Synthesis of α1-acid glycoprotein by the human prostate

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Abstract
In order better to define the extent of protein synthesis capacity of the human prostate, we have studied the translation of selected serum proteins using isolated poly(A)+ RNA preparations and the rabbit reticulocyte lysate system. The translation of α1‐acid glycoprotein could be conclusively demonstrated but there was no apparent translation of albumin and plasmatic transferrin. Labeled α1‐acid glycoprotein was identified by specific immunoprecipitation with a commercial anti α1‐acid glycoprotein antiserum and correct processing by canine pancreatic microsomal membranes. Furthermore, we have shown by the immunoperoxidase technique that α1‐acid glycoprotein was indeed localized mainly in prostatic epithelial cells in 2 out of 2 patients with benign prostatic hypertrophy and in 3 out of 11 patients with prostatic adenocarcinoma. The significance of the synthesis and secretion of α1‐acid glycoprotein by prostatic cell themselves is presently unknown. However, we think that it could represent an interesting subject to explore further in relation with prostatic inflammation.