARBIERI ◽  
Paola VALBONESI ◽  
Pierre ROUGE ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Nitrogen Storage ◽  
Related Protein ◽  
Ribosome Inactivating Protein ◽  
Storage Organ ◽  
Abundant Protein ◽  
Ribosome Inactivating Proteins ◽  
Sequence Identity ◽  
High Degree

The most abundant protein of Iris bulbs has been identified as a type 1 ribosome-inactivating protein (RIP). Analysis of the purified proteins and molecular cloning of the corresponding cDNAs demonstrated that this type 1 RIP is a mixture of three isoforms that exhibit a high degree of sequence identity and have similar, though not identical, ribosome-inactivating and polynucleotide:adenosine glycosidase activities. The accumulation of large quantities of type 1 RIP in a vegetative storage organ suggests that this presumed defence-related protein also plays a role in the nitrogen-storage metabolism of the bulb.

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