Characterization of the molecular forms of parathyroid hormone-related protein in milk

1990 ◽  
Vol 18 (5) ◽  
pp. 927-927
Author(s):  
JEAN F. EMLY ◽  
WENDY A. RATCLIFFE
Keyword(s):  
Parathyroid Hormone ◽  
Molecular Forms ◽  
Related Protein ◽  
Parathyroid Hormone Related Protein

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

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

Immunochemical Characterization of Circulating Parathyroid Hormone–Related Protein in Patients with Humoral Hypercalcemia of Cancer

1990 ◽  
Vol 322 (16) ◽  
pp. 1106-1112 ◽  
Author(s):  
William J. Burtis ◽  
Thomas G. Brady ◽  
John J. Orloff ◽  
Julie B. Ersbak ◽  
Raymond P. Warrell ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Related Protein ◽  
Immunochemical Characterization ◽  
Humoral Hypercalcemia ◽  
Parathyroid Hormone Related Protein
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