Search: onr:"swepub:oai:DiVA.org:umu-184199" >
A human antibody se...
A human antibody selective for transthyretin amyloid removes cardiac amyloid through phagocytic immune cells
-
- Michalon, Aubin (author)
- Neurimmune, Schlieren, Switzerland
-
- Hagenbuch, Andreas (author)
- Neurimmune, Schlieren, Switzerland
-
- Huy, Christian (author)
- Neurimmune, Schlieren, Switzerland
-
show more...
-
- Varela, Evita (author)
- Neurimmune, Schlieren, Switzerland
-
- Combaluzier, Benoit (author)
- Neurimmune, Schlieren, Switzerland
-
- Damy, Thibaud (author)
- Referral Center for Cardiac Amyloidosis and Department of Cardiology, Henri Mondor University Hospital, Créteil, France
-
- Suhr, Ole B. (author)
- Umeå universitet,Avdelningen för medicin
-
- Saraiva, Maria J. (author)
- i3S - Instituto de Investigação e Inovação em Saúde & IBMC - Instituto de Biologia Molecular e Celular, Porto, Portugal
-
- Hock, Christoph (author)
- Neurimmune, Schlieren, Switzerland; Institute for Regenerative Medicine (IREM), University of Zurich, Zurich, Switzerland
-
- Nitsch, Roger M. (author)
- Neurimmune, Schlieren, Switzerland; Institute for Regenerative Medicine (IREM), University of Zurich, Zurich, Switzerland
-
- Grimm, Jan (author)
- Neurimmune, Schlieren, Switzerland
-
show less...
-
(creator_code:org_t)
- 2021-05-25
- 2021
- English.
-
In: Nature Communications. - : Nature Publishing Group. - 2041-1723. ; 12:1
- Related links:
-
https://doi.org/10.1...
-
show more...
-
https://umu.diva-por... (primary) (Raw object)
-
https://www.nature.c...
-
https://urn.kb.se/re...
-
https://doi.org/10.1...
-
show less...
Abstract
Subject headings
Close
- 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.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Klinisk medicin -- Annan klinisk medicin (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Clinical Medicine -- Other Clinical Medicine (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
To the university's database
- By the author/editor
-
Michalon, Aubin
-
Hagenbuch, Andre ...
-
Huy, Christian
-
Varela, Evita
-
Combaluzier, Ben ...
-
Damy, Thibaud
-
show more...
-
Suhr, Ole B.
-
Saraiva, Maria J ...
-
Hock, Christoph
-
Nitsch, Roger M.
-
Grimm, Jan
-
show less...
- About the subject
-
- MEDICAL AND HEALTH SCIENCES
-
MEDICAL AND HEAL ...
-
and Clinical Medicin ...
-
and Other Clinical M ...
- Articles in the publication
-
Nature Communica ...
- By the university
-
Umeå University