RGD Reference Report - A novel type of binding specificity to phospholipids for rat mannose-binding proteins isolated from serum and liver. - Rat Genome Database

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A novel type of binding specificity to phospholipids for rat mannose-binding proteins isolated from serum and liver.

Authors: Kuroki, Y  Honma, T  Chiba, H  Sano, H  Saitoh, M  Ogasawara, Y  Sohma, H  Akino, T 
Citation: Kuroki Y, etal., FEBS Lett. 1997 Sep 8;414(2):387-92.
RGD ID: 6903277
Pubmed: PMID:9315725   (View Abstract at PubMed)

Mannose-binding protein (MBP) belongs to the collectin subgroup of C-type lectins with specificity for mannose and N-acetylglucosamine sugars. We investigated whether rat MBPs isolated from serum (S-MBP) and liver (L-MBP) interact with phospholipids using antibody against each MBP. Both S- and L-MBPs bound to phosphatidylinositol coated onto microtiter wells in a concentration- and a Ca2+-dependent manner. L-MBP also bound to phosphatidylglycerol and weakly to phosphatidylserine. MBPs interacted with liposomes composed of these lipids. S- and L-MBPs bound to phosphatidylinositol 4-monophosphate. L-MBP also bound to cardiolipin. These results provide evidence for a novel type of ligand binding specificity for MBPs, and raise the possibility that phospholipids are ligands for collectins.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
phosphatidylinositol-4-phosphate binding  IDA 6903277; 6903277 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Mbl1  (mannose binding lectin 1)
Mbl2  (mannose binding lectin 2)


Additional Information