Hamster Female Protein. A New Pentraxin Structurally and Functionally Similar to C-reactive Protein and Amyloid P Component

Overview

Journal J Exp Med

Specialties Allergy & Immunology
General Medicine

Date 1981 Apr 1

PMID 6166709

Citations 18

Authors

J E COE

S S Margossian

H S Slayter

J A Sogn

Affiliations

Soon will be listed here.

Abstract

Female protein (FP), a serum protein present in normal female hamsters was found to be similar to acute-phase reactant, C-reactive protein (CRP) and serum amyloid P component (SAP) in the following ways: (a) hamster FP complexed with phosphorylcholine (PC) in a Ca++-dependent fashion as shown by its isolation from serum by affinity chromatography with PC-Sepharose and selective elution with free PC or EDTA; (b) electron microscopy of FP indicated a pentameric structure similar in size and appearance to other pentraxins; (c) the parent molecule of FP (150,000 mol wt) was composed of five noncovalantly assembled subunits of 30,000 mol wt; and (d) the amino acid analysis and terminal NH2 sequence of FP clearly showed homology with SAP-CRP. Although FP evolved from an ancestral gene common to SAP and CRP, and shares functional, morphological and structural properties with these acute-phase proteins, the biological homology of FP appears quite diverse as this protein is a prominent serum constituent (1-2 mg/ml) of normal female hamsters and under hormonal control (testosterone suppression) in males.

Citing Articles

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