Sialidase activity in mouse neuroblastoma cell lines
Sialidase activity was determined for three different neuroblastoma clonal lines derived from the A/J strain mouse C1300 neuroblastoma line. For each cell line, the endogenous and exogenous activities were less than 1 nmol sialic acid released/mg protein/90 min and 50 min reaction time, respectively...
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| Published in | Neurochemical research Vol. 1; no. 2; p. 181 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
United States
01.04.1976
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| Abstract | Sialidase activity was determined for three different neuroblastoma clonal lines derived from the A/J strain mouse C1300 neuroblastoma line. For each cell line, the endogenous and exogenous activities were less than 1 nmol sialic acid released/mg protein/90 min and 50 min reaction time, respectively. The C1300 tumor had similarly low levels of sialidase activity. The sialidase activity associated with the neuroblastomas is less than that associated with synaptosomes. Each cell line had a distinctly different ganglioside pattern varying in complexity from GM3 to GD1a. Treatment of the cells withVibrio cholerae sialidase under isosmotic conditions showed that cell-surface sialyl residues were susceptible to sialidase activity, with some of the susceptible residues coming from the ganglioside constituents. Of the total number ofV. cholerae sialidase-releasable sialyl residues, 50-60% were released by the neuroblastoma sialidase acting on endogenous substrate. |
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| AbstractList | Sialidase activity was determined for three different neuroblastoma clonal lines derived from the A/J strain mouse C1300 neuroblastoma line. For each cell line, the endogenous and exogenous activities were less than 1 nmol sialic acid released/mg protein/90 min and 50 min reaction time, respectively. The C1300 tumor had similarly low levels of sialidase activity. The sialidase activity associated with the neuroblastomas is less than that associated with synaptosomes. Each cell line had a distinctly different ganglioside pattern varying in complexity from GM3 to GD1a. Treatment of the cells withVibrio cholerae sialidase under isosmotic conditions showed that cell-surface sialyl residues were susceptible to sialidase activity, with some of the susceptible residues coming from the ganglioside constituents. Of the total number ofV. cholerae sialidase-releasable sialyl residues, 50-60% were released by the neuroblastoma sialidase acting on endogenous substrate. |
| Author | Schengrund, C L Nelson, J T |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24271341$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1007_BF03160146 crossref_primary_10_1111_j_1471_4159_1978_tb10513_x crossref_primary_10_1111_j_1471_4159_1982_tb11480_x crossref_primary_10_1016_S0300_9084_03_00047_6 crossref_primary_10_1111_j_1471_4159_1977_tb10737_x crossref_primary_10_1007_BF03159989 crossref_primary_10_1016_0014_4827_78_90048_4 crossref_primary_10_1002_1097_0142_19851201_56_11_2640__AID_CNCR2820561118_3_0_CO_2_W crossref_primary_10_1111_j_1471_4159_1979_tb00397_x crossref_primary_10_1111_j_1471_4159_1989_tb08539_x crossref_primary_10_1016_S0022_3468_87_80122_7 |
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