References

Bortolotti M, Biscotti F, Zanello A, Polito L, Bolognesi A (2024) Heterophyllin: A new adenia toxic lectin with peculiar biological properties. Toxins 16(1):1. doi: 10.3390/toxins16010001 PMID: 38276525

Objective: Describe the novel type II Ribosome Inactivating Protein, Heterophyllin.

Summary: Heterophyllin, a novel toxic lectin from Adenia heterophylla shows enzymatic and lectin properties of type 2 RIPs. Heterophyllin was able to completely abolish cell viability at nM concentration. The enzymatic, immunological, and biological activities of heterophyllin provide interest in possible pharmacological application.

Usage: Saporin is used as a Type I Ribosome Inactivating Protein to compare it to Heterophyllin, a type II RIP.

Related Products: Saporin (Cat. #PR-01)

See Also:

• Bortolotti, M.; Biscotti, F.; Zanello, A.; Bolognesi, A.; Polito, L. New insights on saporin resistance to chemical derivatization with heterobifunctional reagents. Biomedicines 2023, 11, 1214.

Chan A, Tsourkas A (2024) Intracellular protein delivery: Approaches, challenges, and clinical applications. BME Frontiers 5:0035. doi: 10.34133/bmef.0035 PMID: 38282957

Objective: To review progress made towards achieving cytosolic delivery of recombinant proteins and possible strategies to enable proteins to cross cell membranes.

Summary: Drug delivery researchers have worked to deliver saporin into tumor cells in the hopes of producing potent next-generation cancer therapeutics. Cationic, anionic, and zwitterionic versions of poly(β-amino ester) have been developed for delivery of saporin. Chemically-modified saporin can be encapsulated by cationic LNPs for in vivo tumor inhibition. Saporin has been used as a model cargo protein for in vivo delivery via fluoropolymer nanoparticles for successful tumor growth inhibition.

Related Products: Saporin (Cat. #PR-01)

See Also:

• Ancheta LR et al. Saporin as a commercial reagent: its uses and unexpected impacts in the biological sciences-tools from the plant kingdom. Toxins (Basel) 14(3):184, 2022.

de Paula FS (2023) Immunomodulatory impact of memory T lymphocyties in periodontitis. Univ Minnesota Thesis.

Objective: This thesis paper sought to determine whether local reactivation of oral tissue resident memory cells (TRM) of a defined antigen specificity could exacerbate ligature-induced periodontal (LIP), a model for periodontal disease in mice.

Summary: Reactivation of oral TRM aggravated alveolar bone loss and amplified gingival and cervical lymph node (cLN) inflammation. Furthermore, oral TRM reactivation enhanced transcriptional changes in pro-inflammatory and periodontitis-related genes. Therapeutic depletion of CD103-expressing oral TRM in advanced of LIP mitigated alveolar bone loss and associated gingiva and cLN inflammation. The study provides evidence that local reactivation of oral TRM can potentiate periodontitis.

Usage: Anti-CD103-SAP (IT-50) was administered in mice via i.p. injection (7 ug in PBS).

Related Products: Anti-CD103-SAP (Cat. #IT-50)

di Leandro L, Colasante M, Pitari G, Ippoliti R (2023) Hosts and heterologous expression strategies of recombinant toxins for therapeutic purposes. Toxins (Basel) 15(12):699. doi: 10.3390/toxins15120699 PMID: 38133203

Objective: Review the recombinant expression of toxins from bacterial, plant, or animal species used as components of immunotoxins.

Summary: Commercial production of recombinant proteins for therapeutic purposes involves the utilization of various hosts, with the most common choices being bacteria, yeasts, and mammalian cell lines. The authors also provide an overview of the primary advantages and disadvantages of various systems for toxin manufacturing.

Related Products: Saporin (Cat. #PR-01)

Heck AJ (2023) Chemical design of a supramolecular protein nanoplatform for therapeutic applications. Univ Johannes Gutenberg Thesis.

Objective: Investigate the potential of using multivalent proteins as an integrative nanoplatform to target protein hallmarks in various diseases by forming supramolecular protein conjugates (SPC).

Summary: The author employs an integrative and adaptable protein-based nanoplatform to combine bioactive entities at the macromolecular level to design multivalent protein-conjugates for versatile therapeutic purposes. Multivalent protein-conjugates, a tetrameric protein with up to four ligand binding sites functions is used as a supramolecular “glue” utilizing avidin-biotin technology. The study investigates the assembly of diverse bioactive components into well organized multifunctional protein-conjugates, ultimately leading to the formation of supramolecular protein conjugates (SPC) that target protein signatures in a variety of diseases.

Usage: Streptavidin-ZAP with Anti-PSMA Antibody

Related Products: Streptavidin-ZAP (Cat. #IT-27)

See Also:

• Kuroda K et al. Saporin toxin-conjugated monoclonal antibody targeting prostate-specific membrane antigen has potent anticancer activity. Prostate 70(12):1286-1294, 2010.

Loftén A, Adermark L, Ericson M, Söderpalm B (2023) Regulation of ethanol-mediated dopamine elevation by glycine receptors located on cholinergic interneurons in the nucleus accumbens. Addict Biol 28(12):e13349. doi: 10.1111/adb.13349 PMID: 38017639

Objective: The aim of this study was to explore the role of glycine receptors (GlyRs) on cholinergic interneurons (CIN) in sustaining extracellular dopamine levels and in ethanol-induced dopamine release.

Summary: Alcohol use disorder is one of the major psychiatric disorders worldwide. Ethanol reward is one of the many factors contributing to the disorder. The rewarding and reinforcing properties of ethanol have been linked to activation of the mesolimbic dopamine system, an effect that involves glycine receptors (GlyRs) in the nucleus accumbens. The study suggests that CIN are not important for GlyR-mediated regulation of basal dopamine output, but that CIN ablation blunts the ethanol-induced dopamine release by reducing the release of GlyR agonists.

Usage: CIN were ablated by Anti-ChAT-SAP administered locally in the nucleus accumbens of male Wistar rats. Rabbit-IgG-SAP was used as a control. Microinfusion was performed unilaterally into the nAc at a concentration of 0.5 ug/ul at 0.05 ul/min for 10 min for a total of 0.5 ul.

Related Products: Anti-ChAT-SAP (Cat. #IT-42), Rabbit IgG-SAP (Cat. #IT-35)

Takanami K, Kuroiwa M, Ishikawa R, Imai Y, Oishi A, Hashino M, Shimoda Y, Sakamoto H, Koide T (2023) Function of gastrin-releasing peptide receptors in ocular itch transmission in the mouse trigeminal sensory system. Front Mol Neurosci 16:1280024. doi: 10.3389/fnmol.2023.1280024 PMID: 38098939

Objective: To investigate the role of gastrin-releasing peptide (GRP) and GRP receptor (GRPR) in itch transmission in the spinal somatosensory system, and to determine whether the GRP system is involved in itch neurotransmission of the eyes in the trigeminal sensory system

Summary: Administering itch mediators like histamine (His) and chloroquine (CQ) caused high levels of eye scratching in a concentration-dependent manner, with significant gender differences observed for His. Histological studies showed that His and CQ significantly activated GRPR-expressing neurons in a specific brain region of transgenic mice. Blocking these neurons with a GRPR antagonist or eliminating them reduced CQ-induced scratching. Injecting a GRPR agonist without an itch stimulus led to excessive facial scratching, indicating the central role of GRPR neurons in mediating itch responses.

Usage: 500 ng Blank-SAP (IT-21) or 500 ng Bombesin-SAP (IT-40) were intracisternally administered (5-uL volume) 2 weeks prior to behavioral experiments.

Related Products: Bombesin-SAP (Cat. #IT-40), Blank-SAP (Cat. #IT-21)

Singh RR, Mondal I, Janjua T, Popat A, Kulshreshtha R (2023) Engineered smart materials for RNA based molecular therapy to treat Glioblastoma. Bioact Mater 33:396-426. doi: 10.1016/j.bioactmat.2023.11.007 PMID: 38059120

Objective: A review of non-coding RNA therapy and its targeted delivery of nucleic acids to treat Glioblastoma, emphasizing smart nano-materials.

Summary: Nano-carriers of ncRNA can offer unique advantages in fighting, such as low cytotoxicity, ability to cross the blood-brain barrier, stealth to bypass immune detection, prolonged release of the cargo, improved circulatory time, and also targeted therapy.

Usage: Saporin as a payload to the nano-carriers angiopep-2 peptide and RAP12.

Related Products: Saporin (Cat. #PR-01)

Chamberlain AR, Huynh L, Huang W, Taylor DJ, Harris ME (2023) The specificity landscape of bacterial ribonuclease P. J Biol Chem 300(1):105498. doi: 10.1016/j.jbc.2023.105498 PMID: 38013087

Objective: Review of the specificity of ribonucleoprotein RNase P in binding different types of RNA.

Summary: Ribonucelase P is involved in the RNA metabolism pathways. By studying the rate at which it combines with different types of RNA under different conditions, like concentration and competition with different enzymes, a model describing its specificity to different RNA motifs can be developed.

Related Products: Saporin (Cat. #PR-01)

See Also:

• Hauf, S., Rotrattanadumrong, R., and Yokobayashi, Y. (2022) Analysis of the sequence preference of saporin by deep sequencing. ACS Chem. Biol.17, 2619–2630

Kirkey DC, Robinson L, Janssens D, Hines MG, Hylkema T, Manselle MK, Ries RE, Peplinski JH, Wallace LK, Otto D, Tarlock K, Henikoff S, Li W, Meshinchi S (2023) CLEC2A is a novel AML-restricted immunotherapeutic target enriched in KMT2A-rearranged acute myeloid leukemia. Blood 142(1):290. doi: 10.1182/blood-2023-188439

Objective: Targeting CLEC2A, a novel immunotherapeutic target, in the treatment of acute myeloid leukemia.

Summary: CLEC2A, a novel immunotherapeutic target expressed highly in acute myeloid leukemia, is a potential target in treating leukemia. By conjugating an antibody targeting this protein to saporin, an ADC for the treatment of leukemia can be created.

Usage: A CLEC2A-antibody was conjugated to Hum-ZAP [IT-22] and treated against CLEC2A+ and CLEC2A- cells and target-specific cytotoxicity was observed at 10nM levels.

Related Products: Hum-ZAP (Cat. #IT-22)