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Literature summary for 3.1.1.34 extracted from

  • Bruce, K.D.; Gorkhali, S.; Given, K.; Coates, A.M.; Boyle, K.E.; Macklin, W.B.; Eckel, R.H.
    Lipoprotein lipase is a feature of alternatively-activated microglia and may facilitate lipid uptake in the CNS during demyelination (2018), Front. Mol. Neurosci., 11, 57 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.34

Cloned(Commentary)

Cloned (Comment) Organism
gene Lpl, real-time PCR enzyme expression analysis Homo sapiens
gene Lpl, real-time PCR enzyme expression analysis Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
triacylglycerol + H2O Homo sapiens
-
 diacylglycerol + a carboxylate
-
 ?
triacylglycerol + H2O Mus musculus
-
 diacylglycerol + a carboxylate
-
 ?
triacylglycerol + H2O Mus musculus C57BL/6J
-
 diacylglycerol + a carboxylate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P06858
-
-
Mus musculus P11152
-
-
Mus musculus C57BL/6J P11152
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Homo sapiens
-
brain
-
 Mus musculus
-
BV-2 cell
-
 Mus musculus
-
central nervous system
-
 Homo sapiens
-
central nervous system
-
 Mus musculus
-
macrophage
-
 Homo sapiens
-
macrophage
-
 Mus musculus
-
microglial cell line
-
 Homo sapiens
-
microglial cell line
-
 Mus musculus
-
Schwann cell
-
 Homo sapiens
-
Schwann cell
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzymatic activity of cell-surface heparin-released LPL is measured using a phospholipid (PL)/3H-triolein substrate with human serum as a source of ApoC2 Mus musculus ?
-
 ?
additional information tic activity of cell-surface heparin-released LPL is measured using a phospholipid (PL)/3H-triolein substrate with human serum as a source of ApoC2 Homo sapiens ?
-
 ?
additional information enzymatic activity of cell-surface heparin-released LPL is measured using a phospholipid (PL)/3H-triolein substrate with human serum as a source of ApoC2 Mus musculus C57BL/6J ?
-
 ?
triacylglycerol + H2O
-
 Homo sapiens diacylglycerol + a carboxylate
-
 ?
triacylglycerol + H2O
-
 Mus musculus diacylglycerol + a carboxylate
-
 ?
triacylglycerol + H2O
-
 Mus musculus C57BL/6J diacylglycerol + a carboxylate
-
 ?

Synonyms

Synonyms Comment Organism
LPL
-
 Homo sapiens
LPL
-
 Mus musculus

General Information

General Information Comment Organism
malfunction lipoprotein lipase (LPL) is increased during the onset of remyelination, which is associated with an anti-inflammatory reparative microglial phenotype, and may facilitate the uptake of myelin-derived lipids in the CNS Homo sapiens
malfunction lipoprotein lipase (LPL)-deficient cells show dramatically reduced expression of anti-inflammatory markers, YM1, and arginase 1 and increased expression of pro-inflammatory markers, such as iNOS compared to wild-type cells. LPL is increased during the onset of remyelination, which is associated with an anti-inflammatory reparative microglial phenotype, and may facilitate the uptake of myelin-derived lipids in the CNS Mus musculus
physiological function lipoprotein lipase is a feature of alternatively-activated microglia and may facilitate lipid uptake in the CNS during demyelination. Lipoprotein lipase is involved in microglial lipid uptake. Lipoprotein lipase (LPL) is the rate-limiting enzyme in the hydrolysis of triglyceride-rich lipoproteins and is increased in Schwann cells and macrophages following nerve crush injury in the peripheral nervous system (PNS), suggesting that LPL may help scavenge myelin-derived lipids. Role of LPL in microglia, overview Homo sapiens
physiological function lipoprotein lipase is a feature of alternatively-activated microglia, reparative microglia cells, and may facilitate lipid uptake in the CNS during demyelination. Lipoprotein lipase is involved in microglial lipid uptake. LPL may support repair through the clearance of myelin-derived lipids. Lipoprotein lipase (LPL) is the rate-limiting enzyme in the hydrolysis of triglyceride-rich lipoproteins and is increased in Schwann cells and macrophages following nerve crush injury in the peripheral nervous system (PNS), suggesting that LPL may help scavenge myelin-derived lipids. Role of LPL in microglia, overview Mus musculus