title: Intracellular degradation of newly synthesized casein in perfused rat mammary gland.
abstract: 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.
authors.affiliation: Hannah Research Institute, Ayr.
authors.forename: C J
authors.initials: CJ
authors.lastname: Wilde
authors.forename: M A
authors.initials: MA
authors.lastname: Kerr
authors.forename: D T
authors.initials: DT
authors.lastname: Calvert
mesh_terms: 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
chemical_list: D002364:Caseins; D002738:Chloroquine; D000255:Adenosine Triphosphate; D011388:Prolactin