Modulation by α-2 Macroglobulin of Human Lymphocyte Proliferation in Response to Mitogens and Antigen

Goutner, A; Simmler, Marie‐Christine; Tapon, J; Rosenfeld, C.

doi:10.1111/j.1432-0436.1976.tb00910.x

Cited by 26 publications

(5 citation statements)

References 9 publications

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“…However, the purified CbM in free form had no effect on the mitogen response of lymphocytes. This does not total ly agree with the observations of others [10][11][12][13]. One pos sible explanation may be that the concentration of (X 2M used in this experiment was not high but nearer to the physiological range for humans.…”

Section: Discussioncontrasting

confidence: 50%

Study on Proteinase-lnhibiting Capacity of Plasma α<sub>2</sub>-Macroglobulin in Idiopathic Nephrotic Syndrome

Asami

Nishihara

Tomisawa

et al. 1996

Nephron

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We studied the relationship between plasma α₂-macroglobulin (α₂M) and depressed cell-mediated immunity in idiopathic nephrotic syndrome (INS). Plasma α₂M concentrations (μmol/l) were increased during relapses of INS; however, the proteinase inhibitory activity, measured using bacterial thermo-lysin, was significantly decreased when calculated per 1 mol of α₂M, implying a reduced proteinase-inhibiting capacity of α₂M. The decreased proteinase-inhibiting capacity of α₂M was associated with the inhibitory activity of plasma on normal lymphocyte blastogenesis. Purified α₂M, when complexed with chymotrypsin, intensively inhibited normal lymphocyte blastogenesis induced by concanavalin A, as compared with the free form of α₂M. From these results it is suggested that, although the amount of α₂M protein has increased in the plasma of INS patients during relapse, its binding capacity to proteinases has relatively decreased. The results of this study may provide speculation for both the well-known high plasma α₂M concentrations and the immunodepres-sion, both of which have been observed in INS patients in the past few decades.

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Section: Discussioncontrasting

confidence: 50%

Study on Proteinase-lnhibiting Capacity of Plasma α<sub>2</sub>-Macroglobulin in Idiopathic Nephrotic Syndrome

Asami

Nishihara

Tomisawa

et al. 1996

Nephron

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“…unspecific toxic effect is unlikely: viability of the cells was similar in all cultures; some complexes active in the PPD-induced stimulation did not influence the effect of the insoluble anti-CD3. The suppressive effect of a2M on the mitogen or PPD-induced lymphocyte proliferation has already been observed by Goutner et al [7] who did not, however, test a2M-PC. Hubbard et al [8] observed a similar effect on the mixed lymphocyte reaction.…”

Section: Discussionmentioning

confidence: 62%

Immunomodulation by α₂‐macroglobulin and α₂‐macroglobulin‐proteinase complexes: the effect on the human T lymphocyte response

Heumann

Vischer

1988

Eur J Immunol

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Alpha 2-macroglobulin (alpha 2M), various alpha 2M-proteinase complexes and methylamine-treated alpha 2M were added to human lymphocyte cultures stimulated with the specific antigen purified protein derivative of tuberculin (PPD), pokeweed mitogen (PWM) and anti-CD3. alpha 2M-trypsin diminished all reactions in a dose-dependent way. In the PPD-induced stimulation of peripheral blood mononuclear cells, both change of configuration and remaining proteinase activity contributed to the suppressive activity. Separate exposure of adherent cells or the highly purified T lymphocytes to alpha 2M-trypsin complexes indicated that the effect was mediated through adherent cells. Addition of indomethacin did not modify the results. In the interleukin 2 (IL2)-dependent stimulation of purified T lymphocytes by anti-CD3 the effect of alpha 2M-proteinase complexes was probably due to the digestion of IL 2 through remaining proteinase activity. As alpha 2M-proteinase complexes are formed at sites of inflammation, the multiple immunomodulatory effects of alpha 2M-proteinase complexes might contribute to the dysregulation of the immune system in inflammatory diseases.

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“…The inhibitors shown to have this ability are Trasylol (Thomson et al, 1978), soya-bean trypsin inhibitor (Moreau et al, 1975) and a2-macroglobulin (Goutner et al, 1976). At concentrations of tick inhibitor as high or higher than those used for these proteins, the tick protein had no effect on lymphocyte stimulation.…”

Section: Discussionmentioning

confidence: 99%

On the biological role of a proteolytic-enzyme inhibitor from the ectoparasitic tick Boophilus microplus

Willadsen¹,

Riding²

1980

Biochemical Journal

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The tick Boophilus microplus contains a protein that inhibits a range of proteolytic enzymes. Variations in the concentration of this protein throughout the life cycle were followed by measuring simultaneously the inhibition of trypsin and chymotrypsin and reaction with an antiserum to the purified inhibitor. The protein is present in large amounts in eggs and in unfed larvae, but its concentration falls very rapidly after the start of the parasitic stage of the life cycle. This, together with previous evidence, suggests that the inhibitor is important both in eggs and in the initial establishment of the parasite on its host. The activity of the protein towards several enzymes has been measured as an indication of its possible function. Bovine trypsin, chymotrypsin and plasmin and pig pancreatic kallikrein are all inhibited. The protein also affects the blood-coagulation system at several points, since it prolongs both activated-partial-thromboplastin time and prothrombin time. It. inhibits the complement-dependent lysis of erythrocytes, but is without significant effect on mitogen-induced lymphocyte stimulation. Thus the inhibitor could have several effects on the host that would be beneficial to the parasite.

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Modulation by α-2 Macroglobulin of Human Lymphocyte Proliferation in Response to Mitogens and Antigen

Cited by 26 publications

References 9 publications

Study on Proteinase-lnhibiting Capacity of Plasma α<sub>2</sub>-Macroglobulin in Idiopathic Nephrotic Syndrome

Study on Proteinase-lnhibiting Capacity of Plasma α<sub>2</sub>-Macroglobulin in Idiopathic Nephrotic Syndrome

Immunomodulation by α₂‐macroglobulin and α₂‐macroglobulin‐proteinase complexes: the effect on the human T lymphocyte response

On the biological role of a proteolytic-enzyme inhibitor from the ectoparasitic tick Boophilus microplus

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Modulation by α-2 Macroglobulin of Human Lymphocyte Proliferation in Response to Mitogens and Antigen

Cited by 26 publications

References 9 publications

Study on Proteinase-lnhibiting Capacity of Plasma α<sub>2</sub>-Macroglobulin in Idiopathic Nephrotic Syndrome

Study on Proteinase-lnhibiting Capacity of Plasma α<sub>2</sub>-Macroglobulin in Idiopathic Nephrotic Syndrome

Immunomodulation by α2‐macroglobulin and α2‐macroglobulin‐proteinase complexes: the effect on the human T lymphocyte response

On the biological role of a proteolytic-enzyme inhibitor from the ectoparasitic tick Boophilus microplus

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Immunomodulation by α₂‐macroglobulin and α₂‐macroglobulin‐proteinase complexes: the effect on the human T lymphocyte response