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Literature summary extracted from

  • Seyrantepe, V.; Iannello, A.; Liang, F.; Kanshin, E.; Jayanth, P.; Samarani, S.; Szewczuk, M.R.; Ahmad, A.; Pshezhetsky, A.V.
    Regulation of phagocytosis in macrophages by neuraminidase 1 (2010), J. Biol. Chem., 285, 206-215.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.18 cathepsin A
-
Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.18 cell surface
-
Mus musculus 9986
-

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.18 Mus musculus O35657
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.18 kidney
-
Mus musculus
-
3.2.1.18 macrophage
-
Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.18 2'-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O
-
Mus musculus 4-methylumbelliferone + N-acetylneuraminic acid
-
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Synonyms

EC Number Synonyms Comment Organism
3.2.1.18 NEU1
-
Mus musculus
3.2.1.18 neuraminidase 1
-
Mus musculus

General Information

EC Number General Information Comment Organism
3.2.1.18 malfunction the absence of Neu1 results in the increased sialylation of the cell surface proteins, probably affecting multiple receptors for phagocytosis. Macrophages from the Neu1-deficient mice show increased sialylation and impaired phosphorylation of FcgammaRas well as markedly reduced phosphorylation of Syk kinase in response to treatment with immunoglobulin G-opsonized beads Mus musculus
3.2.1.18 physiological function treatment of the cells with purified mouse Neu1 reduces surface sialylation and restores phagocytosis. Cell surface Neu1 activates the phagocytosis in macrophages and dendritic cells through desialylation of surface receptors, thus, contributing to their functional integrity Mus musculus