1978Journal of Biological ChemistryOpen access

The in vivo stimulation of mannose incorporation into mannosylretinylphosphate, dolichylmannosylphosphate, and specific glycopeptides of rat liver by high doses of retinylpalmitate.

John R. Hassell, C S Silverman-Jones, Luigi M. De Luca

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Abstract

Excess vitamin A stimulated the incorporation of mannose into rat liver mannosylretinylphosphate (MRP), dolichylmannosylphosphate (DMP), and into glycoproteins by over 200% during a 20-min labeling period. The glycoproteins were digested with pronase and separated into three components by molecular sieve chromatography. The stimulation of mannose incorporation was greatest in the Peak II glycopeptide (Mr = 6500). In contrast, the incorporation of galactose into glycolipids or glycopeptides was not altered by vitamin A treatment. Analysis of the glycopeptide stimulated by vitamin A treatment showed it to contain mannose, glucose, galactose, and glucosamine in the respective molar ratios of 7:10:17:1 and to be rich in glutamic acid, serine, glycine, aspartic acid, and threonine. The results suggest that excess vitamin A stimulates the incorporation of mannose into glycoproteins by enhancing the synthesis of lipid intermediates involved in specific mannosyl transfer reactions.

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Excess vitamin A stimulated the incorporation of mannose into rat liver mannosylretinylphosphate (MRP), dolichylmannosylphosphate (DMP), and into glycoproteins by over 200% during a 20-min labeling period. The glycoproteins were digested with pronase and separated into three components by molecular sieve chromatography. The stimulation of mannose incorporation was greatest in the Peak II glycopeptide (Mr = 6500). In contrast, the incorporation of galactose into glycolipids or glycopeptides was not altered by vitamin A treatment. Analysis of the glycopeptide stimulated by vitamin A treatment showed it to contain mannose, glucose, galactose, and glucosamine in the respective molar ratios of 7:10:17:1 and to be rich in glutamic acid, serine, glycine, aspartic acid, and threonine. The results suggest that excess vitamin A stimulates the incorporation of mannose into glycoproteins by enhancing the synthesis of lipid intermediates involved in specific mannosyl transfer reactions.

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Available abstract

Excess vitamin A stimulated the incorporation of mannose into rat liver mannosylretinylphosphate (MRP), dolichylmannosylphosphate (DMP), and into glycoproteins by over 200% during a 20-min labeling period. The glycoproteins were digested with pronase and separated into three components by molecular sieve chromatography. The stimulation of mannose incorporation was greatest in the Peak II glycopeptide (Mr = 6500). In contrast, the incorporation of galactose into glycolipids or glycopeptides was not altered by vitamin A treatment. Analysis of the glycopeptide stimulated by vitamin A treatment showed it to contain mannose, glucose, galactose, and glucosamine in the respective molar ratios of 7:10:17:1 and to be rich in glutamic acid, serine, glycine, aspartic acid, and threonine. The results suggest that excess vitamin A stimulates the incorporation of mannose into glycoproteins by enhancing the synthesis of lipid intermediates involved in specific mannosyl transfer reactions.

Key concepts: Glycopeptide, Mannose, Pronase, Biochemistry, Glucosamine, Threonine, Glycoprotein, Chemistry

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The in vivo stimulation of mannose incorporation into mannosylretinylphosphate, dolichylmannosylphosphate, and specific glycopeptides of rat liver by high doses of retinylpalmitate. — Research Paper | ScholarLens