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PubMed1993

[Autologous spleen transplantation].

Splenectomy is known to increase the risk of overwhelming bacterial infection. There is a decrease in immunoglobulin IgM, T-lymphocytes, impaired primary antibody response to antigen challenge, an altered opsonic function and a tuftsin deficiency. Splenic autotransplantation has been suggested as a method of preserving function and this concept is supported by experiments in animals (dogs). The study describes autotransplantation of the traumatized spleen in human beings for the preservation of splenic function. Eleven patients operated on for abdominal trauma in the Kenézy Hospital in Debrecen, required total splenectomy, than splenic autotransplantation. In these patients splenic slides were implanted in between two layers of omental pouch (Furka's "spleen chip"). In 10 patients the follow-up radionuclid imaging, the IgM level, and the tuftsin level unambiguously confirmed the functioning of the splenic tissue.

Abdominal Injuries↗
PubMed1993

Cytokine mediation of the suppressive effect of ferritin on colony-stimulating factor-1-dependent monocytopoiesis.

Peptide-specific IgG from a rabbit immunized with an alanine-lysine-proline-arginine ((ALA1)-tuftsin) containing 14-mer "ferritin" peptide neutralized rat liver ferritin inhibition of in vitro CSF-1-dependent monocytopoiesis. Antiferritin IgG similarly neutralized the inhibitory effect of ferritin but did not neutralize peptide inhibition of the in vitro myelopoietic response. No cross-reactivity between the respective antibodies and Ag was detected either by Western immunoblot or by competitive ELISA. Depletion of adherent cells before marrow cell culture significantly reduced the inhibitory effect of ferritin but did not influence peptide inhibition of CSF-1-stimulated colony formation. Adherent marrow cells and P388D1 cells treated with both CSF-1 and ferritin, but not either alone, produced inhibitory supernatant culture media that were neutralized by antipeptide but not antiferritin IgG. High resolution molecular sieve chromatography of the inhibitory adherent marrow cell and P388D1 supernatants resolved two peaks of 50 to 60 kDa and approximately 30 kDa in each. The inhibitory activity in all four peaks was neutralized by antipeptide but not antiferritin IgG. The ferritin/CSF inhibitors were not further characterized although identity with IL-6, IL-8, TNF-alpha, transforming growth factor-beta, and IFN-alpha/beta could be eliminated. The results indicate that ferritin inhibition of CSF-1-dependent monocytopoiesis is mediated by an endogenously produced inhibitor, or inhibitors, that shares antigenic similarity with the (ALA1)-tuftsin-containing 14-mer peptide and that adherent marrow cells, most likely monocytes or macrophages, produce the endogenous inhibitors in response to both CSF-1 and ferritin.

Amino Acid Sequence↗
PubMed1997

Splenic autotransplantation after abdominal trauma in childhood. Clinical and experimental data.

Splenectomy is known to increase the risk of overwhelming bacterial infection. There is a decrease in immunoglobulin IgM and T-lymphocytes, primary antibody response to antigen challenge is impaired, altered opsonic function an Tuftsin deficiency are noted. Splenic autotransplantation has been suggested as a method of preserving function and this concept is supported by experiments in animals. Prior to operation on humans the technique was thoroughly elaborated and practised in animal experiments (dogs). After splenectomy, 6-8 thin segments (Furka's "spleen chip") are placed in between the plates of the major omentum. Within the period of ten years out of 52 patients 11 children (4 girls, 7 boys) suffered from abdominal trauma underwent total splenectomy, and than autotransplantation in the Kenézy Hospital in Debrecen, Hungary. In several patients the postoperative follow-up radionuclide imaging, IgM, and Tuftsin levels, and the haematological changes (leukocytes, differential blood count, platelet count, iron level in serum) unambiguously confirmed the function of the splenic tissue.

Abdominal Injuries↗
PubMedDate not supplied

The search for inhibitors of interleukin-1 based on the sequence of interleukin-1 receptor antagonist.

In order to find the low-molecular-weight interleukin-1 (IL-1) inhibitors, we synthesised a series of peptides, derived from three regions of interleukin-1 receptor antagonist (IL-1ra): N-terminal (residues 5-9), central (90-98) and C-terminal (143-148). The decision was based on the thorough analysis of structural and functional properties of IL-1 proteins and the resemblance of some fragments of IL-1ra to well-known immunomodulators, like thymopentin and tuftsin. The competition between our peptides and IL-1 were measured as the inhibition of IL-1 induced IL-2 production in LBRM/CTLL cell line system. All peptides presented some activity, although the most interesting results (when the range of activity and dose-dependence were taken into account) were obtained for tuftsin and peptide VTKFYF from the C-terminal part of IL-1ra.

Amino Acid Sequence↗
PubMed1983

Structural requirements for microvascular permeability-increasing ability of peptides. Studies on analogues of a fibrinogen pentapeptide fragment.

A pentapeptide, Ala-Arg-Pro-Ala-Lys, liberated from fibrinogen during plasmin-mediated fibrinolysis, was shown earlier to increase microvascular permeability in rat and human skin. Eighteen new analogues have now been synthesized in addition to the 15 previously prepared and examined for their effect on permeability. The old concept that a tetrapeptide with basic amino acids at both ends and a proline residue adjacent to the N-terminal amino acid is essential for high activity on permeability, has now been challenged. The results obtained with several of the new analogues strengthen this concept. More interestingly, however, the third amino acid, which was found in earlier studies to be less sensitive to exchange, has now been deleted as well as duplicated with only a modest loss of activity of the peptide. The chirality of the C-terminal amino acid, most surprisingly, does not seem to be crucial for peptide activity. Slightly superpotent analogues were obtained on amidation of the C-terminus. In addition, a few naturally occurring peptides, namely tuftsin, substance P, neurotensin and bradykinin, the amino acid sequences of which all exhibit characteristic features of some of our active peptide analogues were investigated in the same test system. Tuftsin displayed a potency equal to that of the pentapeptide. The other three peptides were all highly superpotent in this assay system.

Animals↗
PubMed1992

Immunospecificity and affinity studies on anti-luteinizing hormone releasing hormone antibodies developed by azo-LHRH-TT and azo-LHRH-BSA conjugates.

Monoclonal and conventional antibodies against the 'self' decapeptide LHRH produced by azo-LHRH-TT and azo-LHRH-BSA conjugates were studied for immunoreactivity with native LHRH, azo-LHRH, LHRH (OH) and its fragments of sequence 1-10, 7-10, 4-10 and 4-6. The CoAb reacted 8-20% to azo-LHRH, 2-6% to LHRH-Lys, 1-3% LHRH-LYS-MDP and 0.5-1.68% to LHRH-Ala-Ala-Tuftsin but failed to react to LHRH free acid and its fragments. On the other hand MoAb reacted 4-6% to azo-LHRH and 10-18% to LHRH-Lys, 3-5% to LHRH-Ala-Ala-Tuftsin. These results indicate that the azotization drastically inhibited immunoreactivity but that the azo-LHRH-carrier conjugate preserved the immunogenic epitope responsible for the induction of an effective anti-LHRH antibody response.

Amino Acid Sequence↗
PubMedDate not supplied

[Properties and specificity of cathepsin H from the bovine spleen].

Action of cathepsin H from bovine spleen on tuftsin, enkephalin, the oxidized B chain of insulin and a variety of synthetic substrates was studied. Cathepsin H splits off only one N-terminal amino acid from each tuftsin and enkephalin, which, according to the literature, led to inactivation of peptides. The enzyme acts on the oxidized B chain of insulin as an aminoendopeptidase: it splits off the N-terminal phenylalanine and the centrally located bond(s). Km and Vmax for the cathepsin H catalyzed hydrolysis of LeuNA, ArgNA LysNA and BANA were determined. Substrates with the free NH2 group were hydrolyzed at a higher rate. Based on the data obtained and the previously reported results on conversion of kallidin into bradykinin, the specificity of cathepsin H and its possible biological functions were discussed. Cathepsin H appears to participate in formation and inactivation of physiologically active peptides. Using the antiserum to spleen cathepsin H it was found that liver, kidney and lung tissues contained the enzymes identical and/or partially identical to cathepsin H from spleen. The data on the properties of cathepsin H from various sources are summarized.

Animals↗
PubMed1986

[Inhibition of the binding and activation of the first component of human complement. The effect of synthetic peptides, immunoglobulin fragments and various proteins].

A study has been carried out on the inhibition of the subcomponent Clq binding to sensitized sheep erythrocytes (EA) by the following synthetic peptides mimicking the structure of a putative complement binding site of immunoglobulin G: Boc-Trp-Tyr, Boc-Tyr-Trp, Trp-Tyr, Boc-Trp-Phe, Boc-D-Trp-D-Tyr, Boc-D-Tyr-D-Trp, Boc-Leu-Leu, Ac-Phe-Tyr, and commercial Thr-Lys-Pro-Arg (tuftsin). Boc-Trp-Tyr was found to be the most potent inhibitor of Clq binding to EA (Ki 2.86 X 10(-4) M), tuftsin ranking second with Ki 6 X 10(-4) M. The D,D-dipeptides failed to inhibit the Clq binding at the investigated concentrations. Insoluble Z-Trp-Tyr-OMe activated a classical pathway of complement system, as monitored by consumption of C4, C2 and C3 components. Synthetic octapeptide Boc-Glu-Val-Asp-Leu-Leu-Lys-Asp-Glu-OMe (corresponding to the sequence 36-43 of beta 2-microglobulin) inhibited the Clq binding with Ki 4.7 X 10(-4) M, which gave grounds for localizing the complement binding site in beta 2-microglobulin. The finding in the Clq structure of the peptide sequence homologous to than of the pepsin active site, as well as the close similarity in the specificity of these proteins towards hydrophobic amino acid residues justified the assumption on the same structural bases of their specificity. The results of the present study, along with the literature data, underlie the hypothesis on the involvement in the complement binding of the following IgG residues: Trp277, Tyr278, Lys320, Lys322, Glu318 and Lys290. The enlisted residues are closely located in the three-dimensional structure of the CH2 domain of IgG. Lysozyme and lactalbumin having the sequences homologous to Trp277-Tyr278 of IgG inhibited Clq binding to EA with Ki 3 and 1.5 microM respectively.

Amino Acid Sequence↗
PubMed1993

Possible action of human placental aminopeptidase N in feto-placental unit.

Aminopeptidase N purified from human placenta actively hydrolyzed various immunomodulating peptides from their N-terminus such as splenopentin, thymopentin, thymic humoral factor gamma 2, tuftsin and rigin in vitro. Aminopeptidase N also actively hydrolyzed neuropeptide hormones (met-enkephalin, somatostatin and neurokinin A) and vasoactive peptides (lysyl-bradykinin and angiotensin III) from their N-terminus. In addition, angiotensin II, secretin, thymopoietin II peptide fragment, motilin, endothelin-I and insulin were tested for hydrolysis by aminopeptidase N. Km and Vmax values for the N-terminal amino acid, Thr, a liberation from tuftsin were 267 microM and 8.33 mumol/min/mg protein, respectively. L-Leucyl-p-nitroanilidase activity in the human placental membrane fraction was almost completely neutralized by anti-aminopeptidase N antibody. Our present study suggests that possible roles for surface enzyme aminopeptidase N in the human placenta would be to down-regulate the action of immunomodulating peptides as well as vasoactive and neuropeptide hormones, and to control both immunology and endocrinology of pregnancy.

Amino Acid Sequence↗
PubMed1989

Modulation of phagocytic activity in cultured Sertoli cells.

Phagocytic activity of rat Sertoli cells that were cultured in vitro has been evaluated as the ability to internalize polystyrene beads. Our data demonstrate that these cells are active phagocytes and that such phagocytic activity is under negative control by follicle-stimulating hormone (FSH). The hormonal control is mediated by increased intracellular levels of cAMP. Moreover Sertoli cell responds to tuftsin, an oligopeptide known to act only on macrophages and granulocytes, by increasing up to five times its phagocytic activity. Phagocytic uptake of polystyrene beads is associated with dramatic changes of the cellular shape. Such morphological modifications are significantly reduced under FSH stimulation. The physiological implications of the data are discussed.

Animals↗
PubMed1982

Mechanisms controlling differentiation and function of antigen-presenting macrophages.

We have briefly reviewed our studies on the mechanisms controlling the differentiation and activation of peritoneal antigen-presenting cells. We demonstrated that the peritoneal population is composed of two main subsets of cells, only one of which participates actively in primary antigen presentation. The latter is missing in athymic mice and seems to differentiate under the influence of the shortlived, cortisone-resistant subpopulation of thymocytes. The maturation of the peritoneal macrophages is subjected also to an additional inducing effect, that of the spleen. Macrophages from splenectomized donors are impaired both with respect to antigen presentation to naive and to primed lymphocytes, and with respect to phagocytosis of "opsonized" bacteria. The mature antigen-presenting cell is subjected to activating signals deriving from the Fc-bound Ig molecule. This is mediated via a tetrapeptide, tuftsin, which is cleaved off the CH2 portion of the Ig and activates the immunogenic effect of the antigen-pulsed macrophage.

Animals↗
PubMed1979

Specific isolation of biologically-active peptides by means of immobilized anhydrotrypsin and anhydrochymotrypsin.

Anhydrotrypsin, a derivative of bovine trypsin, immobilized on Sepharose tightly adsorbs various peptides containing L-arginine at the carboxyl termini, such as bradykinin and tuftsin. These peptides correspond to the specific products of the action of trypsin-like enzymes. Native trypsin immobilized on Sepharose does not show such strong affinity. Fragment 2, a peptide with 41 amino acid residues, which has been released together with bradykinin from bovine high-molecular-weight kininogen by the action of plasm kallikrein, is also adsorbed on the immobilized anhydrotrypsin. When only the carboxyl-terminal arginine is removed with carboxy-peptidase B, however, the peptide loses its adsorptive ability. Immobilized anhydrochymotrypsin, on the other hand, exerts specific affinity for the peptides which correspond to the products of chymotrypsin. These results suggest that the anhydro-derivatives of serine-proteseas in general may be of great use in the affinity chromatography of respective series of various naturally occurring peptides.

Amino Acid Sequence↗
PubMed1982

Effect of immunomodulating agents on leucocyte chemotaxis and cyclic nucleotides.

We have studied the effect of immunomodulating agents on polymorphonuclear leucocyte chemotaxis and their relation to the modification of cyclic nucleotide levels. The tested drugs (levamisole, tuftsin, azimexon, muramyl dipeptide, isoprinosine) inhibited the chemotaxis of 'normal' cells but restored the impaired chemotactic responsiveness of inflammatory cells. None of these drugs had any significant effect on cyclic nucleotide levels in 'normal' cells. All the drugs, except isoprinosine, produced an increase in the cGMP levels in inflammatory cells. These results suggest that immunomodulators are able to modify PMN chemotaxis. This effect cannot, however, be related to modification of the cyclic nucleotide levels.

Acetylmuramyl-Alanyl-Isoglutamine↗
PubMed1986

Regulation of macrophage phagocytosis.

The removal of pathogens from the circulation is achieved primarily by cells of the mononuclear phagocyte system, also known as the reticuloendothelial system. The tissue macrophage is the most important component of this system. The phagocytic activity of macrophages is regulated by opsonins on pathogenic materials and by endogenous cytokines. A number of diseases are caused by qualitative or quantitative disorders of phagocytosis by four major mechanisms: a decrease in the flow of blood to organs which contain macrophages (e.g. congestive heart failure and portal hypertension); a decrease in the quantity of tissue which contains macrophages (e.g. hepatic cirrhosis and splenectomy); a decrease in the effective opsonization of pathogens because of a deficiency of complement or IgG; and qualitative dysfunction of macrophages due to a deficiency of regulatory cytokines (e.g. gamma interferon and tuftsin) or a direct inhibitory effect on the macrophage (e.g. viral infections). New approaches for selective regulation of the phagocytic activity of macrophages are emerging.

Anemia, Sickle Cell↗
PubMed1989

Covalent peptide transfer to cell membrane proteins (peptidyl transferase).

HL60 cells, rabbit peritoneal granulocytes or membrane preparations of these cells incorporate radioactivity when reacted with the radioactive peptide tuftsin [3H Pro3]-Thr-Lys-Pro-Arg. The radioactivity which is not diminished by repeated treatments with TCA and NaOH, is covalently bound to a membrane acceptor protein of 100 kDa. The peptide is not displaced by large concentrations of its constituent amino acids. The acceptor protein is resolved into one labeled peak by gel filtration on Sephadex G-200, Sephacryl S-300 and by SDS-PAGE. Digestion by trypsin and chymotrypsin results in the production of smaller fragments.

Acyltransferases↗
PubMed1983

The effect of oligopeptides on the C3b receptor-mediated functions of rat macrophages.

Effects of various substances known to influence macrophage functions on the adherence of C3b-coated sheep erythrocytes (E-C3b) and their phagocytosis by elicited rat peritoneal macrophages (PM) has been studied. Different oligopeptides (OP) having a chemotactic effect, such as tuftsin, angiotensin II (At II) and the OP-fraction of a lymphokine preparation (LK-OP) increased both adherence and phagocytosis of E-C3b in a concentration-dependent fashion. In contrast, neither substances influencing the membrane cation transport nor prostaglandins (PG) and cyclic nucleotides significantly changed the C3b receptor (C3bR)-dependent effector functions of macrophages. Enhanced functions of the C3bR were not associated with an increased capability of PMs for intracellular killing of Candida albicans.

Angiotensin II↗
PubMed1995

Polytuftsin: its possible effects and mechanism during macrophage activation.

Polytuftsin (PT) a 35-40 repeat unit of tuftsin (TKPR), when administered as a conjugate with the malarial peptide, ring-infected erythrocyte surface antigen (RESA), enhanced antigen-induced lymphoproliferation and antibody levels in mice as compared to RESA alone. This enhancement was unrelated to the H-2 background of the animals. The present study was undertaken with a view to understanding the mechanism(s) responsible for this immune enhancement. Peritoneal adherent cells (PAC) from H-2b and H-2d mice were incubated with RESA alone, PT-conjugated RESA, a physical mixture of RESA + PT and PT alone. They were subsequently evaluated for I-A expression using monoclonal antibodies and flow cytometry as well as cell-ELISA. Significant increase in I-A expression on PAC was observed in all 4 groups as compared to untreated cells. Whereas cells treated with PT-conjugated RESA showed highly significant increase in I-A (P < 0.001), the other groups showed moderate increase (P < 0.05). This enhancement was attributable to increase in the number of I-A-positive cells rather than I-A molecules per cell. Moreover, IL-1 release, as assayed by bioassay, was significantly higher in cells treated with conjugated RESA as compared to cells treated with RESA or PT alone (P < 0.05). Thus, it would appear that PT-conjugated RESA peptide of the malarial antigen selectively enhances major histocompatibility complex (MHC) class II molecules on antigen-presenting cells (APC) and may therefore improve immune functions by stimulating better antigen presentation and proliferation of T cells.

Adjuvants, Immunologic↗
PubMed1994

Rat brain microglia and peritoneal macrophages show similar responses to respiratory burst stimulants.

Respiratory burst activity was compared between cultured newborn rat microglia and directly harvested adult rat peritoneal macrophages using a Clarke oxygen electrode system. Both types of cells showed stimulated oxygen consumption almost immediately after the administration of opsonized zymosan, phorbol myristate acetate, concanavalin A, or tuftsin. The absolute values of stimulated oxygen consumption after administration of these agents ranged from 0.11 to 0.99 nmol per min per million cells, with some variation in relative response of microglia compared with peritoneal macrophages. After lysis of cells with deoxycholate, or disruption by sonication, oxygen consumption was restored by NADPH for stimulated microglia but not stimulated astrocytes. The potential for stimulated microglia to generate oxygen free radicals may have implications in several degenerative neurological diseases where activated microglia are found in association with the lesions.

Animals↗