Studies on glycoconjugate metabolism in developing skeletal muscle membranes
The postnatal development of mammalian skeletal muscle is characterized by changes in the properties of several key membrane glycoprotein enzymes and receptors. In the recent study, CMP-sialic acid: fetuin sialyltransferase and CMP-sialic acid: lactosylceramide sialytransferase activity was characte...
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| Published in | Biochimica et biophysica acta Vol. 755; no. 1; pp. 56 - 64 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
04.01.1983
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0304-4165 0006-3002 1872-8006 |
| DOI | 10.1016/0304-4165(83)90272-6 |
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| Abstract | The postnatal development of mammalian skeletal muscle is characterized by changes in the properties of several key membrane glycoprotein enzymes and receptors. In the recent study, CMP-sialic acid: fetuin sialyltransferase and CMP-sialic acid: lactosylceramide sialytransferase activity was characterized in sarcolemma and sarcoplasmic reticulum membranes isolated from neonatal (0–1 week) and adult (8 week) rabbit skeletal muscle. CMP-sialic acid: fetuin sialytransferase decreased by a factor of 10 in sarcolemma and 6 in sarcoplasmic reticulum during development, whereas CMP-sialic acid: lactosylceramide sialytransferase activity decreased by a factor of 6 in sarcolemma and 18 in sarcoplasmic reticulum. The
K
m for CMP-sialic acid using the lipid acceptor declined during the development of sarcoplasmic reticulum (neonate vs. adult: 538 vs. 33 μM), but not in sarcolemma. The carbohydrate composition of sarcolemma was changed only with respect to total sialic acid content (neonate vs. adult: 67 vs. 44 nmol/mg). Similar analysis of sarcoplasmic reticulum carbohydrates showed decreases in total sialic acid, lipid-bound sialic acid, hexosamines and hexoses. The major ganglioside was GM3 for both types of membrane. No qualitative changes were observed in ganglioside composition comparing neonatal and adult membranes. |
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| AbstractList | The postnatal development of mammalian skeletal muscle is characterized by changes in the properties of several key membrane glycoprotein enzymes and receptors. In the recent study, CMP-sialic acid: fetuin sialyltransferase and CMP-sialic acid: lactosylceramide sialytransferase activity was characterized in sarcolemma and sarcoplasmic reticulum membranes isolated from neonatal (0–1 week) and adult (8 week) rabbit skeletal muscle. CMP-sialic acid: fetuin sialytransferase decreased by a factor of 10 in sarcolemma and 6 in sarcoplasmic reticulum during development, whereas CMP-sialic acid: lactosylceramide sialytransferase activity decreased by a factor of 6 in sarcolemma and 18 in sarcoplasmic reticulum. The
K
m for CMP-sialic acid using the lipid acceptor declined during the development of sarcoplasmic reticulum (neonate vs. adult: 538 vs. 33 μM), but not in sarcolemma. The carbohydrate composition of sarcolemma was changed only with respect to total sialic acid content (neonate vs. adult: 67 vs. 44 nmol/mg). Similar analysis of sarcoplasmic reticulum carbohydrates showed decreases in total sialic acid, lipid-bound sialic acid, hexosamines and hexoses. The major ganglioside was GM3 for both types of membrane. No qualitative changes were observed in ganglioside composition comparing neonatal and adult membranes. The postnatal development of mammalian skeletal muscle is characterized by changes in the properties of several key membrane glycoprotein enzymes and receptors. In the present study, CMP-sialic acid: fetuin sialyltransferase and CMP-sialic acid: lactosylceramide sialyltransferase activity was characterized in sarcolemma and sarcoplasmic reticulum membranes isolated from neonatal (0-1 week) and adult (8 week) rabbit skeletal muscle. CMP-sialic acid: fetuin sialyltransferase decreased by a factor of 10 in sarcolemma and 6 in sarcoplasmic reticulum during development, whereas CMP-sialic acid: lactosylceramide sialyltransferase activity decreased by a factor of 6 in sarcolemma and 18 in sarcoplasmic reticulum. The Km for CMP-sialic acid using the lipid acceptor declined during the development of sarcoplasmic reticulum (neonate vs. adult: 538 vs. 33 microM), but not in sarcolemma. The carbohydrate composition of sarcolemma was changed only with respect to total sialic acid content (neonate vs. adult: 67 vs. 44 nmol/mg). Similar analysis of sarcoplasmic reticulum carbohydrates showed decreases in total sialic acid, lipid-bound sialic acid, hexosamines and hexoses. The major ganglioside was GM3 for both types of membrane. No qualitative changes were observed in ganglioside composition comparing neonatal and adult membranes.The postnatal development of mammalian skeletal muscle is characterized by changes in the properties of several key membrane glycoprotein enzymes and receptors. In the present study, CMP-sialic acid: fetuin sialyltransferase and CMP-sialic acid: lactosylceramide sialyltransferase activity was characterized in sarcolemma and sarcoplasmic reticulum membranes isolated from neonatal (0-1 week) and adult (8 week) rabbit skeletal muscle. CMP-sialic acid: fetuin sialyltransferase decreased by a factor of 10 in sarcolemma and 6 in sarcoplasmic reticulum during development, whereas CMP-sialic acid: lactosylceramide sialyltransferase activity decreased by a factor of 6 in sarcolemma and 18 in sarcoplasmic reticulum. The Km for CMP-sialic acid using the lipid acceptor declined during the development of sarcoplasmic reticulum (neonate vs. adult: 538 vs. 33 microM), but not in sarcolemma. The carbohydrate composition of sarcolemma was changed only with respect to total sialic acid content (neonate vs. adult: 67 vs. 44 nmol/mg). Similar analysis of sarcoplasmic reticulum carbohydrates showed decreases in total sialic acid, lipid-bound sialic acid, hexosamines and hexoses. The major ganglioside was GM3 for both types of membrane. No qualitative changes were observed in ganglioside composition comparing neonatal and adult membranes. The postnatal development of mammalian skeletal muscle is characterized by changes in the properties of several key membrane glycoprotein enzymes and receptors. In the present study, CMP-sialic acid: fetuin sialyltransferase and CMP-sialic acid: lactosylceramide sialyltransferase activity was characterized in sarcolemma and sarcoplasmic reticulum membranes isolated from neonatal (0-1 week) and adult (8 week) rabbit skeletal muscle. CMP-sialic acid: fetuin sialyltransferase decreased by a factor of 10 in sarcolemma and 6 in sarcoplasmic reticulum during development, whereas CMP-sialic acid: lactosylceramide sialyltransferase activity decreased by a factor of 6 in sarcolemma and 18 in sarcoplasmic reticulum. The Km for CMP-sialic acid using the lipid acceptor declined during the development of sarcoplasmic reticulum (neonate vs. adult: 538 vs. 33 microM), but not in sarcolemma. The carbohydrate composition of sarcolemma was changed only with respect to total sialic acid content (neonate vs. adult: 67 vs. 44 nmol/mg). Similar analysis of sarcoplasmic reticulum carbohydrates showed decreases in total sialic acid, lipid-bound sialic acid, hexosamines and hexoses. The major ganglioside was GM3 for both types of membrane. No qualitative changes were observed in ganglioside composition comparing neonatal and adult membranes. |
| Author | Clark, Gary F. Smith, P.Blaise |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/6824728$$D View this record in MEDLINE/PubMed |
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| Keywords | Skeletal muscle membrane Sialytransferase GT1 Development GM1 Glycoconjugate GM3 GD1A GT1A CMP-sialic acid GT1B |
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| SubjectTerms | Aging Animals Animals, Newborn Cell Membrane - metabolism Development Female Glycoconjugate Glycolipids - metabolism Glycoproteins - metabolism Kinetics Membrane Proteins - metabolism Muscle Development Muscles - metabolism Rabbits Sarcoplasmic Reticulum - enzymology Sialyltransferases - metabolism Sialytransferase Skeletal muscle membrane Transferases - metabolism |
| Title | Studies on glycoconjugate metabolism in developing skeletal muscle membranes |
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