scholarly journals Serum Amyloid P Component (SAP)-Like Protein From Botryllid Ascidians Provides a Clue to Amyloid Function

1992 ◽  
Vol 3 (1) ◽  
pp. 67-84 ◽  
Author(s):  
V. L. Scofield ◽  
L. Puntambekar ◽  
S. F. Schluter ◽  
D. R. Coombe
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Serum Amyloid ◽  
Amyloid Protein ◽  
Inflammatory Lesions ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid Deposits ◽  
Fouling Organisms ◽  
Amyloid P

The HA-1 lectin isolated from Botrylloides leachii has an amino acid composition similar to that of mammalian serum amyloid protein (SAP). SAP is a universal component of mammalian amyloid deposits. Like SAP, HA-1 has a disc ultrastructure, and antibody to HA-1 binds both (a) to amyloidlike fibers deposited between rejectedBotrylloidescolonies and (b) to cerebral amyloid deposits in Alzheimer's disease brains. Deposition of protochordate amyloid within rejection sites and surrounding fouling organisms implies that these fibers function as barriers to allogeneic and infectious challenge. Similarly, mammalian amyloid may also function to contain inflammatory lesions and to limit the spread of certain infections. Pathological amyloidotic conditions in humans, such as Alzheimer's disease, may result from unregulated expression of this primitive encapsulation response.

scholarly journals Pharmacological removal of serum amyloid P component from intracerebral plaques and cerebrovascular Aβ amyloid deposits in vivo

Open Biology ◽  
2016 ◽  
Vol 6 (2) ◽  
pp. 150202 ◽  
Author(s):  
Raya Al-Shawi ◽  
Glenys A. Tennent ◽  
David J. Millar ◽  
Angela Richard-Londt ◽  
Sebastian Brandner ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid Deposits ◽  
Amyloid P ◽  
Cerebrovascular Amyloid

Human amyloid deposits always contain the normal plasma protein serum amyloid P component (SAP), owing to its avid but reversible binding to all amyloid fibrils, including the amyloid β (Aβ) fibrils in the cerebral parenchyma plaques and cerebrovascular amyloid deposits of Alzheimer's disease (AD) and cerebral amyloid angiopathy (CAA). SAP promotes amyloid fibril formation in vitro , contributes to persistence of amyloid in vivo and is also itself directly toxic to cerebral neurons. We therefore developed (R)-1-[6-[(R)-2-carboxy-pyrrolidin-1-yl]-6-oxo-hexanoyl]pyrrolidine-2-carboxylic acid (CPHPC), a drug that removes SAP from the blood, and thereby also from the cerebrospinal fluid (CSF), in patients with AD. Here we report that, after introduction of transgenic human SAP expression in the TASTPM double transgenic mouse model of AD, all the amyloid deposits contained human SAP. Depletion of circulating human SAP by CPHPC administration in these mice removed all detectable human SAP from both the intracerebral and cerebrovascular amyloid. The demonstration that removal of SAP from the blood and CSF also removes it from these amyloid deposits crucially validates the strategy of the forthcoming ‘Depletion of serum amyloid P component in Alzheimer's disease (DESPIAD)’ clinical trial of CPHPC. The results also strongly support clinical testing of CPHPC in patients with CAA.

P2-307: CPHPC depletes serum amyloid P component from the cerebrospinal fluid in Alzheimer's disease

2008 ◽  
Vol 4 ◽  
pp. T462-T462
Author(s):  
Basil H. Ridha ◽  
Martin N. Rossor ◽  
Sebastian J. Crutch ◽  
Geoffrey Keir ◽  
J. Ruth Gallimore ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cerebrospinal Fluid ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P

Serum Amyloid P Component Scintigraphy in Alzheimer's Disease

1996 ◽  
Vol 90 (s34) ◽  
pp. 18P-18P
Author(s):  
L B Lovat ◽  
A A J O'brien ◽  
S J Armstrong ◽  
S Madhoo ◽  
C J Bulpitt ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P
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