tuftsin
Sign in to saveTuftsin is a tetrapeptide (Thr-Lys-Pro-Arg, TKPR) located in the Fc-domain of the heavy chain of immunoglobulin G (residues 289-292). It has an immunostimulatory effect. It is named for Tufts University where it was first discovered in 1983.
Research
689 papers- Helminth derivative tuftsin-phopshorylcholine to treat autoimmunity.Autoimmunity reviews · 2024
- Tuftsin - Properties and Analogs.Current medicinal chemistry · 2017
- FcγR-targeted tuftsin clusters rejuvenate macrophages in preclinical sepsis-associated secondary infection.Science translational medicine · 2025
- [Tuftsin].Allergie und Immunologie · 1984
- Tuftsin phosphorylcholine-a novel compound harnessing helminths to fight autoimmunity.Immunologic research · 2018
via PubMed
Wikidata facts
- Mass
- 500.307
Show 3 more facts
- chemical formula
- C₂₁H₄₀N₈O₆
- isomeric SMILES
- C[C@H]([C@@H](C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)N)O
- canonical SMILES
- CC(C(C(=O)NC(CCCCN)C(=O)N1CCCC1C(=O)NC(CCCN=C(N)N)C(=O)O)N)O
Sources (2)
via Wikidata · CC0
~7 min read
Article
13 sectionsContents
- Formation
- Function
- Phagocytosis
- Motility and chemotaxis
- Formation of reactive oxygen compounds
- Augmentation of Tumor Necrosis Factor
- Immunmodulating activity
- Effect of cell cytotoxicity
- Nontoxicity for animals and humans
- Pathology
- Clinical significance
- Tuftsin analogues
- References
Tuftsin is a tetrapeptide (Thr-Lys-Pro-Arg, TKPR) located in the Fc-domain of the heavy chain of immunoglobulin G (residues 289-292). It has an immunostimulatory effect. It is named for Tufts University where it was first discovered in 1983.
==Formation== Two enzymes are needed to release tuftsin from immunoglobulin G.First, the spleen enzyme tuftsin-endocarboxypeptidase nicks the heavy chain at the Arg-Glu bond (292-293). The arginine carboxy-terminal is now susceptible to the action of the second enzyme, carboxypeptidase β. The leukokinin-S so nicked is present in tissues and blood, free or bound to outer membrane of the appropriate phagocyte. The membrane enzyme leukokininase acts on the bound leukokinin-S to cleave it at the amino end of threonine between residues 288 and 289 (-Lys-Thr-). Free tuftsin is biologically active. The phagocytic cell plays a unique role in releasing its own activator. Leukokininase can be found on the outer membrane of phagocytic cells: blood neutrophil leukocytes of human and dog, rabbit peritoneal granulocyte. It is a highly active enzyme with pH optimum:6.8.