Literature DB >> 13211907

A study of the chemical nature of components of bovine white matter effective in producing allergic encephalomyelitis in the rabbit.

B H WAKSMAN, H PORTER, M D LEES, R D ADAMS, J FOLCH.   

Abstract

Fractions of bovine white matter, prepared by the methods of Folch and Lees, were studied for chemical composition and for their ability to produce experimental allergic encephalomyelitis in rabbits. Evaluation of the disease and of the lesions in animals injected with the more active fractions at several dose levels permitted comparison of the antigenic activity of these materials. When tissue was fractionated by the methods of Folch and Lees, antigenic activity was found in the chloroform-methanol extract but not in the denatured tissue residue. This activity was traced to proteolipides A and B and to the lower phase, more specifically the ether-soluble fraction of the lower phase. Proteolipide C was inactive. Correlation of the chemistry of fractions with their antigenic activity suggested two possibilities: (a) that there might be two antigens, one proteolipide and the other non-proteolipide; or (b) that a small specific proteolipide is responsible for all the observed activity. The high concentration of acetal phosphatide in the ether-soluble lower phase suggested that compounds of this type might be the hypothetical non-proteolipide antigen, but this hypothesis was disproved by analytic study of active and inactive materials. The possibility that proteolipide might account for all the antigenic activity was strongly supported by the experimental finding that total lipide and proteolipide progressively lost activity as proteolipide was degraded by adequate processing. The use of an entirely different method for preparing total lipides free of proteolipide (the colloidal iron technique) indicated that this loss of activity did not result from incidental removal of some non-proteolipide antigen. These tentative conclusions are in agreement with those of Tal and Olitsky and provide a satisfactory interpretation of the findings of Goldstein et al. The very fact, however, that the suggested proteolipide antigen would amount to no more than 1 per cent of the total chloroform-methanol extractives leaves open the possibility that some unrecognized trace substance may be the antigen. Skin tests with the various fractions indicated some cross-reactivity between proteolipides A and B and the ether-soluble lower phase fraction and a fair correlation of positive skin reactions with disease. This finding is compatible with the suggestion that the same antigen is present in both of these types of material. When the disease produced by whole tissue or fractions was evaluated by the use of the proportion of animals developing disease, the day of onset, and the severity of the histologic lesions, it was found that fractions produced milder disease of later onset than intact tissue at all dose levels. The disease-producing activity was not enhanced by increasing the dose; i.e., it appeared to reach an asymptotic maximum below that obtainable with whole fresh tissue. This finding suggests both a quantitative loss of activity and a qualitative change during the initial chloroform-methanol extraction, a procedure which denatures all proteins in the tissue residue. A comparable change appeared to occur in whole white matter stored at -15 degrees C. for 15 months and thawed and refrozen several times during this period. The later fractionation steps resulted in no apparent loss of antigenic activity. A scoring method employing the same type of data to estimate the actual relative antigen contents of different preparations is presented in the Appendix.

Entities:  

Keywords:  ANTIGENS AND ANTIBODIES; BRAIN; ENCEPHALOMYELITIS/experimental

Mesh:

Substances:

Year:  1954        PMID: 13211907      PMCID: PMC2136392          DOI: 10.1084/jem.100.5.451

Source DB:  PubMed          Journal:  J Exp Med        ISSN: 0022-1007            Impact factor:   14.307


  21 in total

1.  Relationship of homologous brain proteolipid to allergic encephalomyelitis in guinea pigs.

Authors:  N P GOLDSTEIN; L C KOLB; H L MASON; G P SAYRE; A G KARLSON
Journal:  Neurology       Date:  1953-08       Impact factor: 9.910

2.  THE WASSERMANN ANTIGEN AND RELATED "ALCOHOL-SOLUBLE" ANTIGENS.

Authors:  A J Weil
Journal:  Bacteriol Rev       Date:  1941-12

3.  Studies on the etiology and pathogenesis of experimental meningoencephalomyelitis in the guinea pig.

Authors:  E C ALVORD
Journal:  J Immunol       Date:  1949-04       Impact factor: 5.422

4.  The relationship of the demyelinating diseases to allergic encephalomyelitis.

Authors:  L C KOLB
Journal:  Medicine (Baltimore)       Date:  1950-05       Impact factor: 1.889

5.  Allergic encephalitis following injection of dialysate of brain tissue.

Authors:  G A HOTTLE; G A NEDZEL
Journal:  Proc Soc Exp Biol Med       Date:  1949-11

6.  ALLERGIC ENCEPHALOMYELITIS IN MONKEYS IN RESPONSE TO INJECTION OF NORMAL MONKEY NERVOUS TISSUE.

Authors:  I M Morgan
Journal:  J Exp Med       Date:  1947-01-01       Impact factor: 14.307

7.  Experimental disseminated encephalomyelitis in white mice.

Authors:  P K OLITSKY; R H YAGER
Journal:  J Exp Med       Date:  1949-09       Impact factor: 14.307

8.  THE RAPID PRODUCTION OF ACUTE DISSEMINATED ENCEPHALOMYELITIS IN RHESUS MONKEYS BY INJECTION OF HETEROLOGOUS AND HOMOLOGOUS BRAIN TISSUE WITH ADJUVANTS.

Authors:  E A Kabat; A Wolf; A E Bezer
Journal:  J Exp Med       Date:  1947-01-01       Impact factor: 14.307

9.  Studies on acute disseminated encephalomyelitis produced experimentally in rhesus monkeys.

Authors:  E A KABAT; A WOLF; A E BEZER
Journal:  J Exp Med       Date:  1948-10-01       Impact factor: 14.307

10.  Acute disseminated encephalomyelitis following immunization with homologous brain extracts; studies on the role of a circulating antibody in the production of the condition in dogs.

Authors:  L THOMAS; P Y PATERSON; B SMITHWICK
Journal:  J Exp Med       Date:  1950-08       Impact factor: 14.307

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  33 in total

1.  [Immunochemical studies for the identification of an ethanol-soluble myelin haptene].

Authors:  B NIEDIECK; E PETTE
Journal:  Klin Wochenschr       Date:  1963-08-01

2.  [Experimental leuk-encephalitis after intrathecal administration of a mucopolysaccharase (hyaluronidase)].

Authors:  A BISCHOFF
Journal:  Dtsch Z Nervenheilkd       Date:  1960

3.  [Pathohistology and pathogenesis of experimental allergic encephalomyelitis of monkeys].

Authors:  G KERSTING; E PETTE
Journal:  Dtsch Z Nervenheilkd       Date:  1957

4.  [Experimental encephalomyelitis in guinea pigs].

Authors:  J ROSS; H J COLMANT; P BOHM
Journal:  Dtsch Z Nervenheilkd       Date:  1958

5.  [Pathogenesis of demyelinating encephalomyelitis (including acute multiple sclerosis) and polyneuritis].

Authors:  E PETTE; H PETTE
Journal:  Klin Wochenschr       Date:  1956-07-15

6.  Studies of the effect of the generalized Shwartzman reaction on the lesions of experimental allergic encephalomyelitis.

Authors:  R D ADAMS; B H WAKSMAN
Journal:  Am J Pathol       Date:  1957 Jan-Feb       Impact factor: 4.307

7.  A history of proteolipids: a personal memoir.

Authors:  M B Lees
Journal:  Neurochem Res       Date:  1998-03       Impact factor: 3.996

8.  Apoptosis of oligodendrocytes in the central nervous system results in rapid focal demyelination.

Authors:  Andrew V Caprariello; Saisho Mangla; Robert H Miller; Stephen M Selkirk
Journal:  Ann Neurol       Date:  2012-09       Impact factor: 10.422

Review 9.  MS as autoimmune disease: myelin antigens.

Authors:  W Fierz
Journal:  Res Immunol       Date:  1989-02

10.  Interaction between human myelin basic protein and lipophilin.

Authors:  D D Wood; G J Vella; M A Moscarello
Journal:  Neurochem Res       Date:  1984-10       Impact factor: 3.996

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