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

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Mbl1Ratphosphatidylinositol-4-phosphate binding  IDA  RGD 
Mbl2Ratphosphatidylinositol-4-phosphate binding  IDA  RGD 

Objects Annotated

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


Additional Information