C-reactive protein in the hemolymph of Achatina fulica: interrelationship with sex steroids and metallothionein

C-reactive protein in Achatina fulica (ACRP) is a normal component of the hemolymph. Its concentration varied from 1mg/ml in the newly hatched male, 3–5 mg/ml in the most active hermaphrodite and 1.5–2.8 mg/ml in the sedentary female showing a direct relationship of the protein with the active phase of the animal. ACRP has a molecular mass of 400 kDa and showed high absorbance in the region of 200–230 nm. It has four subunits with relative molecular masses of 110, 90, 62 and 60 kDa, respectively. Interestingly, rat platelet aggregation in vitro was significantly enhanced by ACRP in presence of 10 μM ADP and 2 mM Ca²⁺ suggesting a probable role of ACRP in the aggregation of amoebocytes during the formation of plug in injured tissue. Like other vertebrate CRPs, ACRP also acts as a scavenger of chromatin fragments as evidenced by its binding to poly- -arginine. Among the sex steroids, 4-androstenedione induces ACRP synthesis in the newly hatched male reaching the level found in the most active hermaphrodite phase (4mg/ml). A very high molar ratio (5) of mercury binding to ACRP confirmed its sequestration property of heavy metals as observed in vertebrates. The level of metallothionein (MT) in the hemolymph gradually increased from the male to the hermaphrodite to the female, a pattern distinctly different from that of the ACRP titer. Since both MT and ACRP can sequester inorganic mercury, the high level of MT compensates functionally for the low titer of ACRP in the sedentary female.