Identification and partial characterization of parathyroid hormone-related protein in human and bovine milk

1990 ◽  
Vol 127 (1) ◽  
pp. 167-176 ◽  
Author(s):  
W. A. Ratcliffe ◽  
E. Green ◽  
J. Emly ◽  
S. Norbury ◽  
M. Lindsay ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Cyclic Amp ◽  
Molecular Species ◽  
Bovine Milk ◽  
Gel Filtration ◽  
Molecular Forms ◽  
Gel Chromatography ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein

ABSTRACT Parathyroid hormone-related protein (PTHrP) was measured in human and bovine milk by radioimmunoassay (RIA) and bioassay, and the molecular forms characterized by gel chromatography and immunoblotting of affinity-purified PTHrP. Mean immunoreactive PTHrP(1–34) concentrations were 23 and 87 μg/l in human and bovine milk respectively. Bioactive (BIO) PTHrP concentrations determined by cyclic AMP production by ROS 17/2·8 cells correlated significantly (P< 0·001) with those obtained by RIA (BIO = 1·04RIA−3·4, r = 0·939). Gel filtration of human and bovine milk identified several peaks with immunoactivity and bioactivity. Immunoblotting of affinity-purified PTHrP revealed multiple molecular species including components with mobilities similar to those of PTHrP and its subfragments. These studies confirm the presence of immuno- and bioactive PTHrP in milk and suggest that post-translational processing is complex and variable. Journal of Endocrinology (1990) 127, 167–176

scholarly journals Purification and Characterization of Recombinant Human Parathyroid Hormone-related Protein

1989 ◽  
Vol 264 (25) ◽  
pp. 14806-14811
Author(s):  
R G Hammonds ◽  
P McKay ◽  
G A Winslow ◽  
H Diefenbach-Jagger ◽  
V Grill ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Related Protein ◽  
Human Parathyroid Hormone ◽  
Purification And Characterization ◽  
Parathyroid Hormone Related Protein

scholarly journals Parathyroid hormone-related protein detection and interaction with NO and cyclic AMP in the renovascular system

1996 ◽  
Vol 50 (5) ◽  
pp. 1591-1603 ◽  
Author(s):  
Thierry Massfelder ◽  
Andrew F. Stewart ◽  
Karlhans Endlich ◽  
Neil Soifer ◽  
Clément Judes ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Cyclic Amp ◽  
Protein Detection ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein

Effects of two synthetic parathyroid hormone-related protein fragments on maternofetal transfer of calcium and magnesium and release of cyclic AMP by the in-situ perfused rat placenta

1991 ◽  
Vol 129 (3) ◽  
pp. 399-404 ◽  
Author(s):  
A. J. Shaw ◽  
M. Z. Mughal ◽  
M. J. A. Maresh ◽  
C. P. Sibley
Keyword(s):  
Parathyroid Hormone ◽  
Cyclic Amp ◽  
Ringer Solution ◽  
Related Protein ◽  
Placental Perfusion ◽  
Protein Fragments ◽  
Parathyroid Hormone Related Protein ◽  
Peak Release ◽  
Similar Peak

ABSTRACT Two human parathyroid hormone-related protein (hPTHrP) fragments were tested for effects on maternofetal transfer of 45Ca and Mg across the in-situ perfused rat placenta at 21 days of gestation (term = 23 days). The fetal placental circulation was perfused with a Mg-free Krebs–Ringer solution and the unidirectional maternofetal clearance (Kmf) of 45Ca and Mg compared with that of 51Cr-EDTA, the latter being employed as a paracellular diffusional marker. Placental perfusion with hPTHrP(1–34) (100 ng/ml) or hPTHrP(75–86)amide (50 ng/ml) did not significantly alter the Kmf of 45Ca or that of Mg. In separate rats, however, hPTHrP(1–34) but not hPTHrP(75–86)amide stimulated marked placental cyclic AMP (cAMP) release, the peak response of 63±7 pmol/min occurring 10 min after the beginning of the peptide perfusion. A lower dose of hPTHrP(1–34) (4 ng/ml) produced a similar peak release of cAMP, as did [Nle8,21,Tyr34]-rPTH(1–34)amide (4 ng/ml) and the adenylate cyclase agonist forskolin (17 μmol/l). Forskolin also rapidly increased the Kmf of 45Ca but not that of Mg or 51Cr-EDTA. The present study indicates that hPTHrP does not acutely affect maternofetal transfer of Ca or Mg across the perfused rat placenta. The data also question the role played by cAMP in the stimulatory actions of forskolin on placental Ca transport. Journal of Endocrinology (1991) 129, 399–404

scholarly journals Cloning of bovine parathyroid hormone-related protein (PTHrP) cDNA and expression of PTHrP mRNA in the bovine mammary gland

1998 ◽  
Vol 20 (2) ◽  
pp. 271-280 ◽  
Author(s):  
SF Wojcik ◽  
FL Schanbacher ◽  
LK McCauley ◽  
H Zhou ◽  
V Kartsogiannis ◽  
...  
Keyword(s):  
Mammary Gland ◽  
Parathyroid Hormone ◽  
Cdna Library ◽  
Bovine Milk ◽  
Bovine Brain ◽  
Molecular Heterogeneity ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein ◽  
Lactating Mammary Gland ◽  
Brain Cdna Library

Parathyroid hormone-related protein (PTHrP) produced by the mammary gland has been postulated to have multiple functions in both the mother and neonate. In humans, alternative 3'-mRNA splicing and endoproteolytic processing result in multiple bioactive PTHrP peptides. Multiple PTHrP peptides also have been reported in bovine milk. To investigate the source of molecular heterogeneity of PTHrP in bovine milk, bovine PTHrP was cloned from a bovine brain cDNA library, sequenced and used to characterize the mammary PTHrP transcript. A 1065 bp clone (bP1) for bovine PTHrP was isolated from a brain cDNA library. The bP1 clone contained the entire coding sequence of PTHrP and 61 and 473 nucleotides of the 5'- and 3'-untranslated regions (UTRs) respectively. The predicted amino acid sequence of bovine PTHrP was 72-92% homologous to the sequences of chicken, rat, mouse, human, and canine PTHrP with the highest sequence divergence present in the C-terminal region of the peptide. The 5'- and 3'-UTRs of bovine brain PTHrP have a high degree of homology to exons 4 and 9 of human PTHrP respectively. PTHrP was expressed as a single 1200 nucleotide mRNA transcript in lactating bovine mammary tissue. RT-PCR using region-specific oligonucleotide primers derived from bP1 demonstrated that PTHrP mRNA transcripts in bovine brain and lactating mammary gland utilize the same 5'- and 3'-UTRs. Expression of PTHrP mRNA was localized to secretory and ductular epithelial cells within the lactating mammary gland, as detected using in situ hybridization. Expression of PTHrP mRNA was demonstrated in the mammary gland during late pregnancy and throughout lactation in cows.

Parathyroid hormone-related protein in human term placenta and membranes

1994 ◽  
Vol 142 (2) ◽  
pp. 217-224 ◽  
Author(s):  
S J Bowden ◽  
J F Emly ◽  
S V Hughes ◽  
G Powell ◽  
A Ahmed ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Caesarean Section ◽  
Amniotic Fluid ◽  
Elective Caesarean Section ◽  
Molecular Forms ◽  
Molecular Heterogeneity ◽  
Related Protein ◽  
Human Term Placenta ◽  
Parathyroid Hormone Related Protein ◽  
Spontaneous Labour

Abstract Parathyroid hormone-related protein (PTHrP), the hypercalcaemia of malignacy factor, is expressed in the tissues of the human uteroplacental unit, including the placenta, amnion and chorion. We have used three region-specific immunoassays to quantitate and compare the distribution of PTHrP in tissues obtained at term following spontaneous labour and vaginal delivery or elective Caesarean section. In non-labouring women highest PTHrP(1–86) and (37–67) immunoreactivity was found in amnion covering the placenta, rather than the decidua parietalis of the uterus (reflected amnion) (median 1020 vs 451 fmol/g; 2181 vs 1444 fmol/g respectively). In labouring women, the PTHrP(1–86) concentration in reflected amnion was inversely correlated with the interval between rupture of the membranes and delivery. Tissue PTHrP(1–86) concentrations were lower in placenta than in chorion and amnion (medians 12, 109 and 664 fmol/g respectively) and, in all tissues, PTHrP(1–34) and (37–67) concentrations were significantly higher than that of PTHrP(1–86). Bioactive PTHrP(1–34) was detected in placenta, chorion and amnion using the ROS cell bioassay. The PTHrP(1–86) concentration (mean ± s.e.m.=41·4 ± 4·5 pmol/l) was high in amniotic fluid at term, although in maternal and cord plasma levels were only modestly increased. The molecular forms of PTHrP present in tissues and amniotic fluid were investigated by column chromatography which confirmed its molecular heterogeneity and suggested that processing is tissue-specific and occurs at both amino- and carboxy-terminals of the peptide. Journal of Endocrinology (1994) 142, 217–224

Synthesis of fully active biotinylated analogs of parathyroid hormone and parathyroid hormone-related protein as tools for the characterization of parathyroid hormone receptors

Biochemistry ◽  
1992 ◽  
Vol 31 (16) ◽  
pp. 4026-4033 ◽  
Author(s):  
Eliahu Roubini ◽  
Le T. Duong ◽  
Susan W. Gibbons ◽  
Chih T. Leu ◽  
Michael P. Caulfield ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Hormone Receptors ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein

scholarly journals Structural and Physiologic Characterization of the Mid-region Secretory Species of Parathyroid Hormone-related Protein

1996 ◽  
Vol 271 (40) ◽  
pp. 24371-24381 ◽  
Author(s):  
Terence L. Wu ◽  
Rupangi C. Vasavada ◽  
Kai Yang ◽  
Thierry Massfelder ◽  
Michael Ganz ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein
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