Abstract
Ectoglycosyltransferase activities were measured in cultured normal and mucolipidosis II fibroblasts using endogenous glycoproteins and glycolipids and whole cells. Nucleotide pyrophosphatase, known to interfere with glycosyltransferases, was completely inhibited with 6 mM 5’ AMP. Since preliminary experiments have shown multiple abnormalities of ectoglycosyltransferases in mucolipidosis II fibroblasts (Di Donato, unpublished results), galactosyl (Gal)- and Aiacetylglucosaminyl (GluNac)- transferase were studied in further detail in confluent and non- confluent cultures of normal and patient fibroblasts. Activities of both transferases on glycoproteins were higher in nonconfluent cultures. A 50% reduced activity of Gal-transferase was measured in confluent mucolipidosis II cultures and of GluNac- transferase in nonconfluent mucolipidosis II cultures towards incorporation of sugar precursors into glycoprotein. Substrate saturation kinetics of both transferases in mucolipidosis II fibroblasts revealed an abnormal Km for Gal incorporation into endogenous glycoproteins. Glycosylation of glycolipids in mucolipidosis fibroblasts was normal. Speculation: The finding of multiple abnormalities of ectoglycosyltransfer-ases in mucolipidosis fibroblasts is compatible with an abnormal composition of the cell membrane glycoproteins. We speculate that there could be a link between these results and the abnormal glycoproteins recognition marker of lysosomal enzymes, both resulting from a common defect in glycosylation.
| Original language | English |
|---|---|
| Pages (from-to) | 1094-1096 |
| Number of pages | 3 |
| Journal | Pediatric Research |
| Volume | 11 |
| Issue number | 10 |
| Publication status | Published - 1977 |
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ASJC Scopus subject areas
- Pediatrics, Perinatology, and Child Health
Cite this
Multiple abnormalities of ectoglycosyltransferases in cultured fibroblasts from patients with mucolipidosis II : Possible indication for abnormal plasma membrane glycoproteins. / Di Donato, Stefano; Wiesmann, Ulrich N.; Rossi, E.; Herschkowitz, Norbert.
In: Pediatric Research, Vol. 11, No. 10, 1977, p. 1094-1096.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Multiple abnormalities of ectoglycosyltransferases in cultured fibroblasts from patients with mucolipidosis II
T2 - Possible indication for abnormal plasma membrane glycoproteins
AU - Di Donato, Stefano
AU - Wiesmann, Ulrich N.
AU - Rossi, E.
AU - Herschkowitz, Norbert
PY - 1977
Y1 - 1977
N2 - Ectoglycosyltransferase activities were measured in cultured normal and mucolipidosis II fibroblasts using endogenous glycoproteins and glycolipids and whole cells. Nucleotide pyrophosphatase, known to interfere with glycosyltransferases, was completely inhibited with 6 mM 5’ AMP. Since preliminary experiments have shown multiple abnormalities of ectoglycosyltransferases in mucolipidosis II fibroblasts (Di Donato, unpublished results), galactosyl (Gal)- and Aiacetylglucosaminyl (GluNac)- transferase were studied in further detail in confluent and non- confluent cultures of normal and patient fibroblasts. Activities of both transferases on glycoproteins were higher in nonconfluent cultures. A 50% reduced activity of Gal-transferase was measured in confluent mucolipidosis II cultures and of GluNac- transferase in nonconfluent mucolipidosis II cultures towards incorporation of sugar precursors into glycoprotein. Substrate saturation kinetics of both transferases in mucolipidosis II fibroblasts revealed an abnormal Km for Gal incorporation into endogenous glycoproteins. Glycosylation of glycolipids in mucolipidosis fibroblasts was normal. Speculation: The finding of multiple abnormalities of ectoglycosyltransfer-ases in mucolipidosis fibroblasts is compatible with an abnormal composition of the cell membrane glycoproteins. We speculate that there could be a link between these results and the abnormal glycoproteins recognition marker of lysosomal enzymes, both resulting from a common defect in glycosylation.
AB - Ectoglycosyltransferase activities were measured in cultured normal and mucolipidosis II fibroblasts using endogenous glycoproteins and glycolipids and whole cells. Nucleotide pyrophosphatase, known to interfere with glycosyltransferases, was completely inhibited with 6 mM 5’ AMP. Since preliminary experiments have shown multiple abnormalities of ectoglycosyltransferases in mucolipidosis II fibroblasts (Di Donato, unpublished results), galactosyl (Gal)- and Aiacetylglucosaminyl (GluNac)- transferase were studied in further detail in confluent and non- confluent cultures of normal and patient fibroblasts. Activities of both transferases on glycoproteins were higher in nonconfluent cultures. A 50% reduced activity of Gal-transferase was measured in confluent mucolipidosis II cultures and of GluNac- transferase in nonconfluent mucolipidosis II cultures towards incorporation of sugar precursors into glycoprotein. Substrate saturation kinetics of both transferases in mucolipidosis II fibroblasts revealed an abnormal Km for Gal incorporation into endogenous glycoproteins. Glycosylation of glycolipids in mucolipidosis fibroblasts was normal. Speculation: The finding of multiple abnormalities of ectoglycosyltransfer-ases in mucolipidosis fibroblasts is compatible with an abnormal composition of the cell membrane glycoproteins. We speculate that there could be a link between these results and the abnormal glycoproteins recognition marker of lysosomal enzymes, both resulting from a common defect in glycosylation.
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M3 - Article
C2 - 904973
AN - SCOPUS:0017696909
VL - 11
SP - 1094
EP - 1096
JO - Pediatric Research
JF - Pediatric Research
SN - 0031-3998
IS - 10
ER -