Hamster female protein, a sex-limited pentraxin, is a constituent of Syrian hamster amyloid.

Coe, John E.; Ross, Mary Jane

doi:10.1172/jci111978

Cited by 37 publications

(45 citation statements)

References 24 publications

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“…The ¢rst hint that deposition of SAP in amyloid might be of pathogenetic signi¢cance, rather than just an epiphenomenon, came when we observed that circulating SAP values correlated much more closely with experimental murine AA amyloidosis deposition than did the SAA values (Baltz et al 1980). This ¢nding was subsequently replicated even more dramatically in the Syrian hamster, in which expression of SAP is under female sex hormone control and females with very high SAP values get AA amyloidosis much more readily than males with low SAP values, despite equal production of SAA, the actual ¢bril precursor protein (Coe & Ross 1985Snel et al 1989). …”

Section: (C) Inhibition Of ¢Brillogenesismentioning

confidence: 91%

Pathogenesis, diagnosis and treatment of systemic amyloidosis

Pepys

2001

Phil. Trans. R. Soc. Lond. B

203

156

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Amyloidosis is a disorder of protein folding in which normally soluble proteins are deposited as abnormal, insoluble ¢brils that disrupt tissue structure and cause disease. Although about 20 di¡erent unrelated proteins can form amyloid ¢brils in vivo, all such ¢brils share a common cross-b core structure. Some natural wild-type proteins are inherently amyloidogenic, form ¢brils and cause amyloidosis in old age or if present for long periods at abnormally high concentration. Other amyloidogenic proteins are acquired or inherited variants, containing amino-acid substitutions that render them unstable so that they populate partly unfolded states under physiological conditions, and these intermediates then aggregate in the stable amyloid fold. In addition to the ¢brils, amyloid deposits always contain the non-¢brillar pentraxin plasma protein, serum amyloid P component (SAP), because it undergoes speci¢c calcium-dependent binding to amyloid ¢brils. SAP contributes to amyloidogenesis, probably by stabilizing amyloid ¢brils and retarding their clearance. Radiolabelled SAP is an extremely useful, safe, speci¢c, non-invasive, quantitative tracer for scintigraphic imaging of systemic amyloid deposits. Its use has demonstrated that elimination of the supply of amyloid ¢bril precursor proteins leads to regression of amyloid deposits with clinical bene¢t. Current treatment of amyloidosis comprises careful maintenance of impaired organ function, replacement of end-stage organ failure by dialysis or transplantation, and vigorous e¡orts to control underlying conditions responsible for production of ¢bril precursors. New approaches under development include drugs for stabilization of the native fold of precursor proteins, inhibition of ¢brillogenesis, reversion of the amyloid to the native fold, and dissociation of SAP to accelerate amyloid ¢bril clearance in vivo.

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Section: (C) Inhibition Of ¢Brillogenesismentioning

confidence: 91%

Pathogenesis, diagnosis and treatment of systemic amyloidosis

Pepys

2001

Phil. Trans. R. Soc. Lond. B

203

156

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“…On the other hand, human SAP specifically binds to the 4,6 cyclic pyruvate acetal of [3-D-galactose (MO3DG) [16] and also to all types of amyloid fibrils [17], which are not recognized by human CRP. The major pentraxin in Syrian hamsters, formerly known as female protein [18] (here designated HSAP), is the hamster counterpart of human SAP, in that it binds to hamster amyloid [19,20], but it shares with human CRP the capacity to bind to PC as well as PE [18,21].…”

Section: Introductionmentioning

confidence: 99%

Comparative analyses of pentraxins: implications for protomer assembly and ligand binding

et al. 1994

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Background: Pentraxins are a family of plasma proteins characterized by their pentameric assembly and calciumdependent ligand binding. The recent determination of the crystal structure for a member of this family, human serum amyloid P component (SAP), provides a basis for the comparative analysis of the pentraxin family. Results: We have compared the sequences, tertiary structures and quaternary arrangements of SAP with human C-reactive protein (CRP), Syrian hamster SAP (HSAP) and Limulus polyphemus CRP (LIM). These proteins can adopt a 3 -jelly roll topology and a hydrophobic core similar to that seen in SAP. Only minor differences are observed in the positions of residues involved in coordinating calcium ions. Conclusions: Calcium-mediated ligand binding by CRP, HSAP and LIM is similar to that defined by the crystal structure of SAP, but sequence differences in the hydrophobic pocket explain the differential ligand specificities exhibited by the homologous proteins. Differences elsewhere, including insertions and deletions, account for the different (hexameric) quaternary structure of LIM.

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“…Amyloid is a common spontaneous disease in the Syrian hamster and can be found in the female hamster at an earlier age than in the male hamsters [11,12]. We have previously reported that, in the hamster model, amyloidosis may participate in the pathogenesis of nephropathy developed after infection with either S. mansoni or S. hematobium [3,4].…”

Section: Discussionmentioning

confidence: 99%

“…However, FP is an unusual homology because its expression is sex limited and it is a prominent serum protein in females (1-2 mg/ml), while normal males have low serum levels (0.01-0.02 mg/ml), [10]. FP was found to be a constituent of Syrian hamster amyloid as it is detected in amyloid deposits by fluorescent microscopy with specific antisera and the amount of FP extracted from hamster livers directly correlated with the presence of amyloid [11].…”

Section: Introductionmentioning

confidence: 99%

Schistosoma-induced amyloidosis in hamsters is gender-dependent

et al. 2007

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From this study, we conclude that, in hamster model, Schistosoma-induced amyloidosis is enhanced in females than male hamsters. This may be due to the high serum level of FP that is normally detected in females. As an experimental model for schistosomal nephropathy, we recommend to use male hamsters instead of females to minimize the effect of amyloid deposits, which may mask other pathological changes associated with schistosomal infection.

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Hamster female protein, a sex-limited pentraxin, is a constituent of Syrian hamster amyloid.

Abstract: Female protein (FP) is a pentraxin of Syrian hamster which is a homologue of two human pentraxins, C-reaction protein (CRP) and amyloid P component (AP

Cited by 37 publications

References 24 publications

Pathogenesis, diagnosis and treatment of systemic amyloidosis

Pathogenesis, diagnosis and treatment of systemic amyloidosis

Comparative analyses of pentraxins: implications for protomer assembly and ligand binding

Schistosoma-induced amyloidosis in hamsters is gender-dependent

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