Evidence that C4b-binding protein (proline-rich protein) is synthesized by hepatocytes.
C4b-binding protein (C4bp), a glycoprotein involved in regulating the classical pathway of the complement system, binds the activated form of C4b and accelerates the decay rate of the C4b, C2a complex. Recently, sequence analysis of the cDNA for proline-rich protein (PRP) demonstrated that PRP is identical with C4bp. We measured the concentration of C4bp in serum by single radial immunodiffusion in patients with various liver diseases. Concentration of C4bp was significantly lower in hepatic cirrhosis (P = 0.001) and higher in fatty liver (P = 0.0002) than the control values, after adjusting for age, sex, and concentration of total cholesterol, triglyceride, and C-reactive protein. Significant positive correlations were observed between the concentration of C4bp in serum and total protein, albumin, cholinesterase level, and lecithin-cholesterol acyltransferase activity. Immunohistochemical analysis of human liver with specific antiserum to human C4bp demonstrated reaction endproducts in the hepatocytes around the central veins. These observations provide evidence that C4bp is synthesized by hepatocytes.
Kusada-Funakoshi
M
M
Department of Internal Medicine, Fukuoka University School of Medicine, Japan.
Sasaki
J
J
Takada
Y
Y
Soji
T
T
Arakawa
K
K
D000818:Animals; D002352:Carrier Proteins / Q000096:biosynthesis*; D015935:Complement C4b / Q000378:metabolism*; D003169:Complement Inactivator Proteins; D006023:Glycoproteins; D006801:Humans; D066298:In Vitro Techniques; D008099:Liver / Q000378:metabolism*; D011817:Rabbits
D002352:Carrier Proteins; D003169:Complement Inactivator Proteins; D006023:Glycoproteins; D015935:Complement C4b