Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.291 extracted from

  • Xu, Z.; Zhou, J.; McCoy, D.M.; Mallampalli, R.K.
    LASS5 is the predominant ceramide synthase isoform involved in de novo sphingolipid synthesis in lung epithelia (2005), J. Lipid Res., 46, 1229-1238 .
    View publication on PubMed
Search for more literature for 2.3.1.291

Inhibitors

Inhibitors Comment Organism Structure
fumonisin B1
-
 Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-associated Mus musculus 16020
-

Organism

Organism UniProt Comment Textmining
Mus musculus Q9D6K9
-
-

Source Tissue

Source Tissue Comment Organism Textmining
epithelium
-
 Mus musculus
-
lung LASS5 is the predominant ceramide synthase isoform detected in lung epithelia Mus musculus
-

Synonyms

Synonyms Comment Organism
LASS5
-
 Mus musculus
longevity assurance homolog 5
-
 Mus musculus

Expression

Organism Comment Expression
Mus musculus pulmonary LASS5 is developmentally regulated, but its expression is spatially and gender nonspecific additional information

General Information

General Information Comment Organism
physiological function exogenously expressed LASS5 in lung epithelia triggers increased ceramide synthesis, knockdown studies using fumonisin B1 or LASS5 siRNA reduce ceramide synthase activity by 78% or 45%, respectively. Overexpression of LASS5 also reduces phosphatidylcholine synthesis. Maximal inhibition is achieved when LASS5 is coexpressed with a plasmid encoding a neutral sphingomyelinase involved in sphingomyelin hydrolysis Mus musculus