Anti-tumour effect of the physiological tetrapeptide, tuftsin

Nishioka, Kenji

doi:10.1038/bjc.1979.59

Cited by 64 publications

(8 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In direct line with the above study, the work of Nishioka (72) indicates that tuftsin may probably act as an immunotherapeutic agent. Thus, mice inoculated, intraperitoneally, simultaneously with leukemic cells (U21 0; 10 4 cells) and tuftsin (0.21Lg) had a statistically significant mean survival time, which is longer than the control group.…”

Section: Anti-tumor Ellect Of Tufisinsupporting

confidence: 71%

“…In the same study it was also demonstrated that tuftsin markedly enhanced in vivo spreading of macrophages as well as augmentation, of in vitro cytotoxicity of macrophages though at a rather moderate level (72).…”

Section: Anti-tumor Ellect Of Tufisinmentioning

confidence: 70%

“…Recently, an antitumor effect of tuftsin has been described (72,73). Though only preliminary results are available it should not be entirely and immediately excluded that combatting tumors via the reticuloendothelial system is part of the physiological role of tuftsin.…”

Section: Clinical Aspects Of Tuftsinmentioning

confidence: 99%

See 2 more Smart Citations

Tuftsin, Thr-Lys-Pro-Arg

Fridkin

Gottlieb

1981

Immunologically Active Peptides

View full text Add to dashboard Cite

Tuftsin, a natural occurring tetrapeptide, has been found to exhibit several biological activities connected with immune system function. Although little is known about tuftsin's 'biogenesis', much information has been gleaned about its structure-function relationships, which have shown that several features of the molecule are essential for expression offull biological activity. Furthermore, specific receptor sites for tuftsin have been found to exist exclusively on phagocytic cells. Research indicates that tuftsin binding to target cells effect intracellular calcium and cyclic nucleotide levels. Implication of these facts on tuftsin's mode of action are discussed.Basic peptidic segments resembling tuftsin are found in a variety of regulatory peptides. Questions are, therefore, raised as to the biospecificity and cross-reactivity of these sequences. Substance P, one such peptide, which binds with and activates tuftsin receptors, is described.In light of tuftsin's therapeutic potential, assays for its determination have been introduced. When applied to analyze human blood serum of normal as well as of various pathological origins, direct correlation was found between tuftsin levels and susceptibility to bacterial infections. Molecular and Cellular Biochemistry 41,73-97 (1981). 0300 8177/81 0041 0073/$05.00.

show abstract

Section: Anti-tumor Ellect Of Tufisinsupporting

confidence: 71%

Section: Anti-tumor Ellect Of Tufisinmentioning

confidence: 70%

See 1 more Smart Citation

Tuftsin, Thr-Lys-Pro-Arg

Fridkin

Gottlieb

1981

Immunologically Active Peptides

View full text Add to dashboard Cite

show abstract

“…Tuftsin's chief role is to stimulate several functions of phagocytic cells, primarily in the macrophage. These functions form an important component of the immune system and comprise phagocytosis, pinocytosis, mobility (4,5), chemotaxis (5)(6)(7)(8), and immunogenic activity (9), resulting in the augmentation of the number of antibody-forming cells (10,11), bactericidal activity (12), and tumoricidal activity (13)(14)(15)(16)(17)(18). The latter has been shown in mice for L1210 cells (15)(16)(17)(18) and BCL1 leukemia cells (19), several melanoma cell lines (16)(17)(18), chemically induced sarcoma (14,19), and several virally induced tumors (20)(21)(22).…”

mentioning

confidence: 99%

Isolation and subunit composition of tuftsin receptor.

Bump¹,

Lee²,

M³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Tuftsin (Thr-Lys-Pro-Ari) receptor was purified to apparent homogeneity by affinity chromatography, using a pentapeptide analog (Thr-Lys-Pro-Pro-Arg) that binds the receptor more than 4 times as avidly as tuftsin. The analog was covalently linked to a solid support (Affi-Gel 10). Rabbit peritoneal granulocyte membrane solubilized with 3-[(3-cholamidopropyl)dimethylammonio]-l-propanesulfonate was applied to the affinity column, the column was washed with 0.1 M ammonium carbonate (pH 7.9) and 0.1 M ammonium acetate (pH 5), and bound material was eluted with 20 nM tuftsin or pentapeptide. The eluate was concentrated and subjected to gel filtration; this yielded one major peak of [3lH]tuftsin binding activity corresponding to =500 kDa and a minor peak at -250 kDa. Rechromatography of either peak resulted in the appearance of the same maor and minor peaks. NaDodSO4/PAGE of the affinity-purified material under nonreducing conditions showed only two silver-staining bands.Electroblotting followed by [3H]tuftsin overlay and fluorography showed two adjacent radioactive bands corresponding in mobility to the silver-stained bands. Under reducing conditions, NaDodSO4/PAGE yielded molecular mass values 62 kDa and 52 kDa for the two tuftsin receptor subunits. Electron microscopy revealed a homogeneous population of spherical molecules with diameters of 104 A.

show abstract

“…Tuftsin is the active component of leukokinin, a cytophilic molecule that carries y-globulin (Nishioka et al, 1972). Treatment of phagocytic cells, granulocytes, monocytes and macrophages with tuftsin results in phagocytosis and pinocytosis (Najjar & Nishioka, 1970;Nishioka et al, 1973a, b;Najjar, 1974), chemotactic migration (Nishioka et al, 1973b;Najjar, 1974), bacteriocidal activity (Martinez et al, 1977), immunogenie function (Tzehovel et al, 1978;Florentin et al, 1978), and tumoricidal and tumoristatic activity (Florentin et al, 1978;Nishioka, 1979). At present, it is believed that tuftsin-specific receptors, which confer susceptibility, are present only on phagocytic cells (Stabinsky et al, 1978).…”

mentioning

confidence: 99%

Increased Expression of Endogenous Xenotropic Murine Retrovirus by Treatment with the Tetrapeptides, Tuftsin and Kentsin

Suk

Long

1981

Journal of General Virology

View full text Add to dashboard Cite

SUMMARYEnhancement of endogenous xenotropic virus expression has been found upon treatment with tetrapeptides of a high-passage clone of Balb/c (K-Balb) mouse cells transformed with Kirsten sarcoma virus. Tuftsin (Thr-Lys-Pro-Arg) and kentsin (Thr-Pro-Arg-Lys) increased the expression of virus that was infectious for rat, but not mouse, cells in a concentration-dependent fashion. The enhancement of virus expression by the tetrapeptides was proportional to the spontaneous release of virus. The infectivity of the enhanced virus was neutralized by goat anti-RLV gp70 serum. Actinomycin D inhibited the induction of virus, suggesting that enhanced expression required de novo RNA synthesis. The effects observed using K-Balb cells offer an opportunity to study the many biological effects of these peptides in a fibroblast culture system.

show abstract

Anti-tumour effect of the physiological tetrapeptide, tuftsin

Cited by 64 publications

References 16 publications

Tuftsin, Thr-Lys-Pro-Arg

Tuftsin, Thr-Lys-Pro-Arg

Isolation and subunit composition of tuftsin receptor.

Increased Expression of Endogenous Xenotropic Murine Retrovirus by Treatment with the Tetrapeptides, Tuftsin and Kentsin

Contact Info

Product

Resources

About