1985International Journal of Developmental NeuroscienceRequires access

Rat brain glycosyltransferase activities during postnatal development

Pierre Broquet, Mireille Serres‐Guillaumond, Héléne Baubichon‐Cortay, Pierre Louisot

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Abstract

Enzymatic activity of seven glycoprotein and glycolipid glycosyltransferases was studied in microsomal fractions during postnatal development of rat brain from 3 to 42 days after birth. Specific enzymatic variations were detected for some glycosyltransferases, i.d. a maxima was shown at 7 days post partum for the glycoprotein galactosyltransferase and another one at 21 days for galactosylceramide biosynthesis, this latter correlated to myelin synthesis. However, a regular and important activity maxima was always detected for six of the enzymes studied (asialofetuin fucosyltransferase, ovomucoid galactosyltransferase, dolichyl phosphate mannose synthase, ceramide, galactosylceramide and glucosylceramide galactosyltransferases) at the period from 35 to 40 days post partum. As this period corresponds to immediate post-puberty, an endocrinoneuronal control of the glycosyltransferases by sexual hormones is suggested.

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Enzymatic activity of seven glycoprotein and glycolipid glycosyltransferases was studied in microsomal fractions during postnatal development of rat brain from 3 to 42 days after birth. Specific enzymatic variations were detected for some glycosyltransferases, i.d. a maxima was shown at 7 days post partum for the glycoprotein galactosyltransferase and another one at 21 days for galactosylceramide biosynthesis, this latter correlated to myelin synthesis. However, a regular and important activity maxima was always detected for six of the enzymes studied (asialofetuin fucosyltransferase, ovomucoid galactosyltransferase, dolichyl phosphate mannose synthase, ceramide, galactosylceramide and glucosylceramide galactosyltransferases) at the period from 35 to 40 days post partum. As this period corresponds to immediate post-puberty, an endocrinoneuronal control of the glycosyltransferases by sexual hormones is suggested.

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Available abstract

Enzymatic activity of seven glycoprotein and glycolipid glycosyltransferases was studied in microsomal fractions during postnatal development of rat brain from 3 to 42 days after birth. Specific enzymatic variations were detected for some glycosyltransferases, i.d. a maxima was shown at 7 days post partum for the glycoprotein galactosyltransferase and another one at 21 days for galactosylceramide biosynthesis, this latter correlated to myelin synthesis. However, a regular and important activity maxima was always detected for six of the enzymes studied (asialofetuin fucosyltransferase, ovomucoid galactosyltransferase, dolichyl phosphate mannose synthase, ceramide, galactosylceramide and glucosylceramide galactosyltransferases) at the period from 35 to 40 days post partum. As this period corresponds to immediate post-puberty, an endocrinoneuronal control of the glycosyltransferases by sexual hormones is suggested.

Key concepts: Galactosyltransferase, Glycosyltransferase, Glycolipid, Fucosyltransferase, Enzyme, Glycoprotein, Biochemistry, Biosynthesis

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