Studies on mannosyl carrier function of retinol and retinoic acid in epithelial and mesenchymal tissues

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Abstract

The mannosyl derivative of phosphorylated vitamin A, mannosylretinylphosphate, is synthesized in vivo and in vitro by most epithelial tissues, including mouse epidermal cells. This compound is but one component of the complex biosynthetic machinery responsible for the assembly of glycoproteins in mammalian membranes; its specific role remains to be understood, even though it has been established that it functions as a carrier of mannose mostly in a direct transfer to protein. The system of five conjugated double bonds appears necessary for this function, since upon saturation the resulting perhydroretinylphosphate is incapable of acting in mannosyl transfer to endogenous microsomal proteins. Using vitamin A-deficient hamsters and rats, retinoic acid was shown to be as active as retinol in restoring the in vivo incorporation of mannose into glycoproteins to normal levels within a short time, in liver and tracheal tissues. Retinoic acid was also active in increasing adhesive properties of spontaneously transformed mouse dermal fibroblasts (3T12 cells) in a reversible manner. The free carboxyl group appeared to be a requirement for this activity inasmuch as the lactonized form of 11-hydroxyretinoic acid was inactive. Even though retinoic acid, as well as retinol, was able to enhance adhesion of 3T12 cells, only the cellular retinoic acid-binding protein was detected, suggesting that the cellular retinol-binding protein is not a requirement for this activity. A metabolite of retinoic acid, compound X, different from retinol, was found incorporated into a mannosylretinoidphosphate (MXP) by 3T12 cells. This derivative constitutes up to 40% of the total radioactive pool of derivatives of retinoic acid after 48 hours of labeling. These data suggest that retinol, as mannosylretinylphosphate, and retinoic acid, as mannosylretinoidphosphate, function as mannosyl carriers in biologic membranes.

Original languageEnglish (US)
Pages (from-to)611-619
Number of pages9
JournalJournal of the American Academy of Dermatology
Volume6
Issue number4 II
StatePublished - 1982
Externally publishedYes

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Tretinoin
Vitamin A
Epithelium
Mannose
Glycoproteins
Cellular Retinol-Binding Proteins
Retinoic Acid Receptors
Membranes
Cell Adhesion
Cricetinae
Adhesives
Proteins
Fibroblasts
Skin
Acids
Liver

ASJC Scopus subject areas

  • Dermatology

Cite this

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title = "Studies on mannosyl carrier function of retinol and retinoic acid in epithelial and mesenchymal tissues",
abstract = "The mannosyl derivative of phosphorylated vitamin A, mannosylretinylphosphate, is synthesized in vivo and in vitro by most epithelial tissues, including mouse epidermal cells. This compound is but one component of the complex biosynthetic machinery responsible for the assembly of glycoproteins in mammalian membranes; its specific role remains to be understood, even though it has been established that it functions as a carrier of mannose mostly in a direct transfer to protein. The system of five conjugated double bonds appears necessary for this function, since upon saturation the resulting perhydroretinylphosphate is incapable of acting in mannosyl transfer to endogenous microsomal proteins. Using vitamin A-deficient hamsters and rats, retinoic acid was shown to be as active as retinol in restoring the in vivo incorporation of mannose into glycoproteins to normal levels within a short time, in liver and tracheal tissues. Retinoic acid was also active in increasing adhesive properties of spontaneously transformed mouse dermal fibroblasts (3T12 cells) in a reversible manner. The free carboxyl group appeared to be a requirement for this activity inasmuch as the lactonized form of 11-hydroxyretinoic acid was inactive. Even though retinoic acid, as well as retinol, was able to enhance adhesion of 3T12 cells, only the cellular retinoic acid-binding protein was detected, suggesting that the cellular retinol-binding protein is not a requirement for this activity. A metabolite of retinoic acid, compound X, different from retinol, was found incorporated into a mannosylretinoidphosphate (MXP) by 3T12 cells. This derivative constitutes up to 40{\%} of the total radioactive pool of derivatives of retinoic acid after 48 hours of labeling. These data suggest that retinol, as mannosylretinylphosphate, and retinoic acid, as mannosylretinoidphosphate, function as mannosyl carriers in biologic membranes.",
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T1 - Studies on mannosyl carrier function of retinol and retinoic acid in epithelial and mesenchymal tissues

AU - De Luca, Luigi M

PY - 1982

Y1 - 1982

N2 - The mannosyl derivative of phosphorylated vitamin A, mannosylretinylphosphate, is synthesized in vivo and in vitro by most epithelial tissues, including mouse epidermal cells. This compound is but one component of the complex biosynthetic machinery responsible for the assembly of glycoproteins in mammalian membranes; its specific role remains to be understood, even though it has been established that it functions as a carrier of mannose mostly in a direct transfer to protein. The system of five conjugated double bonds appears necessary for this function, since upon saturation the resulting perhydroretinylphosphate is incapable of acting in mannosyl transfer to endogenous microsomal proteins. Using vitamin A-deficient hamsters and rats, retinoic acid was shown to be as active as retinol in restoring the in vivo incorporation of mannose into glycoproteins to normal levels within a short time, in liver and tracheal tissues. Retinoic acid was also active in increasing adhesive properties of spontaneously transformed mouse dermal fibroblasts (3T12 cells) in a reversible manner. The free carboxyl group appeared to be a requirement for this activity inasmuch as the lactonized form of 11-hydroxyretinoic acid was inactive. Even though retinoic acid, as well as retinol, was able to enhance adhesion of 3T12 cells, only the cellular retinoic acid-binding protein was detected, suggesting that the cellular retinol-binding protein is not a requirement for this activity. A metabolite of retinoic acid, compound X, different from retinol, was found incorporated into a mannosylretinoidphosphate (MXP) by 3T12 cells. This derivative constitutes up to 40% of the total radioactive pool of derivatives of retinoic acid after 48 hours of labeling. These data suggest that retinol, as mannosylretinylphosphate, and retinoic acid, as mannosylretinoidphosphate, function as mannosyl carriers in biologic membranes.

AB - The mannosyl derivative of phosphorylated vitamin A, mannosylretinylphosphate, is synthesized in vivo and in vitro by most epithelial tissues, including mouse epidermal cells. This compound is but one component of the complex biosynthetic machinery responsible for the assembly of glycoproteins in mammalian membranes; its specific role remains to be understood, even though it has been established that it functions as a carrier of mannose mostly in a direct transfer to protein. The system of five conjugated double bonds appears necessary for this function, since upon saturation the resulting perhydroretinylphosphate is incapable of acting in mannosyl transfer to endogenous microsomal proteins. Using vitamin A-deficient hamsters and rats, retinoic acid was shown to be as active as retinol in restoring the in vivo incorporation of mannose into glycoproteins to normal levels within a short time, in liver and tracheal tissues. Retinoic acid was also active in increasing adhesive properties of spontaneously transformed mouse dermal fibroblasts (3T12 cells) in a reversible manner. The free carboxyl group appeared to be a requirement for this activity inasmuch as the lactonized form of 11-hydroxyretinoic acid was inactive. Even though retinoic acid, as well as retinol, was able to enhance adhesion of 3T12 cells, only the cellular retinoic acid-binding protein was detected, suggesting that the cellular retinol-binding protein is not a requirement for this activity. A metabolite of retinoic acid, compound X, different from retinol, was found incorporated into a mannosylretinoidphosphate (MXP) by 3T12 cells. This derivative constitutes up to 40% of the total radioactive pool of derivatives of retinoic acid after 48 hours of labeling. These data suggest that retinol, as mannosylretinylphosphate, and retinoic acid, as mannosylretinoidphosphate, function as mannosyl carriers in biologic membranes.

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