Characterization of the Binding of Serum Amyloid P to Type IV Collagen

Zahedi, Kamyar

doi:10.1074/jbc.271.25.14897

Cited by 36 publications

(33 citation statements)

References 30 publications

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“…In peripheral tissues, SAP is associated with several ECM proteins, such as elastin in the skin and collagen and laminin in the glomerular basement membrane of the kidney (43)(44)(45)(46)(47)(48). The observation that fibrocytes are evident in experimental wound chambers within days of induction suggests that fibrocytes differentiate quickly after wounding (7,8).…”

Section: Discussionmentioning

confidence: 99%

Inhibition of Fibrocyte Differentiation by Serum Amyloid P

Pilling

Buckley

Salmon

et al. 2003

The Journal of Immunology

288

437

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Wound healing and the dysregulated events leading to fibrosis both involve the proliferation and differentiation of fibroblasts and the deposition of extracellular matrix. Whether these fibroblasts are locally derived or from a circulating precursor population is unclear. Fibrocytes are a distinct population of fibroblast-like cells derived from peripheral blood monocytes that enter sites of tissue injury to promote angiogenesis and wound healing. We have found that CD14+ peripheral blood monocytes cultured in the absence of serum or plasma differentiate into fibrocytes within 72 h. We purified the factor in serum and plasma that prevents the rapid appearance of fibrocytes, and identified it as serum amyloid P (SAP). Purified SAP inhibits fibrocyte differentiation at levels similar to those found in plasma, while depleting SAP reduces the ability of plasma to inhibit fibrocyte differentiation. Compared with sera from healthy individuals and patients with rheumatoid arthritis, sera from patients with scleroderma and mixed connective tissue disease, two systemic fibrotic diseases, were less able to inhibit fibrocyte differentiation in vitro and had correspondingly lower serum levels of SAP. These results suggest that low levels of SAP may thus augment pathological processes leading to fibrosis. These data also suggest mechanisms to inhibit fibrosis in chronic inflammatory conditions, or conversely to promote wound healing.

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Section: Discussionmentioning

confidence: 99%

Inhibition of Fibrocyte Differentiation by Serum Amyloid P

Pilling

Buckley

Salmon

et al. 2003

The Journal of Immunology

288

437

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“…All four are secreted glycoproteins widely distributed in most physiological fluids, including plasma and CSF (Barrett 1981;Baltz et al, 1982;Bowman and Kurosky 1982;. Moreover, all bind to a broad range of ligands (Barrett 1981;Capiau et al, 1986;Katnik et al, 1987;Aruga et al, 1993;Katnik et al, 1993;Zahedi 1996;Ashton et al, 1997;Langlois et al, 1997;Zahedi 1997;Kurdowska et al, 2000;Wilson and Easterbrook-Smith 2000;Kimura et al, 2001;Sen and Heegaard 2002) and have been found associated with clinical amyloid deposits in vivo (Table (1)) (Powers et al, 1981;Baltz et al, 1982;Van Gool et al, 1993;McHattie and Edington 1999;Calero et al, 2000). In addition all have been shown to mediate receptormediated endocytosis of ligands (see below).…”

Section: Extracellular Chaperonesmentioning

confidence: 99%

Extracellular Chaperones and Amyloids

Wilson¹,

Yerbury²,

Poon³

2008

Heat Shock Proteins and the Brain: Implications for Neurodegenerative Diseases and Neuroprotection

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The pathology of more than 40 human degenerative diseases is associated with fibrillar proteinaceous deposits called amyloid. Collectively referred to as protein deposition diseases, many of these affect the brain and the central nervous system. In many cases the amyloid deposits are extracellular and are found associated with newly identified abundant extracellular chaperones (ECs). Evidence is discussed which suggests an important regulatory role for ECs in amyloid formation and disposal in vivo. This is emerging as an exciting field. A model is presented in which it is proposed that, under normal conditions, ECs stabilize extracellular misfolded proteins by binding to them, and then guide them to specific receptors for uptake and subsequent degradation. In this scenario, EC receptors are a critical part of a quality control system which protects the brain against dangerously hydrophobic proteins/peptides. However, it also appears possible that in the presence of a high molar excess of misfolded protein, such as might occur during disease, the limited amounts of ECs available may actually exacerabate pathology. Further advances in understanding of the mechanisms that control extracellular protein folding are likely to identify new strategies for effective disease therapies. ABSTRACTThe pathology of more than 40 human degenerative diseases is associated with fibrillar proteinaceous deposits called amyloid. Collectively referred to as protein deposition diseases, many of these affect the brain and the central nervous system. In many cases the amyloid deposits are extracellular and are found associated with newly identified abundant extracellular chaperones (ECs). Evidence is discussed which suggests an important regulatory role for ECs in amyloid formation and disposal in vivo. This is emerging as an exciting field. A model is presented in which it is proposed that, under normal conditions, ECs stabilize extracellular misfolded proteins by binding to them, and then guide them to specific receptors for uptake and subsequent degradation. In this scenario, EC receptors are a critical part of a quality control system which protects the brain against dangerously hydrophobic proteins/peptides. However, it also appears possible that in the presence of a high molar excess of misfolded protein, such as might occur during disease, the limited amounts of ECs available may actually exacebate pathology. Further advances in understanding of the mechanisms that control extracellular protein folding are likely to identify new strategies for effective disease therapies.

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“…Serum amyloid P (SAP: a member of the pentraxin family) is known to bind to a diverse array of ligands (154)(155)(156), however, no clear biological function for this protein has yet been established. It has been reported that SAP has ATP-independent refolding chaperone activity, however, this was achieved using a very high molar excess of SAP and even then the recovery of heat-denatured lactate dehydrogenase activity was only 25% (157).…”

Section: Other Ecsmentioning

confidence: 99%

Extracellular Chaperones and Proteostasis

Wyatt

Yerbury

Ecroyd

et al. 2013

Annu. Rev. Biochem.

157

173

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There is a family of currently untreatable serious human diseases that arise from the inappropriate misfolding and aggregation of extracellular proteins. At present our understanding of mechanisms that operate to maintain proteostasis in extracellular body fluids is limited but has significantly advanced with the discovery of a small but growing family of constitutively secreted extracellular chaperones (ECs). The available evidence strongly suggests that these chaperones act as both sensors and disposal-mediators of misfolded proteins in extracellular fluids, thereby normally protecting us from disease pathologies. It is critically important to further increase our understanding of the mechanisms that operate to effect extracellular proteostasis, as this will be essential knowledge upon which to base the development of effective therapies for some of the world's most debilitating, costly and intractable diseases.

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Characterization of the Binding of Serum Amyloid P to Type IV Collagen

Cited by 36 publications

References 30 publications

Inhibition of Fibrocyte Differentiation by Serum Amyloid P

Inhibition of Fibrocyte Differentiation by Serum Amyloid P

Extracellular Chaperones and Amyloids

Extracellular Chaperones and Proteostasis

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