Incorporation of the APR Sialoglycoproteins in ranulomatous Tissues

Jayle, M F; Janiaud, P; Engler, R; Degrelle, H; Marcais, J

doi:10.1016/b978-0-08-016622-3.50029-3

Cited by 4 publications

(2 citation statements)

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“…Haptoglobin is a representative of acute phase reactive proteins and plasma haptoglobin levels increase as a result of increased hepatic synthesis in a variety of diverse pathologic states, such as infection, experimentally induced inflammatory states, traumas and neoplasmas, characterized by breakdown, repair or proliferation of tissues with or without hemolysis. Whether the hemoglobin-binding is the sole function has not been established, but there are suggestions of some functions in the extravascular compartments concerning with these pathological states ~ (Snellman and Sylv6n, 1967;Moretti and Jayle, 1965;Jayle et al, 1970).…”

Section: Discussionmentioning

confidence: 99%

“…Haptoglobin has a specific capacity to bind hemoglobin and has recently been noted as a representative of acute phase reactive proteins (Snellman and Sylv6n, 1967;Jayle et al, 1970;Sutton, 1970). The authors (Ogawa and Kawamura, 1966;Kawamura et al, 1973) and Fiiller et al (1973) have reported the molecular structure of haptoglobins of three types.…”

Section: Introductionmentioning

confidence: 99%

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Type-dependent difference in the metabolism of human haptoglobins

et al. 1979

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Metabolic properties of haptoglobin 1-1 and 2-2 proteins were investigated by performing turnover studies in normal rabbits in a steady state concerning haptoglobin metabolism. Studies in six rabbits showed that the average plasma half-lives of iodinated haptoglobin 1-1 and 2-2 were similar with values of 2.3 and 2.4 days, respectively. The distribution in the body compartments, however, was significantly different at the equilibrium time and was such that the extravascular compartments contained 57.0~ of the total body pool of haptoglobin 1-1, compared only 36.9~ in the case of haptoglobin 2-2. These findings suggest that the former protein is higher than the latter in capillary permeability.These phenomena may be attributable to the difference in the molecular size and/or polymeric structure rather than that in the primary structure between two haptoglobins. The present results would reflex the survival of human haptoglobins in normal man, although the results were obtained by tracing human haptoglobins injected in rabbits. Finally, the biological significance of the type-dependent metabolism of haptoglobins was discussed.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Type-dependent difference in the metabolism of human haptoglobins

et al. 1979

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Acute‐Phase Proteins in Wound Healing

1973

Novartis Foundation Symposia

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Alpha‐globulins suppress human leukocyte tumor necrosis factor secretion

et al. 1989

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The secretion of tumor necrosis factor (TNF) by human peripheral blood mononuclear cells was suppressed by either whole human plasma alpha-globulins or purified alpha 1-acid-glycoprotein, alpha 1-antitrypsin and alpha 2-macroglobulin in a concentration-dependent manner. alpha 1-Antitrypsin was found to be the most suppressive of the purified proteins tested and completely blocked TNF release at concentrations above 1.25 mg/ml. Both alpha 1-acid glycoprotein and alpha 1-antitrypsin blocked TNF secretion by leukocytes which were simultaneously stimulated with either recombinant human interferon-gamma (IFN-gamma) or lipopolysaccharide (LPS). IFN-gamma- and LPS-activated cells were also susceptible to suppression mediated by these two alpha-globulins and the inhibition produced by 5 mg/ml alpha 1-antitrypsin was greater than that caused by either 1 microM prostaglandin E2 or 10 ng/ml transforming growth factor-beta 1. The level of TNF mRNA in TNF-secreting and alpha-globulin-suppressed cells was examined and found to be equal in both groups. The suppressive effect of whole alpha-globulins was confined to the inhibition of TNF secretion and these plasma proteins had no effect on the cytolytic activity of the recombinant cytokine as measured on murine L-929 target cells. Thus the alpha-globulins, which are a major fraction of the circulating plasma proteins, may function in TNF homeostasis by controlling TNF secretion without inhibiting the biological activity of the released cytokine.

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Incorporation of the APR Sialoglycoproteins in ranulomatous Tissues

Cited by 4 publications

References 2 publications

Type-dependent difference in the metabolism of human haptoglobins

Type-dependent difference in the metabolism of human haptoglobins

Acute‐Phase Proteins in Wound Healing

Alpha‐globulins suppress human leukocyte tumor necrosis factor secretion

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