Article (Scientific journals)
Characterization of growth hormone-binding protein in cattle plasma: prolactin-binding activity and 24-hour profile.
Massart, Serge; Ban, A. M.; Renaville, Robert et al.
1996In Domestic Animal Endocrinology, 13 (1), p. 47-57
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Keywords :
Animals; Blotting, Western; Carrier Proteins/blood/metabolism; Cattle/blood/physiology; Chromatography, Gel; Circadian Rhythm/physiology; Growth Hormone/analysis/metabolism; Iodine Radioisotopes; Male; Prolactin/analysis/metabolism; Protein Binding
Abstract :
[en] The purpose of this study was to characterize circulating growth hormone-binding proteins (GHBP) and prolactin-binding proteins (PRLBP) in cattle blood plasma. In particular, the 24-hr profile of these molecules was investigated. The preincubation of bull plasma with iodinated bovine growth hormone (bGH) or bovine prolactin (bPRL), followed by gel filtration chromatography (Superdex 200; 1.6 x 60 cm column), resulted in the formation of essentially two complexes. The majority of [125I]bPRL eluted with the first one (M(r) approximately 600 kDa), whereas [125I]bGH mainly appeared in the second one (M(r) approximately 70 kDa). The fractions corresponding to these two peaks were analyzed by western ligand blotting (WLB), under reducing conditions. WLB revealed, respectively, 190-, 56-, 52-, and 28-kDa bands for the first peak and only 52- and 28-kDa bands for the second one. The nature of the 600-kDa peak is at present undetermined, but the 70-kDa one was previously identified as high-affinity GHBP. Displacement studies demonstrated that bGH and bPRL were both able to bind to this GHBP, because the bGH- and bPRL-binding activities of this protein could be saturated by an excess of either of these two hormones. This was indirectly confirmed by the close correlation (r = 0.615; P = 0.0001; n = 155) observed between plasma bGH- and bPRL-binding activities, because this correlation could suggest that both ligands are bound to the same proteins. The temporal concentrations of plasma GHBP were measured in samples collected at 20-min intervals for 24 hr from 8 young bulls. The evaluation of GHBP was realized by WLB, followed by densitometric analysis. Some fluctuations were observed, but these were not correlated with bGH release, even with a +/- 2-hr lag period. In summary, we found that bovine high-affinity GHBP binds not only bGH, but also bPRL. A second type of protein, of higher molecular weight, also binds these two hormones, but further investigations are needed to determine its nature. Finally, GHBP concentrations in cattle blood plasma apparently show fluctuations over a 24-hr period, but no correlation was found between these fluctuations and plasma growth hormone concentrations.
Disciplines :
Veterinary medicine & animal health
Agriculture & agronomy
Author, co-author :
Massart, Serge;  Université de Liège - ULiège > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech
Ban, A. M.
Renaville, Robert ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech
Van Eenaeme, Christian 
Sneyers, M.
Falaki, M.
Istasse, Louis ;  Université de Liège - ULiège > Département de productions animales > Nutrition des animaux domestiques
Clinquart, Antoine ;  Université de Liège - ULiège > Département de sciences des denrées alimentaires > Technologie des denrées alimentaires
Devolder, A.
Burny, Arsène ;  Université de Liège - ULiège > Agro Biotech Gembloux
Portetelle, Daniel ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech
Language :
English
Title :
Characterization of growth hormone-binding protein in cattle plasma: prolactin-binding activity and 24-hour profile.
Publication date :
1996
Journal title :
Domestic Animal Endocrinology
ISSN :
0739-7240
eISSN :
1879-0054
Publisher :
Butterworth Heinemann, Stoneham, United States - Massachusetts
Volume :
13
Issue :
1
Pages :
47-57
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 12 March 2009

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