Pathological review of cardiac amyloidosis using autopsy cases in a single Japanese institution

Tateishi, Yuki; Yamada, Yuichi; Katsuki, Masashi; Nagata, Takuya; Yamamoto, Hidetaka; Kohashi, Kenichi; Koga, Yutaka; Hashisako, Mikiko; Kiyozawa, Daisuke; Mori, Taro; Kuboyama, Yusuke; Kakinokizono, Ayumi; Miyazaki, Yoshiko; Yamaguchi, Aina; Tsutsui, Hiroyuki; Ninomiya, Toshiharu; Naiki, Hironobu; Oda, Yoshinao

doi:10.1016/j.prp.2021.153635

Cited by 6 publications

(4 citation statements)

References 21 publications

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“…As a secondary consequence of this chronic inflammation an amyloid fibril seed forms by continuous SAA1 overexpression and proteolytic processing thereof, with can progress to AA amyloidosis. AA amyloidosis predominantly affects the kidney and can progress to a systemic amyloidosis in several organs including the heart [ 37 ].…”

Section: The Amyloid Connection – Causation or Just Correlation?mentioning

confidence: 99%

Viruses and amyloids - a vicious liaison

Hammarström

Nyström

2023

Prion

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The crosstalk between viral infections, amyloid formation and neurodegeneration has been discussed with varying intensity since the last century. Several viral proteins are known to be amyloidogenic. Post-acute sequalae (PAS) of viral infections is known for several viruses. SARS-CoV-2 and COVID-19 implicate connections between amyloid formation and severe outcomes in the acute infection, PAS and neurodegenerative diseases. Is the amyloid connection causation or just correlation? In this review we highlight several aspects where amyloids and viruses meet. The evolutionary driving forces that dictate protein amyloid formation propensity are different for viruses compared to prokaryotes and eukaryotes, while posttranslational endoproteolysis appears to be a common mechanism leading up to amyloid formation for both viral and human proteins. Not only do human and viral proteins form amyloid irrespective of each other but there are also several examples of co-operativity between amyloids, viruses and the inter-, and intra-host spread of the respective entity. Abnormal blood clotting in severe and long COVID and as a side effect in some vaccine recipients has been connected to amyloid formation of both the human fibrin and the viral Spike-protein. We conclude that there are many intersects between viruses and amyloids and, consequently, amyloid and virus research need to join forces here. We emphasize the need to accelerate development and implementation in clinical practice of antiviral drugs to preclude PAS and downstream neurological damage. There is also an ample need for retake on suitable antigen targets for the further development of next generation of vaccines against the current and coming pandemics.

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Section: The Amyloid Connection – Causation or Just Correlation?mentioning

confidence: 99%

Viruses and amyloids - a vicious liaison

Hammarström

Nyström

2023

Prion

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“…Amyloid in these anatomic sites may represent subclinical deposits or those with yet unknown clinical sequelae. Recent autopsy studies do indicate that amyloid is often widespread throughout the body, consistent with 124 I-p5+14 imaging [48][49][50].…”

Section: Discussionmentioning

confidence: 76%

Clinical Confirmation of Pan-Amyloid Reactivity of Radioiodinated Peptide 124I-p5+14 (AT-01) in Patients with Diverse Types of Systemic Amyloidosis Demonstrated by PET/CT Imaging

et al. 2023

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There are at least 20 distinct types of systemic amyloidosis, all of which result in the organ-compromising accumulation of extracellular amyloid deposits. Amyloidosis is challenging to diagnose due to the heterogeneity of the clinical presentation, yet early detection is critical for favorable patient outcomes. The ability to non-invasively and quantitatively detect amyloid throughout the body, even in at-risk populations, before clinical manifestation would be invaluable. To this end, a pan-amyloid-reactive peptide, p5+14, has been developed that is capable of binding all types of amyloid. Herein, we demonstrate the ex vivo pan-amyloid reactivity of p5+14 by using peptide histochemistry on animal and human tissue sections containing various types of amyloid. Furthermore, we present clinical evidence of pan-amyloid binding using iodine-124-labeled p5+14 in a cohort of patients with eight (n = 8) different types of systemic amyloidosis. These patients underwent PET/CT imaging as part of the first-in-human Phase 1/2 clinical trial evaluating this radiotracer (NCT03678259). The uptake of 124I-p5+14 was observed in abdominothoracic organs in patients with all types of amyloidosis evaluated and was consistent with the disease distribution described in the medical record and literature reports. On the other hand, the distribution in healthy subjects was consistent with radiotracer catabolism and clearance. The early and accurate diagnosis of amyloidosis remains challenging. These data support the utility of 124I-p5+14 for the diagnosis of varied types of systemic amyloidosis by PET/CT imaging.

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“…7,8 In 2018, the Group for Surveys and Research of Amyloidosis in Japan (GSRA-J) started a nation-wide pathology consultation of amyloidosis, 1 and amyloid transthyretin (ATTR) was found to be the most common subtype of systemic amyloidosis in Japan. 9 Tateishi et al 10 reviewed autopsy cases in a single Japanese institution (Kyushu University) from 1990 to 2020 and found that ATTR is the most common subtype of cardiac amyloidosis, followed by AA.…”

Section: Introductionmentioning

confidence: 99%

Epidemiological study of the subtype frequency of systemic amyloidosis listed in the Annual of the Pathological Autopsy Cases in Japan

Yamaguchi,

Tasaki,

Ueda

et al. 2023

Pathology International

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Clinical presentation of systemic amyloidosis differs among subtypes, and accurate subtype classification is important for choosing the treatment. Amyloid transthyretin (ATTR) amyloidosis was the predominant among the recently consulted amyloidosis cases in Japan. To reveal the latest subtype frequency of systemic amyloidosis among autopsy cases in Japan. We analyzed systemic amyloidosis cases autopsied from January 2017 to December 2018, that were listed in the Annuals of the Pathological Autopsy Cases in Japan, Volumes 60 and 61. When the subtype was unclear, we performed a questionnaire survey, immunohistochemistry with in‐house rabbit polyclonal anti‐κ116–133, anti‐λ118–134, and anti‐transthyretin115–124 antibodies, and proteomic analysis. Out of 481 systemic amyloidosis cases listed in the Annuals, 411 cases were available for analysis (85.4%). We classified 399 of these systemic amyloidosis cases. ATTR was the most common subtype (44.4%, n = 177), followed by amyloid immunoglobulin light chain (AL) (38.8%, n = 155). Amyloid A and amyloid β2‐microglobulin were 9.3% (n = 37) and 6.0% (n = 24), respectively. Double deposition of amyloid was identified in 1.6% (n = 6). In 168 cases (42.1%), systemic amyloidosis was the main cause of death. Of these cases, AL was the most common subtype (47.6%, n = 80), followed by ATTR (41.1%, n = 69). ATTR is the most predominant subtype among the current autopsy cases in Japan.

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Pathological review of cardiac amyloidosis using autopsy cases in a single Japanese institution

Cited by 6 publications

References 21 publications

Viruses and amyloids - a vicious liaison

Viruses and amyloids - a vicious liaison

Clinical Confirmation of Pan-Amyloid Reactivity of Radioiodinated Peptide 124I-p5+14 (AT-01) in Patients with Diverse Types of Systemic Amyloidosis Demonstrated by PET/CT Imaging

Epidemiological study of the subtype frequency of systemic amyloidosis listed in the Annual of the Pathological Autopsy Cases in Japan

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