GLYCOLIPID GLYCOSYLTRANSFERASE ACTIVITIES DURING EARLY DEVELOPMENT OF XENOPUS: EFFECT OF RETINOIC ACID
โ Scribed by Federica Rossi; Rosalba Gornati; Angela M Rizzo; Loretta Venturini; Giovanni Bernardini; Bruno Berra
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 105 KB
- Volume
- 23
- Category
- Article
- ISSN
- 1065-6995
No coin nor oath required. For personal study only.
โฆ Synopsis
Retinoic acid (RA) plays an important role in differentiation stage in which it also influences glycoconjugate metabolism. Previous work in our laboratory has shown that treatment with RA modifies glycolipid synthesis and distribution in total Xenopus embryos during development. In this study we have investigated the activity of the following anabolic enzymes involved in glycolipid biosynthesis: sialyltransferase-1 (SAT-1), GM3( 1,4)-N-acetylgalactosaminyltransferase (GalNAcT-1) and LacCer( 1,3)N-acetylglucosaminyltransferase (GlcNAcT-1). These enzymes are located at the branching point of lactosylceramide (Lc 2 ) metabolism. Enzyme activities were assayed after treatment with different doses of RA added exogenously to the medium during the first 7 days of Xenopus embryo development. Our results show that RA activates GlcNAcT-1, the enzyme that drives Lc 2 to the glycolipids of the lacto-series, and SAT-1 that inserts Lc 2 in the ganglio-series pathway. These data support our previous analysis of glycolipid pattern in Xenopus embryos after RA treatment (Rizzo et al., 1995; Cell Biol Int 19: 895-901) indicating a possible correlation between the distribution of glycolipids and the enzymes involved in their metabolism.
๐ SIMILAR VOLUMES
Control of retinoic acid synthesis in vertebrate organisms is undoubtedly important for regulating the numerous retinoid signaling events which occur during development. The mechanisms which accomplish this task involve enzymes such as class I aldehyde dehydrogenase (ALDH1), which has recently been
The Xenopus CNBP homologue (XCNBP) has been cloned from stage 14 neurula. XCNBP encodes a 18.4-kDa protein containing seven highly conserved zinc finger (Zn-finger) repeats (CX 2 CX 4 HX 4 CX 2 ), with sequence similarity to human, mouse, rat, and yeast CNBP. A unique feature of XCNBP is that it con