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  1. Article ; Online: Transthyretin amyloidosis: new answers but many questions.

    Pepys, Mark B

    Journal of internal medicine

    2021  Volume 289, Issue 6, Page(s) 933–935

    MeSH term(s) Amyloid Neuropathies, Familial/genetics ; Humans
    Language English
    Publishing date 2021-02-20
    Publishing country England
    Document type Editorial
    ZDB-ID 96274-0
    ISSN 1365-2796 ; 0954-6820
    ISSN (online) 1365-2796
    ISSN 0954-6820
    DOI 10.1111/joim.13250
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ua VI Zs.44: Show issues Location:
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  2. Article ; Online: C-reactive protein predicts outcome in COVID-19: is it also a therapeutic target?

    Pepys, Mark B

    European heart journal

    2021  Volume 42, Issue 23, Page(s) 2280–2283

    MeSH term(s) C-Reactive Protein ; COVID-19 ; Humans ; SARS-CoV-2
    Chemical Substances C-Reactive Protein (9007-41-4)
    Language English
    Publishing date 2021-03-26
    Publishing country England
    Document type Editorial ; Comment
    ZDB-ID 603098-1
    ISSN 1522-9645 ; 0195-668X
    ISSN (online) 1522-9645
    ISSN 0195-668X
    DOI 10.1093/eurheartj/ehab169
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    Zs.A 1563: Show issues Location:
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    Zs.MO 640: Show issues

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  3. Article ; Online: The Pentraxins 1975-2018: Serendipity, Diagnostics and Drugs.

    Pepys, Mark B

    Frontiers in immunology

    2018  Volume 9, Page(s) 2382

    Abstract: The phylogenetically ancient, pentraxin family of plasma proteins, comprises C-reactive protein (CRP) and serum amyloid P component (SAP) in humans and the homologous proteins in other species. They are composed of five, identical, non-covalently ... ...

    Abstract The phylogenetically ancient, pentraxin family of plasma proteins, comprises C-reactive protein (CRP) and serum amyloid P component (SAP) in humans and the homologous proteins in other species. They are composed of five, identical, non-covalently associated protomers arranged with cyclic pentameric symmetry in a disc-like configuration. Each protomer has a calcium dependent site that mediates the particular specific ligand binding responsible for all the rigorously established functional properties of these proteins. No genetic deficiency of either human CRP or SAP has been reported, nor even any sequence polymorphism in the proteins themselves. Although their actual functions in humans are therefore unknown, gene deletion studies in mice demonstrate that both proteins can contribute to innate immunity. CRP is the classical human acute phase protein, routinely measured in clinical practice worldwide to monitor disease activity. Human SAP, which is not an acute phase protein, is a universal constituent of all human amyloid deposits as a result of its avid specific binding to amyloid fibrils of all types. SAP thereby contributes to amyloid formation and persistence
    MeSH term(s) Alzheimer Disease/diagnosis ; Alzheimer Disease/etiology ; Alzheimer Disease/metabolism ; Alzheimer Disease/therapy ; Amyloidosis/diagnosis ; Amyloidosis/etiology ; Amyloidosis/metabolism ; Amyloidosis/therapy ; Animals ; Biomarkers ; C-Reactive Protein/chemistry ; C-Reactive Protein/metabolism ; Humans ; Molecular Targeted Therapy ; Protein Aggregates ; Protein Aggregation, Pathological/metabolism ; Protein Binding ; Serum Amyloid P-Component/chemistry ; Serum Amyloid P-Component/metabolism ; Serum Amyloid P-Component/ultrastructure ; Structure-Activity Relationship
    Chemical Substances Biomarkers ; Protein Aggregates ; Serum Amyloid P-Component ; C-Reactive Protein (9007-41-4)
    Language English
    Publishing date 2018-10-16
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2018.02382
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  4. Article ; Online: Immunotherapeutic clearance of systemic amyloid deposits by antibodies to serum amyloid P component.

    Pepys, Mark B

    Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis

    2016  Volume 24, Issue sup1, Page(s) 5–6

    MeSH term(s) Antibodies/administration & dosage ; Female ; Humans ; Immunoglobulin Light-chain Amyloidosis/diagnostic imaging ; Immunoglobulin Light-chain Amyloidosis/metabolism ; Immunoglobulin Light-chain Amyloidosis/therapy ; Immunotherapy ; Male ; Serum Amyloid P-Component/antagonists & inhibitors ; Serum Amyloid P-Component/metabolism
    Chemical Substances Antibodies ; Serum Amyloid P-Component
    Language English
    Publishing date 2016-12-26
    Publishing country England
    Document type Letter
    ZDB-ID 1205246-2
    ISSN 1744-2818 ; 1350-6129
    ISSN (online) 1744-2818
    ISSN 1350-6129
    DOI 10.1080/13506129.2016.1269735
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4114: Show issues Location:
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  5. Article ; Online: Serum amyloid P component accumulates and persists in neurones following traumatic brain injury.

    Yip, Ping K / Liu, Zhou-Hao / Hasan, Shumaila / Pepys, Mark B / Uff, Christopher E G

    Open biology

    2023  Volume 13, Issue 12, Page(s) 230253

    Abstract: The mechanisms underlying neurodegenerative sequelae of traumatic brain injury (TBI) are poorly understood. The normal plasma protein, serum amyloid P component (SAP), which is normally rigorously excluded from the brain, is directly neurocytotoxic for ... ...

    Abstract The mechanisms underlying neurodegenerative sequelae of traumatic brain injury (TBI) are poorly understood. The normal plasma protein, serum amyloid P component (SAP), which is normally rigorously excluded from the brain, is directly neurocytotoxic for cerebral neurones and also binds to A
    MeSH term(s) Humans ; Aged ; Serum Amyloid P-Component/chemistry ; Serum Amyloid P-Component/metabolism ; Brain Injuries, Traumatic/metabolism ; Brain/metabolism ; Blood Proteins/metabolism ; Dementia/metabolism ; Amyloid beta-Peptides/metabolism
    Chemical Substances Serum Amyloid P-Component ; Blood Proteins ; Amyloid beta-Peptides
    Language English
    Publishing date 2023-12-06
    Publishing country England
    Document type Journal Article
    ZDB-ID 2630944-0
    ISSN 2046-2441 ; 2046-2441
    ISSN (online) 2046-2441
    ISSN 2046-2441
    DOI 10.1098/rsob.230253
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  6. Article: Genetic evidence for serum amyloid P component as a drug target for treatment of neurodegenerative disorders.

    Schmidt, A Floriaan / Finan, Chris / Chopade, Sandesh / Ellmerich, Stephan / Rossor, Martin N / Hingorani, Aroon D / Pepys, Mark B

    medRxiv : the preprint server for health sciences

    2023  

    Abstract: The direct causes of neurodegeneration underlying Alzheimer's disease (AD) and many other dementias, are not known. Here we identify serum amyloid P component (SAP), a constitutive plasma protein normally excluded from the brain, as a potential drug ... ...

    Abstract The direct causes of neurodegeneration underlying Alzheimer's disease (AD) and many other dementias, are not known. Here we identify serum amyloid P component (SAP), a constitutive plasma protein normally excluded from the brain, as a potential drug target. After meta-analysis of three genome-wide association studies, comprising 44,288 participants,
    Language English
    Publishing date 2023-08-16
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.08.15.23293564
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Book ; Conference proceedings: Rheumatoid arthritis

    Pepys, Mark B.

    the role of acute phase proteins ; proceedings of a satellite meeting held at the VIIth EULAR symposium, 23 July 1992, London, United Kingdom

    (British journal of rheumatology ; 32, Suppl. 3)

    1993  

    Institution European League against Rheumatism
    Author's details guest ed.: M. B. Pepys
    Series title British journal of rheumatology ; 32, Suppl. 3
    Collection
    Keywords Arthritis, Rheumatoid / congresses ; Acute-Phase Proteins / congresses ; Biological Markers / congresses
    Size V, 25 S. : graph. Darst.
    Publisher Baillière Tindall
    Publishing place London
    Publishing country Great Britain
    Document type Book ; Conference proceedings
    HBZ-ID HT004551028
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    Zs B 240 -32,Suppl.3- verfügbar in Königswinter Königswinter

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  8. Article ; Online: Invasive candidiasis: new insights presaging new therapeutic approaches?

    Pepys, Mark B

    The Journal of infectious diseases

    2012  Volume 206, Issue 9, Page(s) 1339–1341

    MeSH term(s) Candida albicans/chemistry ; Candidiasis, Invasive/pathology ; Gastrointestinal Diseases/pathology ; Humans ; Plaque, Amyloid/pathology ; Serum Amyloid P-Component/analysis
    Chemical Substances Serum Amyloid P-Component
    Language English
    Publishing date 2012-11
    Publishing country United States
    Document type Comment ; Editorial ; Research Support, Non-U.S. Gov't
    ZDB-ID 3019-3
    ISSN 1537-6613 ; 0022-1899
    ISSN (online) 1537-6613
    ISSN 0022-1899
    DOI 10.1093/infdis/jis521
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    Uh II Zs.50: Show issues Location:
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    Zs.MO 445: Show issues

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  9. Book ; Conference proceedings: Acute phase proteins in the acute phase response

    Pepys, Mark B.

    [proceedings of a 1988 symposium]

    (Argenteuil Symposia)

    1989  

    Author's details M. B. Pepys (ed.)
    Series title Argenteuil Symposia
    Keywords Acute-Phase Proteins / congresses ; Inflammation / congresses ; Akute-Phase-Reaktion ; C-reaktives Protein
    Subject CRP ; Acute phase response ; Postresuscitation Syndrome
    Language English
    Size XIII, 210 S. : Ill., graph. Darst.
    Publisher Springer
    Publishing place London u.a.
    Publishing country Great Britain
    Document type Book ; Conference proceedings
    HBZ-ID HT003501875
    ISBN 3-540-19582-3 ; 0-387-19582-3 ; 978-3-540-19582-5 ; 978-0-387-19582-7
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    1990 A 2580 order for loan Magazin

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  10. Article ; Online: Serum amyloid P component accumulates and persists in neurones following traumatic brain injury

    Ping K. Yip / Zhou-Hao Liu / Shumaila Hasan / Mark B. Pepys / Christopher E. G. Uff

    Open Biology, Vol 13, Iss

    2023  Volume 12

    Abstract: The mechanisms underlying neurodegenerative sequelae of traumatic brain injury (TBI) are poorly understood. The normal plasma protein, serum amyloid P component (SAP), which is normally rigorously excluded from the brain, is directly neurocytotoxic for ... ...

    Abstract The mechanisms underlying neurodegenerative sequelae of traumatic brain injury (TBI) are poorly understood. The normal plasma protein, serum amyloid P component (SAP), which is normally rigorously excluded from the brain, is directly neurocytotoxic for cerebral neurones and also binds to Aβ amyloid fibrils and neurofibrillary tangles, promoting formation and persistence of Aβ fibrils. Increased brain exposure to SAP is common to many risk factors for dementia, including TBI, and dementia at death in the elderly is significantly associated with neocortical SAP content. Here, in 18 of 30 severe TBI cases, we report immunohistochemical staining for SAP in contused brain tissue with blood–brain barrier disruption. The SAP was localized to neurofilaments in a subset of neurones and their processes, particularly damaged axons and cell bodies, and was present regardless of the time after injury. No SAP was detected on astrocytes, microglia, cerebral capillaries or serotoninergic neurones and was absent from undamaged brain. C-reactive protein, the control plasma protein most closely similar to SAP, was only detected within capillary lumina. The appearance of neurocytotoxic SAP in the brain after TBI, and its persistent, selective deposition in cerebral neurones, are consistent with a potential contribution to subsequent neurodegeneration.
    Keywords traumatic brain injury ; serum amyloid P component ; neurodegeneration ; dementia ; Biology (General) ; QH301-705.5
    Subject code 616
    Language English
    Publishing date 2023-12-01T00:00:00Z
    Publisher The Royal Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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