Characterization of an isoelectric focusing variant of SAA1 (ASP-72) in a family of Turkish origin

Kluve‐Beckerman, Barbara; Malle, Ernst; Vitt, Herbert; Pfeiffer, C.; Benson, Merrill D.; Steinmetz, Armin

doi:10.1016/0006-291x(91)92051-k

Cited by 13 publications

(5 citation statements)

References 15 publications

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“…Both positions 52 and 57 are occupied by alanine (A) in SAA1γ [21]. Beach et al [22] described the same SAA1β variant as Parmelee et al [20], but reported aspartic acid (D) at position 72 instead of glycine (G), as was already observed by Kluve-Beckerman et al in a family of Turkish origin [23]. Since the other SAA1 and SAA2 variants all contain glycine (G) at position 72, the SAA1β protein described by Parmelee and co-workers was adopted.…”

Section: Structure Of Human Serum Amyloid a (Saa)mentioning

confidence: 88%

Structure and Expression of Different Serum Amyloid A (SAA) Variants and their Concentration-Dependent Functions During Host Insults

Buck¹,

Gouwy²,

Wang³

et al. 2016

CMC

202

220

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Serum amyloid A (SAA) is, like C-reactive protein (CRP), an acute phase protein and can be used as a diagnostic, prognostic or therapy follow-up marker for many diseases. Increases in serum levels of SAA are triggered by physical insults to the host, including infection, trauma, inflammatory reactions and cancer. The order of magnitude of increase in SAA levels varies considerably, from a 10- to 100-fold during limited inflammatory events to a 1000-fold increase during severe bacterial infections and acute exacerbations of chronic inflammatory diseases. This broad response range is reflected by SAA gene duplications resulting in a cluster encoding several SAA variants and by multiple biological functions of SAA. SAA variants are single-domain proteins with simple structures and few post-translational modifications. SAA1 and SAA2 are inducible by inflammatory cytokines, whereas SAA4 is constitutively produced. We review here the regulated expression of SAA in normal and transformed cells and compare its serum levels in various disease states. At low concentrations (10-100 ng/ml), early in an inflammatory response, SAA induces chemokines or matrix degrading enzymes via Toll-like receptors and functions as an activator and chemoattractant through a G protein-coupled receptor. When an infectious or inflammatory stimulus persists, the liver continues to produce more SAA (> 1000 ng/ml) to become an antimicrobial agent by functioning as a direct opsonin of bacteria or by interference with virus infection of host cells. Thus, SAA regulates innate and adaptive immunity and this information may help to design better drugs to treat specific diseases.

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Section: Structure Of Human Serum Amyloid a (Saa)mentioning

confidence: 88%

Structure and Expression of Different Serum Amyloid A (SAA) Variants and their Concentration-Dependent Functions During Host Insults

Buck¹,

Gouwy²,

Wang³

et al. 2016

CMC

202

220

View full text Add to dashboard Cite

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“…The second group of SAA proteins (SAA4 in humans and SAA3 in mice) is expressed constitutively at plasma concentrations of approximately 55 µg/ml; human SAA4 is synthesised by different organs and tissues and is not an acute phase protein [19]. The physiological functions of SAA were recently reviewed by Uhlar and Whitehead [35,77]; it is not yet known exactly how these functions are associated with the pathogenesis of AA amyloidosis.…”

Section: The Precursor Proteinmentioning

confidence: 98%

Pathology, diagnosis and pathogenesis of AA amyloidosis

2002

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Amyloid is defined as a proteinaceous tissue deposit that shows a typical green birefringence in polarised light after staining with Congo red, the presence of non-branching linear fibrils of indefinite length with an approximate diameter of 10-12 nm and a distinct X-ray diffraction pattern consistent with Pauling's model of a cross-beta fibril. Approximately 45% of generalised amyloidoses are secondary or reactive (AA) amyloidosis. Among the causes of AA amyloidosis are rheumatic diseases, idiopathic diseases, inherited diseases, infectious diseases and malignant tumours. Recent decades have provided significant advances in our understanding of the pathology and pathogenesis of AA amyloidosis. Its pathogenesis is multifactorial involving many variables such as primary structure of the precursor protein, acute phase response, the presence of non-fibril proteins (e.g. amyloid P component, apolipoprotein E, glycosaminoglycans, proteoglycans and basement membrane proteins), receptors, lipid metabolism and proteases. Study of the pathogenesis of AA amyloidosis has provided many insights into the nature of conformational diseases, which may help in the understanding of other members of this particularly heterogeneous group of diseases, such as Alzheimer's disease and transmissible spongiform encephalopathies.

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“…Of particular emphasis is the detection of a cluster of multiple SAA peaks; in addition to the 11.7 kDa peak, a 11.5 kDa (SAA lacking the N-terminal arginine) and a 11.4 kDa peak (SAA lacking the N-terminal arginine-serine residues) have been identified [80]. This is of importance as the corresponding des-arginine forms (11.5 kDa) have been used previously to identify SAA1, SAA2 or other isoelectric focusing SAA variants [10, 81]. Using the SELDI-TOF-MS technique, the 11.7 kDa and 11.5 kDa peaks of SAA have further been identified in serum of RCC patients after rIL-2 treatment [82]; this observation parallels high SAA levels measured in cancer patients following rIL-6 therapy [34, 35]; however, it is indicative that SAA may not necessarily act as a candidate biomarker in RCC [80].…”

Section: Saa and Its Role As A Candidate Tumour-specific Surrogate Bimentioning

confidence: 99%

Serum amyloid A: An acute-phase protein involved in tumour pathogenesis

Malle

Sodin‐Šemrl

Kovacevic

2008

Cell. Mol. Life Sci.

204

181

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The synthesis of acute-phase protein serum amyloid A (SAA) is largely regulated by inflammation- associated cytokines and a high concentration of circulating SAA may represent an ideal marker for acute and chronic inflammatory diseases. However, SAA is also synthesized in extrahepatic tissues, e.g. human carcinoma metastases and cancer cell lines. An increasing body of in vitro data supports the concept of involvement of SAA in carcinogenesis and neoplastic diseases. Accumulating evidence suggests that SAA might be included in a group of biomarkers to detect a pattern of physiological events that reflect the growth of malignancy and host response. This review is meant to provide a broad overview of the many ways that SAA could contribute to tumour development, and accelerate tumour progression and metastasis, and to gain a better understanding of this acute-phase reactant as a possible link between chronic inflammation and neoplasia.

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Characterization of an isoelectric focusing variant of SAA1 (ASP-72) in a family of Turkish origin

Cited by 13 publications

References 15 publications

Structure and Expression of Different Serum Amyloid A (SAA) Variants and their Concentration-Dependent Functions During Host Insults

Structure and Expression of Different Serum Amyloid A (SAA) Variants and their Concentration-Dependent Functions During Host Insults

Pathology, diagnosis and pathogenesis of AA amyloidosis

Serum amyloid A: An acute-phase protein involved in tumour pathogenesis

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