Cell-mediated immunity to measles, myelin basic protein, and central nervous system extract in multiple sclerosis: A longitudinal study employing direct buffy coat migration inhibition assays

Neurology ◽  
1978 ◽  
Vol 28 (8) ◽  
pp. 798-798 ◽  
Author(s):  
R. P. Lisak ◽  
B. Zweiman ◽  
D. Waters ◽  
H. Koprowski ◽  
D. E. Pleasure
Author(s):  
M.P. Day ◽  
J.H. Day ◽  
P.L. Mann

SUMMARY:Twenty-four patients with multiple sclerosis were evaluated and classified according to their clinical state. Specific migration inhibition studies were carried out on blood samples from each using myelin basic protein, an acid soluble protein fraction isolated from normal human CNS white matter, and multiple sclerosis myelin basic protein isolated from patients who had the disease, as the antigenic material. This test system employed selected media. Results were compared with those of normal controls and patients with other neurological disease states. Antigen concentration of 500 μ glml in serum free medium combined to produce the greatest inhibiting effect on leukocytes in patients with apparent multiple sclerosis and differentiated these patients from those in the other groups tested.Leukocytes in patients who had probable multiple sclerosis with partial impairment, signifying possible current activity of the disease, were especially inhibited as compared to the leukocytes from other groups tested against myelin antigen. Cerebrospinal fluid from affected patients when used as a media enhanced the test.This study suggests that migration inhibition of peripheral leukocytes using myelin protein may be useful in the diagnosis of patients with multiple sclerosis. There is additional evidence that the degree of leukocyte migration inhibition may reflect activity of the disease with its consequent implications on treatment and prognosis.


1993 ◽  
Vol 13 (5) ◽  
pp. 3103-3112
Author(s):  
S Haas ◽  
J Gordon ◽  
K Khalili

Transcription of the myelin basic protein (MBP) gene is regulated in a cell-type-specific and developmental stage-specific manner during myelin formation in the murine central nervous system. The 5'-flanking region of the MBP gene contains several regulatory elements that differentially contribute to the cell-type-specific transcription of MBP in cells derived from the central nervous system. The proximal element, termed MB1, which is located between nucleotides -14 and -50 with respect to the RNA start site, has previously been shown to have characteristics of a cell-type-specific enhancer element. In this study, we used band shift and UV cross-linking assays to identify DNA-binding proteins in mouse brain nuclear extract which interact with the MB1 element. Fractionation of these extracts has allowed the identification of a 38- to 41-kDa nuclear protein, derived from mouse brain tissue at the peak of myelination, which specifically binds the MB1 DNA sequence. Fractions enriched in the MB1-binding protein have been shown to stimulate transcription of the MBP promoter in extract derived from HeLa cells. MB1 binding protein activity is expressed in a tissue-specific and development stage-specific pattern which coincides with the pattern of MBP transcription, suggesting that this protein may be a biologically relevant transcription factor for the MBP gene in vivo.


1978 ◽  
Vol 76 (2) ◽  
pp. 502-511 ◽  
Author(s):  
J R Mendell ◽  
J N Whitaker

The location of myelin encephalitogenic or basic protein (BP) in peripheral nervous system (PNS) and central nervous system (CNS) was investigated by immunofluorescence and horseradish peroxidase (HRP) immunocytochemistry. BP or cross-reacting material could be clearly localized to myelin by immunofluorescence and light microscope HRP immunocytochemistry. Fine structural studies proved to be much more difficult, especially in the CNS, due to problems in tissue fixation and penetration of reagents. Sequential fixation in aldehyde followed by ethanol or methanol provided the best conditions for ultrastructural indirect immunocytochemical studies. In PNS tissue, anti-BP was localized exclusively to the intraperiod line of myelin. Because of limitations in technique, the localization of BP in CNS myelin could not be unequivocally determined. In both PNS and CNS tissue, no anti-BP binding to nonmyelin cellular or membranous elements was detected.


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