Summary
Human tissues are known to contain two low molecular weight (MW about 12,000) cysteine proteinase inhibitors, i.e. an acid inhibitor (ACPI) with pI 4.7–5.0 and a neutral inhibitor (NCPI) with pI 6.0–6.5. ACPI is abundant in cornifying epithelial tissues and in the dendritic reticulum cells of germinal centres of the lymph nodes. NCPI is abundant in lymphatic tissue and is known to be synthesized and released by mononuclear phagocytes. In this report NCPI was localized immunohistochemically in the epitheloid cells of most sarcoidotic lymph nodes, in lymph node macrophages after lymphangiography and in alveolar macrophages, while no ACPI could be demonstrated in the same cells by similar methods. These inhibitors were not demonstrable in lymph node sinus histiocytosis. Peripheral blood monocytes did not exhibit any NCPI immunoreactivity. In occasional blood monocytes anti-ACPI serum gave a weak reaction, the specificity of which is questionable. These data suggest that studies on cysteine proteinase inhibitors reveal basic differences in the various histiomonocytic cells and possibly differences in their functional stages.
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References
Bøyum A (1968) Isolation of mononuclear cells and granulocytes from human blood. Scand J Clin Lab Invest 97:Suppl 21 77–89
Davies ME, Barrett AJ (1984) Immunolocalization of human cystatins in neutrophils and lymphocytes. Histochemistry 80: 373–377
Green GDJ, Kembhavi AA, Davies ME, Barrett AJ (1984) Cystatin-like cysteine proteinase inhibitors from human liver. Biochem J 218: 142–147
Hopsu-Havu VK, Joronen I, Järvinen M, Rinne A (1982) A new cysteine proteinase inhibitor in human serum. Eur Rev Med Pharmacol Sci IV: 389–394
Hopsu-Havu VK, Joronen I, Järvinen M, Rinne A (1983) Detection of acid cysteine proteinase inhibitor in human tissues and serum with RIA. Eur Rev Med Pharmacol Sci V: 1–4
Hopsu-Havu VK, Joronen I, Järvinen M, Rinne A, Aalto M (1984) Cysteine proteinase inhibitors of mononuclear phagocytes. Cell Tissue Res 236: 161–164
Hopsu-Havu VK, Joronen I, Rinne A, Järvinen M (1985) Natural cysteine proteinase inhibitors reduce lectin induced lymphocyte stimulation. Acta Histochem [in press]
Järvinen M (1978) Purification and some characteristics of the human epidermal SH-protease inhibitor. J Invest Dermatol 71: 114–118
Järvinen M, Pernu H, Rinne A, Hopsu-Havu VK, Altonen M (1983) Localization of three inhibitors of cysteine proteinases in the human oral mucosa. Acta Histochem 73: 279–282
Järvinen M, Rinne A (1982) Human spleen cysteine proteinase inhibitor. Purification, fractionation into isoelectric variants and some properties of the variants. Biochim Biophys Acta 708: 210–217
Järvinen M, Rinne A (1982) The use of polyvinyl acetate glue to prevent detachment of tissue sections in immunohistochemistry. Acta Histochem 72: 251–252
Nossal GJV, Abbot A, Mitchell J, Lummus Z (1968) Antigens in immunity. XV. Ultrastructural features of antigen capture in primary and secondary lymphoid follicles. J Exp Med 127: 277–290
Rinne A, Alavaikko M, Järvinen M, Martikainen J, Karttunen T, Hopsu-Havu VK (1983) Demonstration of immunoreactive cysteine proteinase inhibitor in reticulum cells of lymph node germinal centres. Virchows Arch [Cell Pathol] 43: 121–126
Rinne A, Järvinen M, Räsänen O (1978) A protein reminiscent of the epidermal SH-protease inhibitor occurs in squamous epithelia of man and rat. Acta Histochem 63: 183–192
Rinne A, Räsänen O, Järvinen M, Dammert K, Kallioinen M, Hopsu-Havu VK (1984) Occurrence of acid and neutral cysteine proteinase inhibitors in epidermal malignancies: Immunohistochemical study. Acta Histochem 74: 75–79
Sternberger LA, Hardy PH Jr, Cuculis JJ, Meyer HC (1970) The unlabelled antibody enzyme method in immunohistochemistry. Preparation and properties of soluble antigen-antibody complex (horseradish peroxidase-antihorseradish peroxidase) and its use in the identification of spirochetes. J Histochem Cytochem 18: 315–333
Tokuda A, Hayashi H, Matsuba K (1960) Biochemical study of cellular antigen-antibody reaction on tissue culture. II. Release of a protease inhibitor. J Exp Med 112: 249–255
Udaka K, Hayashi H (1965) Further purification of a protease inhibitor from rabbit skin with healing inflammation. Biochim Biophys Acta 97: 251–261
Unkeless J, Gordon S, Reich E (1974) Secretion of plasminogen activator by stimulated macrophages. J Exp Med 139: 83450
Werb Z (1981) Characterization and classification of macrophage proteinases and proteinase inhibitors. In: Adams DO, Edelson PJ, Koren H (eds) Methods for studying mononuclear phagocytes. Academic Press, New York, pp 561–575
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The investigation was done with the support of the Sigrid Juselius Foundation and Emil Aaltonen Foundation
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Rinne, A., Järvinen, M., Alavaikko, M. et al. Occurrence of cysteine proteinase inhibitors in cells of the monocytic-histiocytic system. Virchows Archiv B Cell Pathol 49, 153–159 (1985). https://doi.org/10.1007/BF02912093
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DOI: https://doi.org/10.1007/BF02912093