<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ragucci S</submitter><funding>Italian "Ministero dell'Università e della Ricerca" (MUR; Prin 2022 PNRR) entitled 'Direct or indirect effects of protein synthesis inhibitor enzymes from edible plants and mushrooms on intestinal health and microbiota'</funding><funding>European Union NextGenerationEU.</funding><pagination>135</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10975204</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>16(3)</volume><pubmed_abstract>Ribosome inactivating proteins (RIPs) are specific N-β-glycosylases that are well-characterized in plants. Their enzymatic action is to damage ribosomes, thereby blocking protein translation. Recently, several research groups have been working on the screening for these toxins in edible plants to facilitate the use of RIPs as biotechnological tools and biopesticides and to overcome public prejudice. Here, four novel monomeric (type 1) RIPs have been isolated from the seeds of &lt;i>Atriplex hortensis&lt;/i> L. var. &lt;i>rubra&lt;/i>, which is commonly known as edible red mountain spinach. These enzymes, named hortensins 1, 2, 4, and 5, are able to release the β-fragment and, like many other RIPs, adenines from salmon sperm DNA, thus, acting as polynucleotide:adenosine glycosidases. Structurally, hortensins have a different molecular weight and are purified with different yields (hortensin 1, ~29.5 kDa, 0.28 mg per 100 g; hortensin 2, ~29 kDa, 0.29 mg per 100 g; hortensin 4, ~28.5 kDa, 0.71 mg per 100 g; and hortensin 5, ~30 kDa, 0.65 mg per 100 g); only hortensins 2 and 4 are glycosylated. Furthermore, the major isoforms (hortensins 4 and 5) are cytotoxic toward human continuous glioblastoma U87MG cell line. In addition, the morphological change in U87MG cells in the presence of these toxins is indicative of cell death triggered by the apoptotic pathway, as revealed by nuclear DNA fragmentation (TUNEL assay).</pubmed_abstract><journal>Toxins</journal><pubmed_title>Hortensins, Type 1 Ribosome-Inactivating Proteins from Seeds of Red Mountain Spinach: Isolation, Characterization, and Their Effect on Glioblastoma Cells.</pubmed_title><pmcid>PMC10975204</pmcid><funding_grant_id>Prot. P2022YERKR</funding_grant_id><funding_grant_id>Italian research project "Potentiating the Italian Capacity for Structural Biology Services in Instruct Eric" (Acronym: ITACA.SB, grant number IR0000009) within the call MUR D.D. 0003264 dated 28/12/2021 PNRR M4/C2/L3.1.1</funding_grant_id><pubmed_authors>Landi N</pubmed_authors><pubmed_authors>Pedone PV</pubmed_authors><pubmed_authors>Russo V</pubmed_authors><pubmed_authors>Arcella A</pubmed_authors><pubmed_authors>Ragucci S</pubmed_authors><pubmed_authors>Oliva MA</pubmed_authors><pubmed_authors>Di Maro A</pubmed_authors><pubmed_authors>Campanile MG</pubmed_authors><pubmed_authors>Clemente A</pubmed_authors></additional><is_claimable>false</is_claimable><name>Hortensins, Type 1 Ribosome-Inactivating Proteins from Seeds of Red Mountain Spinach: Isolation, Characterization, and Their Effect on Glioblastoma Cells.</name><description>Ribosome inactivating proteins (RIPs) are specific N-β-glycosylases that are well-characterized in plants. Their enzymatic action is to damage ribosomes, thereby blocking protein translation. Recently, several research groups have been working on the screening for these toxins in edible plants to facilitate the use of RIPs as biotechnological tools and biopesticides and to overcome public prejudice. Here, four novel monomeric (type 1) RIPs have been isolated from the seeds of &lt;i>Atriplex hortensis&lt;/i> L. var. &lt;i>rubra&lt;/i>, which is commonly known as edible red mountain spinach. These enzymes, named hortensins 1, 2, 4, and 5, are able to release the β-fragment and, like many other RIPs, adenines from salmon sperm DNA, thus, acting as polynucleotide:adenosine glycosidases. Structurally, hortensins have a different molecular weight and are purified with different yields (hortensin 1, ~29.5 kDa, 0.28 mg per 100 g; hortensin 2, ~29 kDa, 0.29 mg per 100 g; hortensin 4, ~28.5 kDa, 0.71 mg per 100 g; and hortensin 5, ~30 kDa, 0.65 mg per 100 g); only hortensins 2 and 4 are glycosylated. Furthermore, the major isoforms (hortensins 4 and 5) are cytotoxic toward human continuous glioblastoma U87MG cell line. In addition, the morphological change in U87MG cells in the presence of these toxins is indicative of cell death triggered by the apoptotic pathway, as revealed by nuclear DNA fragmentation (TUNEL assay).</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Mar</publication><modification>2025-04-26T11:22:18.095Z</modification><creation>2025-04-06T13:39:00.63Z</creation></dates><accession>S-EPMC10975204</accession><cross_references><pubmed>38535801</pubmed><doi>10.3390/toxins16030135</doi></cross_references></HashMap>