Surfactant‐modified parathyroid hormone fragments with high potency and prolonged action: Structure‐informed design using glycolipid surfactant conjugation

2021 ◽  
Author(s):  
John J. Nestor ◽  
Wei Wang
Keyword(s):  
Parathyroid Hormone ◽  
Prolonged Action ◽  
High Potency ◽  
Parathyroid Hormone Fragments ◽  
Action Structure

INACTIVATION AND DEGRADATION OF PORCINE CALCITONIN BY RAT LIVER, AND RELATIVE STABILITY OF SALMON CALCITONIN

1970 ◽  
Vol 48 (2) ◽  
pp. 181-188 ◽  
Author(s):  
M. de LUISE ◽  
T. J. MARTIN ◽  
R. A. MELICK
Keyword(s):  
Biological Activity ◽  
Rat Liver ◽  
Salmon Calcitonin ◽  
Trichloroacetic Acid ◽  
Maximal Activity ◽  
Active Principle ◽  
Rat Tissues ◽  
Prolonged Action ◽  
High Potency ◽  
Dose Dependent

SUMMARY Slices and homogenates of a number of rat tissues inactivated porcine calcitonin labelled with 125I; the most active tissue was the liver. Maximal activity was found in rat liver supernatant. The reaction was pH- and dose-dependent, the active principle was non-diffusible, inhibited by p-chloromercuribenzoate and EDTA, and destroyed by heat. Biological activity of calcitonin was lost parallel with the breakdown of the labelled calcitonin (as measured by loss of trichloroacetic acid precipitability). Salmon ultimobranchial calcitonin was much less susceptible to inactivation by rat liver supernatant than the porcine hormone, which may explain the high potency and prolonged action of the salmon hormone in the rat.

scholarly journals Evidence That the Amino-Terminal Composition of Non-(1–84) Parathyroid Hormone Fragments Starts before Position 19

2005 ◽  
Vol 51 (1) ◽  
pp. 169-176 ◽  
Author(s):  
Pierre D’Amour ◽  
Jean-Hugues Brossard ◽  
Agnès Räkel ◽  
Louise Rousseau ◽  
Caroline Albert ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
The Other ◽  
Type I ◽  
Dialysis Patients ◽  
Intact Pth ◽  
Amino Terminal ◽  
Hplc Profiles ◽  
Terminal Structure ◽  
Affinity Interaction ◽  
Parathyroid Hormone Fragments

Abstract Background: Non-(1–84) parathyroid hormone (PTH) fragments are large C-terminal fragments of PTH with a partially preserved N-terminal structure. They differ from other C-terminal PTH fragments, which do not have an N-terminal structure and do not react in intact PTH assays. We aimed to identify the minimal N-terminal structure common to all non-(1–84) PTH fragments. Methods: Sera obtained from six healthy individuals and six patients with primary hyperparathyroidism, and six serum pools from dialysis patients with different PTH concentrations were fractionated by HPLC and analyzed by four different PTH assays. Each assay was characterized by saturation analysis of its detection antibody and capacity to react with different PTH fragments. Human PTH(1–84) [hPTH(1–84)] calibrators were normalized to an in-house hPTH(1–84) calibrator. Results: The cyclase-activating PTH (CA-PTH) assay had an early (1, 2,) epitope and reacted only with hPTH(1–84). The other assays had epitopes in region (13–34). Total and intact PTH assays had epitopes proximal to position 18 and reacted equally well with hPTH(1–84) and hPTH(7–84), and the Elecsys PTH assay had an epitope distal to position 19, being saturable by hPTH(18–48) and also reacting with [Tyr34]hPTH(19–84). The HPLC profiles obtained with these assays showed that non-(1–84) PTH fragments did not react in the CA-PTH assay, as expected. The amount of non-(1–84) PTH detected by the other three assays was similar when the assay results were normalized to a common calibrator. Conclusions: The results suggest that the amount of non-(1–84) PTH detected by epitopes proximal or distal to position 19 of the PTH structure is identical, indicating a common minimum structure starting before position 19. This in turn points to a probable high-affinity interaction with the C-PTH receptor, as observed previously with [Tyr34]hPTH(19–84) in various cell lines and in mouse osteocytes with PTH/PTHrP type I receptor ablation.

Stimulatory effect of carboxyl-terminal parathyroid hormone fragments on osteoclast-like cell formation and osteoclastic activity

1994 ◽  
Vol 12 (S1) ◽  
pp. S125-S129 ◽  
Author(s):  
Hiroshi Kaji ◽  
Toshitsugu Sugimoto ◽  
Masanori Kanatani ◽  
Akimitsu Miyauchi ◽  
Toru Yamaguchi ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Cell Formation ◽  
Osteoclastic Activity ◽  
Carboxyl Terminal ◽  
Parathyroid Hormone Fragments

In vivo arteriolar dilation in response to parathyroid hormone fragments

Peptides ◽  
1987 ◽  
Vol 8 (3) ◽  
pp. 443-448 ◽  
Author(s):  
Jessica P. Dowe ◽  
Irving G. Joshua
Keyword(s):  
Parathyroid Hormone ◽  
Parathyroid Hormone Fragments
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