Serum Amyloid P Component Does Not Circulate in Complex with C4‐Binding Protein, Fibronectin or Any Other Major Protein Ligand

Sen, Jette W.; Heegaard, Niels H. H.

doi:10.1046/j.1365-3083.2002.01109.x

Cited by 6 publications

(6 citation statements)

References 49 publications

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“… 64 Serum amyloid P protein is involved in the innate immune system and in clearing cellular debris but also contributes to the progression of neurodegeneration through its interaction with amyloid fibers. 44 , 95 HRG, HMWK, and serum amyloid P protein can all bind to polyanions such as GAGs but also pathogens, anionic phospholipids (such as those exposed by dying cells), and DNA. 94 For certain pathogens, this interaction can destabilize the membrane, leading to cell death or can reduce their pathogenicity through incorporation of the organisms inside fibrin clots.…”

Section: Gag Neutralization During Inflammationmentioning

confidence: 99%

Glycosaminoglycan Neutralization in Coagulation Control

Sobczak

Pitt

Stewart

2018

ATVB

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The glycosaminoglycans (GAGs) heparan sulfate, dermatan sulfate, and heparin are important anticoagulants that inhibit clot formation through interactions with antithrombin and heparin cofactor II. Unfractionated heparin, low-molecular-weight heparin, and heparin-derived drugs are often the main treatments used clinically to handle coagulatory disorders. A wide range of proteins have been reported to bind and neutralize these GAGs to promote clot formation. Such neutralizing proteins are involved in a variety of other physiological processes, including inflammation, transport, and signaling. It is clear that these interactions are important for the control of normal coagulation and influence the efficacy of heparin and heparin-based therapeutics. In addition to neutralization, the anticoagulant activities of GAGs may also be regulated through reduced synthesis or by degradation. In this review, we describe GAG neutralization, the proteins involved, and the molecular processes that contribute to the regulation of anticoagulant GAG activity.

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Section: Gag Neutralization During Inflammationmentioning

confidence: 99%

Glycosaminoglycan Neutralization in Coagulation Control

Sobczak

Pitt

Stewart

2018

ATVB

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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 binds to FcγRI, FcγRIIa, and FcγRIIIb and functions as an opsonin with both neutrophils and macrophages 16, 17. It also binds to C4b‐binding protein and fibronectin,18 although this binding does not occur unless one of the proteins is immobilized on a surface 19. It was previously shown that serum amyloid P binds to polystyrene in a calcium‐dependent manner9; however, the interaction of serum amyloid P with biomedical materials has not been reported.…”

Section: Introductionmentioning

confidence: 99%

Proteomic analysis of protein adsorption: Serum amyloid P adsorbs to materials and promotes leukocyte adhesion

Kim

Scott²,

Elbert³

2005

J Biomedical Materials Res

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Serum and plasma protein adsorption on materials was analyzed using gel electrophoresis and ion trap mass spectrometry. Following incubation of polypropylene, polyethylene terephthalate (PET), or polydimethylsiloxane (PDMS) with 5% serum for longer than 4 h, we found unexpectedly high amounts of the pentraxin serum amyloid P. It was previously shown that serum amyloid P is constitutively expressed in humans, functions as an opsonin, and interacts with the Fcgamma receptors on leukocytes. We demonstrate that serum amyloid P adsorbed to tissue culture polystyrene, PDMS, and PET promotes the adhesion of granulocytes and monocytes in the presence of calcium. The methods developed for these studies may be useful for the large-scale study of protein adsorption and do not rely on radiolabeling or the availability of antibodies.

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Serum Amyloid P Component Does Not Circulate in Complex with C4‐Binding Protein, Fibronectin or Any Other Major Protein Ligand

Cited by 6 publications

References 49 publications

Glycosaminoglycan Neutralization in Coagulation Control

Glycosaminoglycan Neutralization in Coagulation Control

Extracellular Chaperones and Amyloids

Proteomic analysis of protein adsorption: Serum amyloid P adsorbs to materials and promotes leukocyte adhesion

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