alpha-chymotrypsin and Androgen-Insensitivity-Syndrome

Trypsin-like and chymotrypsin-like esteroprotease isozymes of the mouse submandibular gland were separated by isoelectric focusing. In normal female mice the following pI-isozyme activities were found; pI-4.6, -5.6 (shoulder), -5.8, -7.1, and -9.9, hydrolytic activities for benzoylarginine ethylester (BAEE) (trypsin-like enzymes), and pI-4.7 and -10.3 hydrolytic activities for acetyltyrosine ethylester (ATEE) (chymotrypsin-like enzymes). In mice with testicular feminization (Tfm mice), only pI4.6 hydrolytic activity for BAEE was found; no ATEE hydrolytic activity was detected. In normal female mice, both 5 alpha-dihydrotestosterone (5 alpha-DHT) and tri-iodo-L-thyronine (T3) significantly increased all these isozymes except the pI-4.6 hydrolytic activity for BAEE. In Tfm mice, T3 also increased all these isozymes except the pI-4.6 hydrolytic activity for BAEE, but 5 alpha-DHT had no effect on any enzymes. These results suggest that the pI-4.6 hydrolytic activity for BAEE is non-inducible by the two hormones. Androgen does not seem to be involved in the inductions of these esteroproteases by T3.

Topics: Androgen-Insensitivity Syndrome; Androgens; Animals; Arginine; Chymotrypsin; Endopeptidases; Enzyme Induction; Female; Isoenzymes; Male; Mice; Submandibular Gland; Triiodothyronine; Trypsin; Tyrosine