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Literature summary for 1.14.18.2 extracted from

  • Song, K.H.; Kang, Y.J.; Jin, U.H.; Park, Y.I.; Kim, S.M.; Seong, H.H.; Hwang, S.; Yang, B.S.; Im, G.S.; Min, K.S.; Kim, J.H.; Chang, Y.C.; Kim, N.H.; Lee, Y.C.; Kim, C.H.
    Cloning and functional characterization of pig CMP-N-acetylneuraminic acid hydroxylase for the synthesis of N-glycolylneuraminic acid as the xenoantigenic determinant in pig-human xenotransplantation (2010), Biochem. J., 427, 179-188.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in pig kidney PK15 cells and human vascular endothelial ECV304 cells Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa A8WAC5
-
-

Source Tissue

Source Tissue Comment Organism Textmining
colon
-
 Sus scrofa
-
intestine cDNA generated from, mRNA highly expressed Sus scrofa
-
rectum
-
 Sus scrofa
-
spleen
-
 Sus scrofa
-
tongue
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ectopic expression of pcmah in pig kidney PK15 cells and human vascular endothelial ECV304 cells leads to an elevated expression of N-glycolylneuraminic acid Sus scrofa ?
-
 ?

Synonyms

Synonyms Comment Organism
CMP-Neu5Ac hydroxylase
-
 Sus scrofa
pcmah
-
 Sus scrofa

General Information

General Information Comment Organism
malfunction pcmah silencing by short hairpin RNA results in a decrease in N-glycolylneuraminic acid content and xenoantigenicity in pig kidney PK15 cells Sus scrofa