Is there a direct correlation between the activities of various lysosomal enzymes and prolactin secretion in the rat anterior pituitary?
The degree of endocrine activity by rat pituitary lactotrophs was manipulated and the lysosomal involvement in the release and intracellular degradation of PRL was monitored by concomitant assays of acid phosphatase, beta-glucuronidase, dipeptidyl peptidases I and II, and nonspecific esterases in the anterior lobe. The in vitro release of PRL by cell cultures was inhibited by 0.5 or 1.5 microM bromocriptine during 24 or 72 h of incubation and by 0.75 microM for 4 h. Long term treatment caused a 40% reduction in the total PRL content of cells and media; however, after 4 h of bromocriptine treatment, no reduction in PRL content was found. TRH (10 ng/ml) in medium for 4 h increased PRL release, whereas it produced intracellular hormone depletion. In vitro treatment of anterior lobes of diestrous rats with 1 microM dopamine decreased PRL release by 50%. No changes in lysosomal enzyme activities were observed after the inhibition of release or stimulation of the in vitro secretion of PRL. Haloperidol (2.5 mg/kg BW) caused a 90% increase in serum PRL concentrations in diestrous rats 1 h after sc injection. alpha-Methyl-p-tyrosine (200 mg/kg BW, ip) stimulated in vivo PRL secretion, monitored 1, 4, and 24 h after drug administration. The administration of 100 micrograms/rat bromocriptine for 3 consecutive days, a single dose of 100 micrograms/rat polyestradiol phosphate, and their combination resulted in the expected changes in PRL production in female rats. These in vivo treatments failed to alter lysosomal enzyme activities in the anterior pituitary. These findings suggest that the release, intracellular accumulation, or depletion of PRL occurred without concomitant changes in lysosomal enzyme activity in the anterior pituitary. We suggest that the system of lysosome-dependent hormone degradation may involve more specific enzymes than those monitored to date.
D000135:Acid Phosphatase / Q000032:analysis; D000818:Animals; D002403:Cathepsins / Q000032:analysis; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000032:analysis; D004950:Esterases / Q000032:analysis; D005260:Female; D005966:Glucuronidase / Q000032:analysis; D013006:Growth Hormone / Q000378:metabolism; D007986:Luteinizing Hormone / Q000378:metabolism; D008247:Lysosomes / Q000201:enzymology*; D010903:Pituitary Gland, Anterior / Q000201:enzymology / Q000378:metabolism*; D011388:Prolactin / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D011388:Prolactin; D007986:Luteinizing Hormone; D013006:Growth Hormone; D004950:Esterases; D000135:Acid Phosphatase; D005966:Glucuronidase; D002403:Cathepsins; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases