Bioquímica da esquistossomose mansônica: envolvimento dos siderossomos nos processos inflamatórios hepáticos

Rodrigues, Luiz Erlon Araújo; Galle, Pierre

doi:10.1590/S0037-86821990000200003

Resumos

Os processos inflamatórios que se desenvolvem durante as etapas avançadas da esquistossomose mansônica hepática foram relacionados, com o acúmulo de siderossomos, a capacidade dos íons ferrosos/férricos de desencadearem a formação de radicais livres e aperoxidação de lipídios membranáceos, assim como à diminuição da estabilidade das membranas dos diversos componentes do compartimento lisossômico hepático. Os lisossomos isolados de figados de camundongos infectados por 100 cercárias, com 80 e 100 dias de infecção, foram respectivamente, 2,5 e quase 4 vezes mais frágeis que os controles, isolados de figados de camundongos não infectados. A presença de siderossomos em grande quantidade foi demonstrada por espectrometria aos raios-X.

Esquistossomose mansônica; Metabolismo de ferro; Processo inflamatório; Superóxidos; Radicais livres

The inflammatory processes that develop during the advanced stages of hepatic Schistosomiasis mansoni have been related in this study to: (a) accumulation of siderosomes; (b) capacity of the ferrous/ferric ions to unleash the formation of free radicals; (c) peroxidation of membranaceous lipids and; (d) reduction of stability of the membranes of several components of the hepatic lysosomal compartment. The lysosomes isolated from the livers of infected mice by 100 cercariae, with 80 and 100 days of infection, were respectively 2.5 and almost 4 times weaker than the control ones isolated from livers of non-infected mice. The presence of a great quantity of siderosomes has been demonstrated by transmission electronic microscopy and X-ray spectrometry microanalysis.

Schistosomiasis mansoni; Iron metabolism; Inflammatory process; Superoxide; Free radicals

ARTIGOS

Bioquímica da esquistossomose mansônica: envolvimento dos siderossomos nos processos inflamatórios hepáticos

Luiz Erlon Araújo Rodrigues; Pierre Galle

^{Endereço para correspondência} Endereço para correspondência: Dr. Luiz Erlon Araújo Rodrigues. Departamento de Biofunção, Setor de Bioquímica/ICS/UFBA. Caixa Postal 4777 40140 Salvador, BA, Brasil.

RESUMO

Os processos inflamatórios que se desenvolvem durante as etapas avançadas da esquistossomose mansônica hepática foram relacionados, com o acúmulo de siderossomos, a capacidade dos íons ferrosos/férricos de desencadearem a formação de radicais livres e aperoxidação de lipídios membranáceos, assim como à diminuição da estabilidade das membranas dos diversos componentes do compartimento lisossômico hepático. Os lisossomos isolados de figados de camundongos infectados por 100 cercárias, com 80 e 100 dias de infecção, foram respectivamente, 2,5 e quase 4 vezes mais frágeis que os controles, isolados de figados de camundongos não infectados. A presença de siderossomos em grande quantidade foi demonstrada por espectrometria aos raios-X.

Palavras-chave: Esquistossomose mansônica. Metabolismo de ferro. Processo inflamatório. Superóxidos. Radicais livres.

ABSTRACT

The inflammatory processes that develop during the advanced stages of hepatic Schistosomiasis mansoni have been related in this study to: (a) accumulation of siderosomes; (b) capacity of the ferrous/ferric ions to unleash the formation of free radicals; (c) peroxidation of membranaceous lipids and; (d) reduction of stability of the membranes of several components of the hepatic lysosomal compartment. The lysosomes isolated from the livers of infected mice by 100 cercariae, with 80 and 100 days of infection, were respectively 2.5 and almost 4 times weaker than the control ones isolated from livers of non-infected mice. The presence of a great quantity of siderosomes has been demonstrated by transmission electronic microscopy and X-ray spectrometry microanalysis.

Keywords:Schistosomiasis mansoni. Iron metabolism. Inflammatory process. Superoxide. Free radicals.

Texto completo disponível apenas em PDF.

Full text available only in PDF format.

Recebido para publicação em 03/04/90.

Departamento de Biofunção, Setor de Bioquímica do Instituto de Ciências da Saúde da Universidade Federal da Bahia, Salvador, BA, Brasil.

Laboratoire de Biophysique, Facuité de Médecine, Université de Paris, Val de Marne, Créteil, France.

1. Anderson WR, Rao KV. Hepatic iron overload in renal transplant recipients: Ultrastructural observations. Ultrastructural Pathology 10:227-234, 1986.
2. Andrade ZA, Bina JC. A patologia da forma hepato-esplênica da esquistossomose mansônica em sua forma avançada(Estudo de 232 necrópsias completas). Memórias do Instituto Oswaldo Cruz 78:285-305, 1983.
3. Biemond P, Swaak AJG, Van Eijk HG, Koster JF. Superoxide dependent iron release from ferritin in inflammatory diseases. Free Radical Biology and Medicine 4:185-198, 1988.
4. Braughler JM, Duncan LA, Chase RL. The involvement of iron in lipid peroxidation. Importance of ferric to ferrous ratios in initiation. The Journal of Biological Chemistry 261:10282-10289, 1986.
5. Brunk U, Cadenas E. The potential intermediate role of lysosomes in oxygen free radical pathology. Review Article. APMIS 96:3-13, 1988.
6. Buttner H, Hanset E, Stamm D. Statistical analysis control and assessment of experimental results. In: Bergmeyer HU (ed) Methods of enzymatic analysis. 2nd edition, Verlag Chemie, New York, p. 318-393, 1974.
7. Caufield JP, Cianci CML. Human erythrocytes adhering to Schistosomula of Schistosoma mansoni lyse and fail to transfer membranes components to the parasite. The Journal of Cell Biology 101:158-166, 1985.
8. Caulfield JP, Korman G, Butterworth AE, Hogan M, David JR. The adherence of human neutrophils and eosinophils to schistosomula: evidence for membrane fusion between cells and parasites. The Journal of Cell Biology 86:46-63, 1980.
9. Cleton MI, de Bruijin WC, Van Blokland WTM, Marx JJM, Roelofs JM, Rademakers LHPM. Iron content and acid phosphatase activity in hepatic parenchymal lysosomes of patients with hemochromatosis before and after phlebotomy treatment Ultrastructural Pathology 12:161-174, 1988.
10. De Duve C, Pressman BC, Gianetto R, Wattiaux R, Appelmans F. Intracellular distribution on patterns of enzymes in rat-liver tissue. Biochemical Journal 60:604- 617, 1980.
11. Decker RS, Poole AR, Crie JS, Dingle JT, Wildenthal K. Lysosomal alterations in hypoxic and reoxygenated hearts. II Immunohistochemical and biochemical changes in cathepsin D. American Journal of Pathology 98:445-456, 1980.
12. Dickens BF, Mak IT, Weglicki WB. Lysosomal lipolytic enzymes lipid peroxidation and injury. Molecular and Cellular Biochemistry 82:119-123, 1988.
13. Galle P. The role of lysosomes in the renal concentration of mineral elements. Advances in Nephrology from the Necker Hospital 12:85-99, 1983.
14. Golan DE, Brown CS, Cianci CML, Furlong ST, Caulfield JP. Schistosomula of Schistosoma mansoni use lysophosphatidylcholine to lyse adherent human red blood cells and immobilise red cell membrane components. The Journal of Cell Biology 103:819-828, 1986.
15. Halliwell B, Gutteridge JMC. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochemical Journal 219:1-14, 1984.
16. Jamieson D. Oxygen toxicity and reactive oxygen metabolites in mammals. Free Radical Biology and Medicine 7:87-108, 1989.
17. Junqueira LC, Carneiro J, Contopoulos AN. Blood cells. In: Basic Histology 2nd edition. Lange Medical Publications, Los Altos CA p. 1-16, 1977.
18. Kalra J, Lautner D, Massey KL, Prasad K. Oxygen free radicals induced release of lysosomal enzymes in vitro Molecular and CellularBiochemistry 84:233-238,1988.
19. Monteiro HP, Winterboum CC. The superoxide dependent transfer of iron from ferritin to transferrin and lactoferrin. Biochemical Journal 256:923-928, 1988.
20. Olsson GM, Svensson I, Zdolsek JM, Brunk UT. Lysosomal enzyme leakage during the hypoxanthine/ xanthine oxidase reaction. Virchows Archiv B Cell Pathology, Including Molecular Pathology 56:385-391, 1989.
21. Richter GW. Studies of iron overload. Lysosomal proteolysis of rat liver ferritin. Pathology Research and Practice 181:159-167, 1986.
22. Rocha H. Glomerulopatia da esquistossomose mansônica. In: Azevedo ES, Reboufas G, Rocha H, Lyra LGC, Teixeira RS, Andrade SG, Andrade ZA (eds) Aspectos peculiares da infecção por Schistosoma mansoni Centro Editorial da Universidade Federal da Bahia p. 133- 160, 1984.
23. Rodrigues LEA. Alterações bioquímicas lisossômicas na esquistossomose mansônica hepática experimental. Tese para Professor Titular, Universidade Federal da Bahia, Salvador, 1984.
24. Rodrigues LEA, Costa MFD. Bioquímica da esquistossomose mansônica VI - Alterações do compartimento lisossômico hepático relacionadas ao tempo de infecção. Revista "da Sociedade Brasileira de Medicina Tropical 20:169-174, 1987.
25. Rodrigues LEA, Costa MFD, Batista P. Biochemistry of Schistosomiasis mansoni IV. Effects of oxamniquine on the hepatic lysosomal activity. Revista do Instituto de Medicina Tropical de São Paulo 25:223-228, 1983.
26. Rodrigues LEA, Mathias CMC, Amorim MSP. Modificação do método de Lowry para a quantificação de proteínas. Revista Brasileira de Patologia Clínica 25:35, 1989.
27. Roy AV, Brower ME, Flayden JE. Determination of acid phosphatase using thymolphatalein monophosphate. In: Tietz N (ed) Fundamentals of Clinical Chemistry, 2nd edition, WB Saunders Company Philadelphia, p. 617- 618, 1971.
28. Sorokim LM, Morgan EH, Yeoh GCT. Transferrin endocytosis and iron uptake in developing myogenic cell in culture: Effects of microtubular and metabolic inhibitors, sulphydryl reagents and lysosomotrophic agents. Journal of Cellular Physiology 137:483-489, 1988.
29. Standen OD. The penetration of cercarie of Schistosoma mansoni into the skin and lymphatics of mouse. Transactions of the Royal Society of Tropical Medicine and Hygiene 42:292-298, 1953.
30. Topham R, Goger M, Pearce K, Schultz P. The mobilization of ferritin iron by liver cytosol. A comparison of xanthine and NADH as reducing substrates. Biochemical Journal 261:137-143, 1989.
31. Weir MF, Gibson JF, Peters TJ. Haemosiderin and tissue damage. Cell biochemistry and Function 2:186- 194, 1984.

Endereço para correspondência:

Dr. Luiz Erlon Araújo Rodrigues.

Departamento de Biofunção, Setor de Bioquímica/ICS/UFBA.

Caixa Postal 4777

40140

Salvador, BA, Brasil.

Datas de Publicação

Publicação nesta coleção
24 Maio 2013
Data do Fascículo
Jun 1990

Histórico

Recebido
03 Abr 1990
Aceito
03 Abr 1990

This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.

[1] 1. Anderson WR, Rao KV. Hepatic iron overload in renal transplant recipients: Ultrastructural observations. Ultrastructural Pathology 10:227-234, 1986.

[2] 2. Andrade ZA, Bina JC. A patologia da forma hepato-esplênica da esquistossomose mansônica em sua forma avançada(Estudo de 232 necrópsias completas). Memórias do Instituto Oswaldo Cruz 78:285-305, 1983.

[3] 3. Biemond P, Swaak AJG, Van Eijk HG, Koster JF. Superoxide dependent iron release from ferritin in inflammatory diseases. Free Radical Biology and Medicine 4:185-198, 1988.

[4] 4. Braughler JM, Duncan LA, Chase RL. The involvement of iron in lipid peroxidation. Importance of ferric to ferrous ratios in initiation. The Journal of Biological Chemistry 261:10282-10289, 1986.

[5] 5. Brunk U, Cadenas E. The potential intermediate role of lysosomes in oxygen free radical pathology. Review Article. APMIS 96:3-13, 1988.

[6] 6. Buttner H, Hanset E, Stamm D. Statistical analysis control and assessment of experimental results. In: Bergmeyer HU (ed) Methods of enzymatic analysis. 2nd edition, Verlag Chemie, New York, p. 318-393, 1974.

[7] 7. Caufield JP, Cianci CML. Human erythrocytes adhering to Schistosomula of Schistosoma mansoni lyse and fail to transfer membranes components to the parasite. The Journal of Cell Biology 101:158-166, 1985.

[8] 8. Caulfield JP, Korman G, Butterworth AE, Hogan M, David JR. The adherence of human neutrophils and eosinophils to schistosomula: evidence for membrane fusion between cells and parasites. The Journal of Cell Biology 86:46-63, 1980.

[9] 9. Cleton MI, de Bruijin WC, Van Blokland WTM, Marx JJM, Roelofs JM, Rademakers LHPM. Iron content and acid phosphatase activity in hepatic parenchymal lysosomes of patients with hemochromatosis before and after phlebotomy treatment Ultrastructural Pathology 12:161-174, 1988.

[10] 10. De Duve C, Pressman BC, Gianetto R, Wattiaux R, Appelmans F. Intracellular distribution on patterns of enzymes in rat-liver tissue. Biochemical Journal 60:604- 617, 1980.

[11] 11. Decker RS, Poole AR, Crie JS, Dingle JT, Wildenthal K. Lysosomal alterations in hypoxic and reoxygenated hearts. II Immunohistochemical and biochemical changes in cathepsin D. American Journal of Pathology 98:445-456, 1980.

[12] 12. Dickens BF, Mak IT, Weglicki WB. Lysosomal lipolytic enzymes lipid peroxidation and injury. Molecular and Cellular Biochemistry 82:119-123, 1988.

[13] 13. Galle P. The role of lysosomes in the renal concentration of mineral elements. Advances in Nephrology from the Necker Hospital 12:85-99, 1983.

[14] 14. Golan DE, Brown CS, Cianci CML, Furlong ST, Caulfield JP. Schistosomula of Schistosoma mansoni use lysophosphatidylcholine to lyse adherent human red blood cells and immobilise red cell membrane components. The Journal of Cell Biology 103:819-828, 1986.

[15] 15. Halliwell B, Gutteridge JMC. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochemical Journal 219:1-14, 1984.

[16] 16. Jamieson D. Oxygen toxicity and reactive oxygen metabolites in mammals. Free Radical Biology and Medicine 7:87-108, 1989.

[17] 17. Junqueira LC, Carneiro J, Contopoulos AN. Blood cells. In: Basic Histology 2nd edition. Lange Medical Publications, Los Altos CA p. 1-16, 1977.

[18] 18. Kalra J, Lautner D, Massey KL, Prasad K. Oxygen free radicals induced release of lysosomal enzymes in vitro Molecular and CellularBiochemistry 84:233-238,1988.

[19] 19. Monteiro HP, Winterboum CC. The superoxide dependent transfer of iron from ferritin to transferrin and lactoferrin. Biochemical Journal 256:923-928, 1988.

[20] 20. Olsson GM, Svensson I, Zdolsek JM, Brunk UT. Lysosomal enzyme leakage during the hypoxanthine/ xanthine oxidase reaction. Virchows Archiv B Cell Pathology, Including Molecular Pathology 56:385-391, 1989.

[21] 21. Richter GW. Studies of iron overload. Lysosomal proteolysis of rat liver ferritin. Pathology Research and Practice 181:159-167, 1986.

[22] 22. Rocha H. Glomerulopatia da esquistossomose mansônica. In: Azevedo ES, Reboufas G, Rocha H, Lyra LGC, Teixeira RS, Andrade SG, Andrade ZA (eds) Aspectos peculiares da infecção por Schistosoma mansoni Centro Editorial da Universidade Federal da Bahia p. 133- 160, 1984.

[23] 23. Rodrigues LEA. Alterações bioquímicas lisossômicas na esquistossomose mansônica hepática experimental. Tese para Professor Titular, Universidade Federal da Bahia, Salvador, 1984.

[24] 24. Rodrigues LEA, Costa MFD. Bioquímica da esquistossomose mansônica VI - Alterações do compartimento lisossômico hepático relacionadas ao tempo de infecção. Revista "da Sociedade Brasileira de Medicina Tropical 20:169-174, 1987.

[25] 25. Rodrigues LEA, Costa MFD, Batista P. Biochemistry of Schistosomiasis mansoni IV. Effects of oxamniquine on the hepatic lysosomal activity. Revista do Instituto de Medicina Tropical de São Paulo 25:223-228, 1983.

[26] 26. Rodrigues LEA, Mathias CMC, Amorim MSP. Modificação do método de Lowry para a quantificação de proteínas. Revista Brasileira de Patologia Clínica 25:35, 1989.

[27] 27. Roy AV, Brower ME, Flayden JE. Determination of acid phosphatase using thymolphatalein monophosphate. In: Tietz N (ed) Fundamentals of Clinical Chemistry, 2nd edition, WB Saunders Company Philadelphia, p. 617- 618, 1971.

[28] 28. Sorokim LM, Morgan EH, Yeoh GCT. Transferrin endocytosis and iron uptake in developing myogenic cell in culture: Effects of microtubular and metabolic inhibitors, sulphydryl reagents and lysosomotrophic agents. Journal of Cellular Physiology 137:483-489, 1988.

[29] 29. Standen OD. The penetration of cercarie of Schistosoma mansoni into the skin and lymphatics of mouse. Transactions of the Royal Society of Tropical Medicine and Hygiene 42:292-298, 1953.

[30] 30. Topham R, Goger M, Pearce K, Schultz P. The mobilization of ferritin iron by liver cytosol. A comparison of xanthine and NADH as reducing substrates. Biochemical Journal 261:137-143, 1989.

[31] 31. Weir MF, Gibson JF, Peters TJ. Haemosiderin and tissue damage. Cell biochemistry and Function 2:186- 194, 1984.