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

@entity1 @entity1472 @entity527 @entity2783 @entity134 @entity329 @entity4742
Female protein (FP) is a pentraxin of @entity329 which is a homologue of two @entity1 pentraxins, C-reaction protein (CRP) and amyloid P component (AP). Functionally, FP has been shown to be similar to CRP, although FP has more homology at the @entity1472 terminus with AP. The present work investigated amyloid in the @entity329 to determine whether FP was involved in a manner analogous to AP. FP was found to be a constituent of @entity329 amyloid. This conclusion was based on the following results: (a) FP was consistently detected in @entity527 by fluorescent microscopy with specific antisera; (b) The amount of FP extractable from hamster livers directly correlated with the presence of amyloid; and (c) 125I-FP injected intravenously into amyloidotic hamsters rapidly left the intravascular compartment and was found subsequently in @entity527 . This unusual alteration of plasma metabolism and amyloid localization of 125I-FP was a characteristic finding in amyloidotic hamsters and was specific for 125I-FP. Therefore, as an amyloid component, FP appears to be functionally similar to @entity1 AP. However, FP synthesis is under sex @entity134 control and the unique sex-limited expression of this pentraxin was associated with an equally novel propensity for deposition of amyloid in female hamsters under normal or experimental conditions. Thus, a high serum level of FP, as found in normal females or @entity4742 -treated males, was associated with enhanced @entity2783 . Although speculative at present, a primary role for serum FP in hamster @entity527 may be experimentally approachable by hormonal manipulation of FP synthesis.
