Amyloid A Amyloidosis

Gaffney, Patricia M.

doi:10.1177/0300985816677150

Cited by 6 publications

(10 citation statements)

References 62 publications

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“…AA amyloidosis is a common form of systemic amyloid disease, characterized by an accumulation of misfolded protein, reported in both human and veterinary medicine [ 1 ]. AA amyloid is derived from the positive acute-phase protein Serum Amyloid A (SAA), an apolipoprotein of high-density lipoprotein (HDL) [ 2 ].…”

Section: Introductionmentioning

confidence: 99%

Revisiting misfolding propensity of serum amyloid A1: Special focus on the signal peptide region

Haines

Ramirez

Moore

et al. 2022

Biochemistry and Biophysics Reports

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Section: Introductionmentioning

confidence: 99%

Revisiting misfolding propensity of serum amyloid A1: Special focus on the signal peptide region

Haines

Ramirez

Moore

et al. 2022

Biochemistry and Biophysics Reports

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“…AA amyloidosis used to be the major form of human amyloid disease and a major cause of death in tuberculosis patients [ 3 •], but with improved control of infection and inflammation, this disease became relatively rare. In animals (mammals and birds), AA amyloidosis remains the major form of amyloid disease [ 56 ] that can be transmitted in a prion-like manner by a seeding mechanism [ 55 , 56 ]. No animal-to-human or human-to-human transmission has been reported to date.…”

Section: Saa Misfolding In Aa Amyloidosis and Its Key Effectorsmentioning

confidence: 99%

Structural Basis for Vital Function and Malfunction of Serum Amyloid A: an Acute-Phase Protein that Wears Hydrophobicity on Its Sleeve

Gursky

2020

Curr Atheroscler Rep

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Purpose of Review This review addresses normal and pathologic functions of serum amyloid A (SAA), an enigmatic biomarker of inflammation and protein precursor of AA amyloidosis, a life-threatening complication of chronic inflammation. SAA is a small, highly evolutionarily conserved acute-phase protein whose plasma levels increase up to one thousand-fold in inflammation, infection, or after trauma. The advantage of this dramatic but transient increase is unclear, and the complex role of SAA in immune response is intensely investigated. This review summarizes recent advances in our understanding of the structure-function relationship of this intrinsically disordered protein, outlines its newly emerging beneficial roles in lipid transport and inflammation control, and discusses factors that critically influence its misfolding in AA amyloidosis. Recent Findings High-resolution structures of lipid-free SAA in crystals and fibrils have been determined by x-ray crystallography and electron cryo-microscopy. Low-resolution structural studies of SAA-lipid complexes, together with biochemical, cell-based, animal model, genetic, and clinical studies, have provided surprising new insights into a wide range of SAA functions. An emerging vital role of SAA is lipid encapsulation to remove cell membrane debris from sites of injury. The structural basis for this role has been proposed. The lysosomal origin of AA amyloidosis has solidified, and its molecular and cellular mechanisms have emerged. Summary Recent studies have revealed molecular underpinnings for understanding complex functions of this Cambrian protein in lipid transport, immune response, and amyloid formation. These findings help guide the search for much-needed targeted therapies to block the protein deposition in AA amyloidosis.

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“…Amyloidosis refers to a collection of debilitating proteopathies in which misfolded amyloid fibrils accumulate and deposit in extracellular spaces of organs and tissues [4]. There are about 10 types of amyloid fibril proteins recognized in animals to date, each having a distinct precursor protein [15].…”

mentioning

confidence: 99%

“…Deposition can either be systemic or localized, and out of the 6 reported systemic types in animals, the predominant form is amyloid A (AA) amyloidosis [15]. With AA amyloidosis, an increase in the circulating acute phase protein serum amyloid A (SAA) level triggers the accumulation and subsequent deposition of AA in tissues, usually following chronic inflammation [4]. The disease has been diagnosed occasionally in a variety of species, both domestic and wild [5, 7, 9, 18].…”

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confidence: 99%

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Surveillance of amyloidosis in stranded and bycaught cetaceans off Hokkaido, Japan

Nakagun

Watanabe

Matsuishi

et al. 2019

The Journal of Veterinary Medical Science

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Systemic amyloidosis is rarely reported among cetaceans, and a surveillance dedicated for its occurrence across a certain geographic location has not been reported. Between 2013 and 2018, comprehensive gross and histopathologic examinations were conducted on 54 animals comprising 11 species of stranded and bycaught cetaceans in Hokkaido, Japan. Systemic amyloidosis was diagnosed in 2 out of 3 Stejneger’s beaked whales ( Mesoplodon stejnegeri ), through Congo red staining and immunohistochemistry for amyloid A. The kidney and gastrointestinal tract had the largest amounts of amyloid deposits, representing a previously undescribed organ distribution in the species. The current study demonstrates the possibility of Stejneger’s beaked whales being prone to the development of systemic amyloidosis, and highlights the need for further investigations.

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Amyloid A Amyloidosis

Cited by 6 publications

References 62 publications

Revisiting misfolding propensity of serum amyloid A1: Special focus on the signal peptide region

Revisiting misfolding propensity of serum amyloid A1: Special focus on the signal peptide region

Structural Basis for Vital Function and Malfunction of Serum Amyloid A: an Acute-Phase Protein that Wears Hydrophobicity on Its Sleeve

Surveillance of amyloidosis in stranded and bycaught cetaceans off Hokkaido, Japan

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