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A human antibody se...
A human antibody selective for transthyretin amyloid removes cardiac amyloid through phagocytic immune cells
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- Michalon, Aubin (författare)
- Neurimmune, Schlieren, Switzerland
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- Hagenbuch, Andreas (författare)
- Neurimmune, Schlieren, Switzerland
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- Huy, Christian (författare)
- Neurimmune, Schlieren, Switzerland
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- Varela, Evita (författare)
- Neurimmune, Schlieren, Switzerland
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- Combaluzier, Benoit (författare)
- Neurimmune, Schlieren, Switzerland
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- Damy, Thibaud (författare)
- Referral Center for Cardiac Amyloidosis and Department of Cardiology, Henri Mondor University Hospital, Créteil, France
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- Suhr, Ole B. (författare)
- Umeå universitet,Avdelningen för medicin
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- Saraiva, Maria J. (författare)
- i3S - Instituto de Investigação e Inovação em Saúde & IBMC - Instituto de Biologia Molecular e Celular, Porto, Portugal
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- Hock, Christoph (författare)
- Neurimmune, Schlieren, Switzerland; Institute for Regenerative Medicine (IREM), University of Zurich, Zurich, Switzerland
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- Nitsch, Roger M. (författare)
- Neurimmune, Schlieren, Switzerland; Institute for Regenerative Medicine (IREM), University of Zurich, Zurich, Switzerland
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- Grimm, Jan (författare)
- Neurimmune, Schlieren, Switzerland
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(creator_code:org_t)
- 2021-05-25
- 2021
- Engelska.
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Ingår i: Nature Communications. - : Nature Publishing Group. - 2041-1723. ; 12:1
- Relaterad länk:
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https://doi.org/10.1...
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https://umu.diva-por... (primary) (Raw object)
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https://www.nature.c...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Transthyretin amyloid (ATTR) cardiomyopathy is a debilitating disease leading to heart failure and death. It is characterized by the deposition of extracellular ATTR fibrils in the myocardium. Reducing myocardial ATTR load is a therapeutic goal anticipated to translate into restored cardiac function and improved patient survival. For this purpose, we developed the selective anti-ATTR antibody NI301A, a recombinant human monoclonal immunoglobulin G1. NI301A was cloned following comprehensive analyses of memory B cell repertoires derived from healthy elderly subjects. NI301A binds selectively with high affinity to the disease-associated ATTR aggregates of either wild-type or variant ATTR related to sporadic or hereditary disease, respectively. It does not bind physiological transthyretin. NI301A removes ATTR deposits ex vivo from patient-derived myocardium by macrophages, as well as in vivo from mice grafted with patient-derived ATTR fibrils in a dose- and time-dependent fashion. The biological activity of ATTR removal involves antibody-mediated activation of phagocytic immune cells including macrophages. These data support the evaluation of safety and tolerability of NI301A in an ongoing phase 1 clinical trial in patients with ATTR cardiomyopathy.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Klinisk medicin -- Annan klinisk medicin (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Clinical Medicine -- Other Clinical Medicine (hsv//eng)
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Michalon, Aubin
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Hagenbuch, Andre ...
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Huy, Christian
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Varela, Evita
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Combaluzier, Ben ...
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Damy, Thibaud
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visa fler...
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Suhr, Ole B.
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Saraiva, Maria J ...
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Hock, Christoph
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Nitsch, Roger M.
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Grimm, Jan
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visa färre...
- Om ämnet
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- MEDICIN OCH HÄLSOVETENSKAP
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MEDICIN OCH HÄLS ...
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och Klinisk medicin
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och Annan klinisk me ...
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Nature Communica ...
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Umeå universitet