Identification of T-kinin-leu(T-kinin-containing peptide) released from T-kininogen by cathepsin D of granulomatous tissues in rats

Sakamoto, Wataru; Satoh, Fumihiko; Nagasawa, S; Handa, Hiroshi

doi:10.1016/0006-291x(88)90756-5

Cited by 10 publications

(1 citation statement)

References 13 publications

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“…T-Kininogen is present only in rat plasma and is induced by inflammatory response (3-5, [8][9][10][11]. The function of T-kininogen as a precursor of T-kinin remains to be established since the in vivo significance of T-kinin releasing enzymes is not fully understood (18)(19)(20)(21). The function of T-kininogen as a cysteine protease inhibitor may be significant in inflammation since its plasma concentration increases after the injection of lipopolysaccharide or turpentine (3)(4)(5).…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of Two Isoforms of T-Kininogens from Rat Liver Microsomes1

Enjyoji

Kato

1992

The Journal of Biochemistry

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T-Kininogen is one of the acute phase proteins, and is a precursor of T-kinin and a cysteine protease inhibitor. Two homologous T-kininogens (TI- and TII-kininogens) were isolated from microsomal fraction of inflamed rat liver, by chromatographies on columns of DEAE-Sepharose CL-6B and DEAE-5PW and by affinity chromatography on a column of anti T-kininogen monoclonal antibody. The amino terminal amino acid sequences of the two microsomal pyridylethylated T-kininogens after pyroglutamyl aminopeptidase treatment were identical with those of TI- and TII-kininogens from inflamed rat plasma. Microsomal T-kininogens moved faster on SDS-PAGE after treatment with endoglycosidase H. The amounts of microsomal TI- and TII-kininogens in inflamed and non-inflamed rat liver were quantitated by immunoblotting of homogenates of liver microsomes using anti T-kininogen rabbit antiserum. The amounts of microsomal T-kininogens were increased in inflamed rat liver, but the ratio of the amounts of TI-kininogen to TII-kininogen was not different in the inflamed and non-inflamed rat liver. On the other hand, TII-kininogen was not significantly detected in non-inflamed rat plasma. These results indicate that the secretion of one of the T-kininogens, TII-kininogen, into plasma may be prevented by some unknown mechanism.

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Section: Discussionmentioning

confidence: 99%

Purification and Characterization of Two Isoforms of T-Kininogens from Rat Liver Microsomes1

Enjyoji

Kato

1992

The Journal of Biochemistry

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Effect of vitamin E on production of macrophage migration inhibitory factor (MIF) by macrophages

et al. 1999

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Macrophage migration inhibitory factor (MIF), a putative cytokine involved in inflammatory and immune responses, was identified in rat peritoneal macrophages by Western blot analysis and its secretion into culture medium by enzyme-linked immunosorbent assay. To clarify the possibility of vitamin E as an immune modulator, we investigated the effect of vitamin E on MIF production in macrophages in response to calcium ionophore A23187 and lipopolysaccharide (LPS). Intraperitoneal injections of vitamin E (5 mg per rat) for 6 successive days resulted in a significant increase of alpha-tocopherol content in peritoneal macrophages. Alpha-tocopherol content of macrophages in vitamin E-treated rats was 478.3 +/- 90.7 ng/10(6) cells, whereas in control rats it was 1.5 +/- 0.5 ng/10(6) cells. For the control macrophages, total MIF content of the medium (2.5 x 10(6) cells/18 ml) without stimulation was 40.7 +/- 3.6 ng after 14 h culture, whereas stimulation with calcium ionophore A23187 (400 nM) and LPS (5.0 microg/ml) induced the elevation of MIF content to 65.9 +/- 7.5 ng and 74.3 +/- 10.4 ng, respectively (p < 0.05, n = 3). On the other hand, vitamin E-enriched macrophages without stimulation showed less MIF content (14.0 +/- 4.2 ng) than the control (p < 0.05, n = 3). Similarly, the increase of MIF of vitamin E-treated macrophages was significantly suppressed after stimulation with calcium ionophore A23187 or LPS, compared with the control macrophages (p < 0.01, n = 3). From analysis of intracellular MIF content by Western blot, we found no alteration of intracellular MIF content of vitamin E-macrophages, in contrast to the decreased content of control stimulated-macrophages, showing that vitamin E suppressed MIF secretion into the culture medium. Taken together, these results indicate that vitamin E may contribute to the regulation of inflammatory and immune responses through regulation of MIF secretion, possibly by modulating macrophage-membrane architecture.

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Gene Expression of Proteases and Protease Inhibitors in the Human Ciliary Epithelium and ODM-2 Cells

Ortego

Escribano

Coca‐Prados

1997

Experimental Eye Research

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Identification of T-kinin-leu(T-kinin-containing peptide) released from T-kininogen by cathepsin D of granulomatous tissues in rats

Cited by 10 publications

References 13 publications

Purification and Characterization of Two Isoforms of T-Kininogens from Rat Liver Microsomes1

Purification and Characterization of Two Isoforms of T-Kininogens from Rat Liver Microsomes1

Effect of vitamin E on production of macrophage migration inhibitory factor (MIF) by macrophages

Gene Expression of Proteases and Protease Inhibitors in the Human Ciliary Epithelium and ODM-2 Cells

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