Goodpasture Antigen-binding Protein/Ceramide Transporter Binds to Human Serum Amyloid P-Component and Is Present in Brain Amyloid Plaques

Serum amyloid P component (SAP) is a non-fibrillar glycoprotein belonging to the pentraxin family of the innate immune system. SAP is present in plasma, basement membranes, and amyloid deposits. This study demonstrates, for the first time, that the Goodpasture antigen-binding protein (GPBP) binds to...

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Published in:	The Journal of biological chemistry 2012-04, Vol.287 (18), p.14897-14911
Main Authors:	Mencarelli, Chiara, Bode, Gerard H., Losen, Mario, Kulharia, Mahesh, Molenaar, Peter C., Veerhuis, Robert, Steinbusch, Harry W.M., De Baets, Marc H., Nicolaes, Gerry A.F., Martinez-Martinez, Pilar
Format:	Article
Language:	eng
Subjects:	Alzheimer Disease - blood Alzheimer Disease - genetics Amyloid-β (Aβ) Animals Brain Brain - metabolism Ceramide Transporter (CERT) Goodpasture Binding Protein (GPBP) Humans Mice Mice, Transgenic Multiprotein Complexes - blood Multiprotein Complexes - genetics Pentraxins Protein Binding Protein Structure Protein Structure and Folding Protein Structure, Tertiary Protein-Protein Interactions Protein-Serine-Threonine Kinases - blood Protein-Serine-Threonine Kinases - genetics Serum Amyloid P Component (SAP) Serum Amyloid P-Component - genetics Serum Amyloid P-Component - metabolism Surface Plasmon Resonance (SPR)
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Summary:	Serum amyloid P component (SAP) is a non-fibrillar glycoprotein belonging to the pentraxin family of the innate immune system. SAP is present in plasma, basement membranes, and amyloid deposits. This study demonstrates, for the first time, that the Goodpasture antigen-binding protein (GPBP) binds to human SAP. GPBP is a nonconventional Ser/Thr kinase for basement membrane type IV collagen. Also GPBP is found in plasma and in the extracellular matrix. In the present study, we demonstrate that GPBP specifically binds SAP in its physiological conformations, pentamers and decamers. The START domain in GPBP is important for this interaction. SAP and GPBP form complexes in blood and partly colocalize in amyloid plaques from Alzheimer disease patients. These data suggest the existence of complexes of SAP and GPBP under physiological and pathological conditions. These complexes are important for understanding basement membrane, blood physiology, and plaque formation in Alzheimer disease. Background: The Goodpasture antigen-binding protein (GPBP) and serum amyloid P component (SAP) bind to type IV collagen and are found in plasma. Results: GPBP binds to human SAP. Conclusion: GPBP and SAP form complexes under physiological and pathological conditions. Significance: This interaction might be involved in protein aggregation in Alzheimer disease and the resulting innate immune response.
ISSN:	0021-9258 1083-351X