Abstract
Our previous studies have shown that a D-galactose-specific lectin. Ricinus communis-I (RCA-I), does not bind to the plasma membrane of skeletal muscle fibres In DMD whereas it does in normal muscle. RCA-I was subsequently found to recognize a Mr 370000 glycoproteln which is absent or altered in DMD (1. 2).
We have now used RCA-I to characterize the Ultrastructural glycoprotein pattern of developing human skeletal muscle membranes. Five foetuses at high risk of DMD (95% by DNA probe analysis), ranging from 12 to 20 weeks gestation, were compared with five age-matched normal foetuses. The results were compared to the membrane appearance in conventional ultrastructure.
Binding of RCA-I to the muscle fibre basement membrane was consistently strong from the early stages of myogenesis, such as in fusing myoblasts. In both the normal and DMD foetuses RCA-I binding to the plasma membrane was weak but detectable at 12 weeks, more marked by 15 weeks gestation and showed strong labelling at 20 weeks gestation. No difference was observed in RCA-Z binding to the plasma membrane 1n normal and diseased human foetal muscle.
It is concluded that a) the human foetal muscle plasma membrane is undergoing a maturation process between 12 and 20 weeks gestational age leading to an increase 1n expression of RCA-I binding glycoproteins; and b) that the absence of RCA-I binding glycoprotein in mature DMD muscle represents a secondary change developing in the course of the disease.
1) J Neurol Sci 63: 129-142. 1984
2) J Neurol Sci 68: 225-231. 1985
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Voit, T., Sewry, C., Dunn, M. et al. Ultrastructural Localisation Of Ricinus Communis-I Lectin To Skeletal Muscle From Foetuses At High Risk For Duchenne Muscular Dystrophy. Pediatr Res 22, 222 (1987). https://doi.org/10.1203/00006450-198708000-00053
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DOI: https://doi.org/10.1203/00006450-198708000-00053