Intracellular degradation of newly synthesized casein in perfused rat mammary gland.
Degradation of newly synthesized casein in rat mammary gland perfused in situ was measured by a pulse-chase method using [3H]proline. Casein degradation during secretion was observed in the absence of prolactin, but not with prolactin present. Partial inhibition by chloroquine showed that hormone-dependent degradation occurred intracellularly by a lysosomal mechanism. The study indicates that this post-translational mechanism is a physiological regulator of net casein secretion.
Wilde
C J
CJ
Hannah Research Institute, Ayr.
Kerr
M A
MA
Calvert
D T
DT
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002364:Caseins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002738:Chloroquine / Q000494:pharmacology; D005260:Female; D007425:Intracellular Membranes / Q000378:metabolism; D008321:Mammary Glands, Animal / Q000378:metabolism*; D010477:Perfusion; D011388:Prolactin / Q000502:physiology*; D051381:Rats; D011919:Rats, Inbred Strains
D002364:Caseins; D002738:Chloroquine; D000255:Adenosine Triphosphate; D011388:Prolactin