Analysis of low molecular weight intracellular associations of a human mannan binding lectin (MBL)

Human mannan binding lectin (MBL) is a member of the collectins, a group of proteins that contain a dual structure with a lectin and a collagenous moieties. The collectins are considered as major actors of innate immunity. We report the presence of low molecular weight intracellular MBL forms in hum...

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Bibliographic Details
Published in:Molecular immunology 2004, Vol.40 (11), p.795-801
Main Authors: Dumestre-perard, C, Ponard, D, Colomb, M.G
Format: Article
Language:English
Subjects:
Biochemistry, Molecular Biology
Collagen
Collagenases
Collagenases - metabolism
Electrophoresis, Polyacrylamide Gel
Hepatocytes
Hepatocytes - metabolism
Human lectin
Humans
Kinetics
Life Sciences
Ligands
Mannan binding lectin (MBL)
Mannose
Mannose - metabolism
Mannose-Binding Lectin
Mannose-Binding Lectin - metabolism
Polypeptides polymers
Serine Endopeptidases
Serine Endopeptidases - metabolism
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Summary:Human mannan binding lectin (MBL) is a member of the collectins, a group of proteins that contain a dual structure with a lectin and a collagenous moieties. The collectins are considered as major actors of innate immunity. We report the presence of low molecular weight intracellular MBL forms in human hepatocytic cell lysates, with binding capacities associated to its lectin and/or its collagen moiety. Competition with d-mannose and with antibodies directed against the lectin binding site of MBL indicate that the 60 kDa form represents an intracellular association of MBL through its lectin moiety. The effects of collagenase or MBL associated serine proteases (MASPs) from a MBL deficient plasma, gave evidence that the 60 KDa form contains also collagen and suggested the binding of a ligand to this collagen part. These results show that this intracellular form of MBL shares binding properties with circulating MBL. The binding potential of the lectin and the collagenous parts of precursor forms of intracellular MBL may suggest that they behave as molecular chaperone. The complexity of MBL structure and functions deserves further investigation on other intracellular forms of MBL.
ISSN:0161-5890
1872-9142
DOI:10.1016/j.molimm.2003.10.012