Abstract：
:Caprine beta-mannosidosis is an inherited lysosomal storage disorder due to a deficiency of beta-mannosidase which cleaves beta-linked mannose residues from the ends of N-asparagine linked oligosaccharides of glycoproteins. Histological and chemical examination has revealed a deficiency of compact myelin in the brains and spinal cords of affected goats. Since myelin-associated glycoprotein (MAG) is glycosylated and its metabolism could be directly affected in this disease, we investigated the possibility of a differential treatment of MAG in caprine beta-mannosidosis in comparison to non-glycosylated myelin proteins. MAG, myelin basic protein (MBP), 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP), proteolipid protein (PLP) and glial fibrillary acidic protein (GFAP) were quantified by western blot analysis in whole homogenates of spinal cords and hemispheres from affected goats at 1, 3 and 6 days of age and from normal controls. The yields of isolated myelin from the spinal cords of affected goats varied from 37 to 63% of normal and were 7% or less of normal from the hemispheres. In mutant spinal cords, the deficits of MAG, CNP and PLP measured in whole homogenates corresponded reasonably well with the decreased myelin yields, but the levels of MBP were consistently much closer to control levels than those of the other myelin proteins. A greater deficiency of PLP than MBP was also apparent in the myelin fractions purified from the affected spinal cords. In homogenates of mutant hemispheres, MAG, MBP, PLP and CNP were undetectable or at trace levels in comparison to controls.(ABSTRACT TRUNCATED AT 250 WORDS)
journal_name
Brain Resjournal_title
Brain researchauthors
Sasaki M,Lovell KL,Möller JRdoi
10.1016/0006-8993(93)90278-usubject
Has Abstractpub_date
1993-08-20 00:00:00pages
127-32issue
1eissn
0006-8993issn
1872-6240pii
0006-8993(93)90278-Ujournal_volume
620pub_type
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