Proteolytic enzymes in ordinary, hyperacute, monocytic and passive transfer forms of experimental allergic encephalomyelitis
- PMID: 843913
- DOI: 10.1016/0006-8993(77)90649-7
Proteolytic enzymes in ordinary, hyperacute, monocytic and passive transfer forms of experimental allergic encephalomyelitis
Abstract
The changed patterns of proteolytic activity in brain and spinal cord of Lewis rats were examined in 4 different morphological variants of EAE: ordinary induced by the standard emulsion, hyperacute induced by an emulsion plus pertussis vaccine, passive induced by donor EAE cells, and monocytic induced by treatment of passive EAE with the immunosupressive drug tilorone. The following enzymatic changes were found: firstly, in ordinary EAE there was a 2--3.5-fold increase in cathepsins A and C (E.C. 3.4.14.1) in spinal cord one day following the appearance of paralysis with a smaller change in hindbrain, and none in the forebrain regions. With recovery from paralysis, levels of cathepsin A remained high in upper cord, and cathepsin C levels fell to about half. In contrast, increase in cathepsin D(E.C. 3.4.23.5) was smaller and occurred only 4--5 days after paralysis with the largest change in spinal cord areas and with only a small decrease on recovery from paralysis. Secondly, in hyperacute EAE, the increase in all cases was smaller with the largest change in cathepsin A level in upper spinal cord. In passive EAE, the most significant increase occurred only in the lower spinal cord for cathepsins A and C, and fourthly, in monocytic EAE induced by tilorone, there was an exceptionally large, 3-fold increase in cathepsin C in lower cord as compared to a 1.5-2 fold increase for other cathepsins. No major differences were observed on comparison of antigens from different sources (guinea pig and bovin spinal cord myelin peptide). An attempt is made to relate enzymatic changes to the morphological features of each variant with special reference to the nature of the infiltrating cells.
Similar articles
-
Proteolytic activity in brain and spinal cord in sensitive and resistant strains of rat and mouse subjected to experimental allergic encephalomyelitis.Brain Res. 1974 Jul 19;75(1):153-62. doi: 10.1016/0006-8993(74)90777-x. Brain Res. 1974. PMID: 4546325 No abstract available.
-
Proteolytic enzymes and experimental demyelination in the rat and monkey.J Neurochem. 1974 Nov;23(5):965-71. doi: 10.1111/j.1471-4159.1974.tb10748.x. J Neurochem. 1974. PMID: 4140219 No abstract available.
-
Mitigation of experimental allergic encephalomyelitis by cathepsin D inhibition.Adv Exp Med Biol. 1979;121B:317-23. doi: 10.1007/978-1-4684-8914-9_30. Adv Exp Med Biol. 1979. PMID: 317560
-
Experimental allergic encephalomyelitis supernatant transfer activity (EAE-STA) in Lewis rats:immunobiologic and initial biochemical properties.J Immunol. 1980 Apr;124(4):1784-8. J Immunol. 1980. PMID: 6965962
-
Hyperacute, neutrophilic, and localized forms of experimental allergic encephalomyelitis: a review.Acta Neuropathol. 1974;28(3):179-89. doi: 10.1007/BF00719023. Acta Neuropathol. 1974. PMID: 4139872 Review. No abstract available.
Cited by
-
Suppression of experimental allergic encephalomyelitis in Lewis rats after elimination of macrophages.J Exp Med. 1990 Oct 1;172(4):1025-33. doi: 10.1084/jem.172.4.1025. J Exp Med. 1990. PMID: 2145387 Free PMC article.
-
Treatment of experimental allergic encephalomyelitis with an inhibitor of cathepsin D (pepstatin).Neurochem Res. 1978 Apr;3(2):185-94. doi: 10.1007/BF00964059. Neurochem Res. 1978. PMID: 307703
-
Degradation of basic protein in myelin by neutral proteases secreted by stimulated macrophages: a possible mechanism of inflammatory demyelination.Proc Natl Acad Sci U S A. 1978 Mar;75(3):1554-8. doi: 10.1073/pnas.75.3.1554. Proc Natl Acad Sci U S A. 1978. PMID: 148651 Free PMC article.
-
Lysosomal enzymes in experimental allergic encephalomyelitis: time course and evidence of the source.Neurochem Res. 1988 Feb;13(2):165-9. doi: 10.1007/BF00973329. Neurochem Res. 1988. PMID: 3283588
MeSH terms
Substances
LinkOut - more resources
Full Text Sources