The 16 kDa prolactin fragment arises from partial proteolysis of the native 23 kDa prolactin pituitary hormone. The mammary gland has been involved in this processing, although it has not been clarified whether it occurs in stroma or epithelial cells or extracellularly. Also, the processing enzyme has not been defined yet. Here we show that the incubation medium of stroma-deprived mammary acini from lactating rat contains an enzymatic activity able to cleave, in a temperature- and time-dependent fashion, the 23 kDa prolactin to generate a 16 kDa prolactin detectable under reducing conditions. This cleavage was not impaired in the presence of hirudin, a thrombin inhibitor, but strongly weakened in the presence of pepstatin A, a cathepsin D inhibitor. Cathepsin D immuno-depletion abolished the capability of acini-conditioned medium to cleave the 23 kDa prolactin. Brefeldin A treatment of acini, a condition that largely abolished the apical secretion of milk proteins, did not impair the secretion of the enzymatically active single chain of cathepsin D. These results show that mature cathepsin D from endosomes or lysosomes is released, likely at the baso-lateral site of mammary epithelial cells, and that a cathepsin D-dependent activity is required to effect, under physiological conditions, the cleavage of 23 kDa prolactin in the extracellular medium. This is the first report demonstrating that cathepsin D can perform a limited proteolysis of a substrate at physiological pH outside the cell.
-This review describes the effects of milking (routine and management) on milk yield and milk quality on dairy ruminants and examines the physiological effects of milking on the synthesis and secretion of milk. During milking, differences in the composition of milk as a result of milk ejection reflex are observed: the cisternal milk, immediately available, contains little fat, then milk ejection provokes active transport of high-fat content alveolar milk, into the cisternal compartment. Milking frequency has the capacity to affect milk production too. So, an increase in milking frequency augments milk yield whereas a decrease in milking frequency decreases milk production, with effects on milk composition. The milk ejection reflex is mediated by oxytocin, which induces myoepithelial cell contraction. Nevertheless, other actions of oxytocin may exist, such as a direct effect on proliferation and differentiation of myoepithelial cells and on secretory processes in the mammary epithelial cells. milking / milk ejection / oxytocin / physiological effects / milk quantity and quality Résumé -Ocytocine et vidange mammaire : deux facteurs de variation essentiels de la quantité et la qualité du lait pendant la traite et entre les traites. Cette revue bibliographique pré-sente les effets de la traite (technique et conduite) sur la production quantitative et qualitative de lait, puis précise les mécanismes d'action des effets physiologiques de la traite sur la synthèse et la sécrétion des composants du lait. Au cours d'une traite, la composition du lait évolue, grâce au réflexe d'éjection du lait qui provoque le transfert du lait alvéolaire, riche en matières grasses, vers la citerne. Ainsi, le lait de début de traite est pauvre en matière grasse, tandis que le lait de fin de traite est riche en matière grasse. Les rythmes de traite ont aussi un impact sur la production laitière. Ainsi, l'accroissement de la fréquence de traite augmente la production laitière alors que la réduction du nombre de traite la diminue, avec des répercussions en terme de qualité du lait. L'hormone responsable de l'éjection du lait, l'ocytocine, exerce son rôle de vidange mammaire par déclenchement de la Reprod. Nutr. Dev. 42 (2002) 173-186 173
Oxytocin plays a major role in lactation mainly by its action on milk ejection via the contraction of myoepithelial cells. The effect of oxytocin on milk production and the presence of oxytocin receptors on different epithelial cells suggest that this hormone may play a role in mammary epithelial cells. To determine precisely the various roles of oxytocin, we studied localization of oxytocin receptors in lactating rabbit and rat mammary tissue and the influence of oxytocin on secretory processes in lactating rabbit mammary epithelial cells. Immunolocalization of oxytocin receptors on mammary epithelial cells by immunofluorescence and in mammary tissue by immunogold in addition to in situ hybridization showed that lactating rat and rabbit mammary epithelial cells expressed oxytocin receptors. Moreover, oxytocin bound specifically to epithelial cells. To determine whether oxytocin had an effect on lactating rabbit mammary epithelial cells, isolated mammary fragments were incubated in the presence or absence of 10 −6 i.u. ml −1 of oxytocin. After 1 min of incubation with oxytocin, the morphology of epithelial cells and the localization of caseins and proteins associated with the secretory traffic suggested a striking acceleration of the transport leading to exocytosis, whereas the contraction of myoepithelial cells was only detectable after 7 min. Addition of 10 −8 g ml −1 of atosiban before the addition of oxytocin prevented the oxytocin effect on secretory processes and on myoepithelial cell contraction. Addition of 10 −6 i.u. ml −1 of vasopressin to the incubation medium did not mimic the stimulating effect of oxytocin on secretory traffic. These results show that lactating rabbit and rat mammary epithelial cells express oxytocin receptors and that oxytocin binds to these receptors. They strongly suggest that oxytocin has a dual effect on lactating mammary tissue: an acceleration of the intracellular transfer of caseins in mammary epithelial cells followed by the contraction of myoepithelial cells.
-In mammary epithelial cells, milk lipids and proteins are synthesised in the same compartment, the endoplasmic reticulum. Lipids, carried through the cytoplasm, associate with the apical membrane which then pinches off and releases the lipid globule. Proteins, carried through membrane compartments are released in the lumen after fusion of secretory vesicles with the apical membrane. These processes assure a relatively constant composition of milk but it is not known whether lipid and protein secretion are linked. The protein composition of the milk fat globule membrane and the stimulatory effects of prolactin and oxytocin on lipid and protein secretion suggest that these processes are coupled and co-regulated. However, it is possible to observe a dissociation between the formation and the secretion of the two constituents, during differentiation and in various experimental conditions, and this suggests that coupling is not strictly required. milk lipids / mammary epithelial cells / secretionRésumé -Transport des lipides et des protéines du lait dans les cellules épithéliales mammaires. Dans la cellule épithéliale mammaire, les lipides et les protéines du lait sont synthéti-sés dans le même compartiment, le reticulum endoplasmique. Les lipides transportés à travers le cytoplasme s'accolent à la membrane plasmique apicale qui les enveloppe avant leur sécrétion. Les protéines, transportées dans des compartiments membranaires jusqu'aux vésicules de sécrétion, sont libérées dans la lumière après fusion des vésicules avec la membrane apicale. Ces processus assurent une composition relativement constante du lait. Cependant, on ne sait pas si ces deux types de sécré-tion sont liés. La composition protéique de la membrane du globule gras et l'effet stimulant de la prolactine et de l'ocytocine sur la sécrétion des deux constituants suggèrent que synthèse et sécrétion sont liées et co-régulées. Cependant, la possibilité d'observer une dissociation entre la formation et la sécrétion des deux constituants suggère que ce couplage n'est pas obligatoire.lipides du lait / cellule épithéliale mammaire / sécrétion
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.