Characterization of prolactin- and growth hormone-binding proteins in milk and their diversity among species.
Abstract: The present study was undertaken to identify and characterize the diversity and species distribution of soluble prolactin binding-protein (PRL-BP) and growth hormone-binding protein (PRL-BP) in mammalian milk. We previously divided mammalian serum GH-BP into four main groups and identified a GH-BP with shared lactogenic/somatogenic properties in rabbit, horse, dog, pig and cat (Type III species). Here we describe PRL-BP in milk of Type III species and show it is relatively conserved within the group, having similar characteristics in terms of binding affinity for hGH (0.74-5.5 x 10(10) M(-1)), specificity towards the lactogenic hormones and molecular weight (approximately 35 kDa), except for the more heterogeneous pig milk (approximately 43 to approximately 88 kDa) Furthermore, high affinity PRL-BP was also demonstrated in sheep milk, having pure lactogenic specificity and an Mr of approximately 35 kDa. Human milk contained a high affinity PRL-BP/GH-BP, which was recognized by both hPRL and hGH and also having an Mr of approximately 35 kDa. In rabbit milk a separate GH-BP was also detected; it was clearly distinguished from the corresponding milk PRL-BP on the basis of its Mr of approximately 44 kDa (vs. approximately 32 kDa for PRL-BP), its shared lactogenic/somatogenic hormonal specificity (vs. purely lactogenic for PRL-BP) and also on the basis of its relative resistance to heating at 56 degrees C for up to 3 h, while PRL-BP activity was completely destroyed within 30 min. This diversity of milk PRL-BP and GH-BP among mammalian species fits in with our earlier classification of serum GH-BP and also with the reported evolutionary rates of PRL and GH; this suggests these BPs may play important species-specific roles in the suckling newborn and/or maternal mammary gland, in keeping with the functions described for GH-BP.
Publication Date: 1997-06-20 PubMed ID: 9220032DOI: 10.1016/s0303-7207(97)00088-9Google Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research article investigates the diversity of soluble prolactin binding-protein (PRL-BP) and growth hormone-binding protein (GH-BP) in the milk of different mammalian species. The study further attempts to characterize these proteins and explore their potential implications.
Characterization of Prolactin- and Growth Hormone-Binding Proteins
- The study delved into the characterization of soluble prolactin-binding protein (PRL-BP) and growth hormone-binding protein (GH-BP) in mammalian milk. This built on the researchers’ previous work where they divided mammalian serum GH-BP into four main groups.
- The researchers found that PRL-BP in milk from certain species – namely rabbits, horse, dog, pig, and cat (Type III species), exhibited relative conservation and demonstrated similar binding affinity for human growth hormone (hGH). However, pig milk displayed greater heterogeneity.
- Hormonal specificity towards lactogenic hormones (involved in lactation) and similar molecular weight across these Type III species was also observed.
Purity of Lactogenic Specificity and Presence of PRL-BP/GH-BP
- This research also highlighted that high affinity PRL-BP was identified in sheep milk, showing pure lactogenic specificity and a similar molecular weight to the PRL-BP in Type III species.
- Human milk showed the presence of a high-affinity PRL-BP/GH-BP that was recognized by both human prolactin (hPRL) and hGH and held an approximately similar molecular weight as that of sheep PRL-BP and Type III PRL-BP.
Diversity of PRL-BP and GH-BP among Mammalian Species
- The study detected a separate and distinct GH-BP in rabbit milk, based on its molecular weight, its shared lactogenic/somatogenic hormonal specificity, and also on its relative resistance to heating up to 56 degrees Celsius for up to 3 hours. This was in contrast to PRL-BP activity, which was completely destroyed within 30 minutes at the same temperature.
- The findings underline the diversity of PRL-BP and GH-BP among different mammalian species, which aligns with the earlier classification of serum GH-BP by the same researchers, and the reported evolutionary rates of prolactin and growth hormone.
- The conclusion drawn from this study suggested these binding proteins may play species-specific roles in the suckling newborn and/or maternal mammary gland, echoing the functions described for GH-BP.
Cite This Article
APA
Amit T, Dibner C, Barkey RJ.
(1997).
Characterization of prolactin- and growth hormone-binding proteins in milk and their diversity among species.
Mol Cell Endocrinol, 130(1-2), 167-180.
https://doi.org/10.1016/s0303-7207(97)00088-9 Publication
Researcher Affiliations
- Department of Pharmacology, Bruce Rappaport Faculty of Medicine, Technion, Israel Institute of Technology, Haifa.
MeSH Terms
- Animals
- Carrier Proteins / chemistry
- Carrier Proteins / metabolism
- Cats
- Dogs
- Female
- Growth Hormone / metabolism
- Horses
- Hot Temperature
- Human Growth Hormone / metabolism
- Humans
- Kinetics
- Milk / metabolism
- Molecular Weight
- Prolactin / metabolism
- Rabbits
- Rats
- Sheep
- Species Specificity
- Swine
Citations
This article has been cited 4 times.- Playford RJ, Weiser MJ. Bovine Colostrum: Its Constituents and Uses.. Nutrients 2021 Jan 18;13(1).
- Costa-Brito AR, Quintela T, Gonçalves I, Duarte AC, Costa AR, Arosa FA, Cavaco JE, Lemos MC, Santos CRA. The Choroid Plexus Is an Alternative Source of Prolactin to the Rat Brain.. Mol Neurobiol 2021 Apr;58(4):1846-1858.
- Rastrelli G, Corona G, Maggi M. The role of prolactin in andrology: what is new?. Rev Endocr Metab Disord 2015 Sep;16(3):233-48.
- Maniou Z, Wallis OC, Wallis M. Episodic molecular evolution of pituitary growth hormone in Cetartiodactyla.. J Mol Evol 2004 Jun;58(6):743-53.
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