Abstract
We have previously reported that the intact PTH molecule (1-84) stimulates proliferation of human umbilical vein endothelial cells (HUVECs). To define the bioactive portion of the PTH molecule we utilized amino, mid and carboxy-terminal PTH fragments. Carboxy- but not amino-terminal fragments were equivalent to the intact PTH molecule in stimulating [3H]thymidine incorporation in HUVEC. Carboxy- but not amino-terminal PTH fragments increased intracellular calcium. Blocking the rise in intracellular calcium with calcium chelators abolished PTHs proliferative effect on HUVEC. In contrast to PTH 1-84, the carboxy-terminal fragment effect on [3H]thymidine incorporation was blocked by KN-93 an inhibitor of CaM kinase II. Taken together, these data suggest that the carboxy-terminal PTH is (or contains) the bioactive fragment responsible for the changes in intracellular calcium and thymidine incorporation in HUVEC stimulated with the intact PTH molecule.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 853-862 |
| Number of pages | 10 |
| Journal | Peptides |
| Volume | 26 |
| Issue number | 5 |
| DOIs | |
| State | Published - Jan 1 2005 |
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Keywords
- Calcium
- Endothelial cells
- PTH
- Proliferation
- Receptors
- Signaling
ASJC Scopus subject areas
- Biochemistry
- Physiology
- Endocrinology
- Cellular and Molecular Neuroscience
Cite this
Carboxy-terminal PTH fragments stimulate [3H]thymidine incorporation in vascular endothelial cells. / Ding, Kehong; Zhong, Qing; Xie, Ding; Xu, Jianrui; Bollag, Roni Jacob; Bollag, Wendy B; Isales, Carlos M.
In: Peptides, Vol. 26, No. 5, 01.01.2005, p. 853-862.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Carboxy-terminal PTH fragments stimulate [3H]thymidine incorporation in vascular endothelial cells
AU - Ding, Kehong
AU - Zhong, Qing
AU - Xie, Ding
AU - Xu, Jianrui
AU - Bollag, Roni Jacob
AU - Bollag, Wendy B
AU - Isales, Carlos M
PY - 2005/1/1
Y1 - 2005/1/1
N2 - We have previously reported that the intact PTH molecule (1-84) stimulates proliferation of human umbilical vein endothelial cells (HUVECs). To define the bioactive portion of the PTH molecule we utilized amino, mid and carboxy-terminal PTH fragments. Carboxy- but not amino-terminal fragments were equivalent to the intact PTH molecule in stimulating [3H]thymidine incorporation in HUVEC. Carboxy- but not amino-terminal PTH fragments increased intracellular calcium. Blocking the rise in intracellular calcium with calcium chelators abolished PTHs proliferative effect on HUVEC. In contrast to PTH 1-84, the carboxy-terminal fragment effect on [3H]thymidine incorporation was blocked by KN-93 an inhibitor of CaM kinase II. Taken together, these data suggest that the carboxy-terminal PTH is (or contains) the bioactive fragment responsible for the changes in intracellular calcium and thymidine incorporation in HUVEC stimulated with the intact PTH molecule.
AB - We have previously reported that the intact PTH molecule (1-84) stimulates proliferation of human umbilical vein endothelial cells (HUVECs). To define the bioactive portion of the PTH molecule we utilized amino, mid and carboxy-terminal PTH fragments. Carboxy- but not amino-terminal fragments were equivalent to the intact PTH molecule in stimulating [3H]thymidine incorporation in HUVEC. Carboxy- but not amino-terminal PTH fragments increased intracellular calcium. Blocking the rise in intracellular calcium with calcium chelators abolished PTHs proliferative effect on HUVEC. In contrast to PTH 1-84, the carboxy-terminal fragment effect on [3H]thymidine incorporation was blocked by KN-93 an inhibitor of CaM kinase II. Taken together, these data suggest that the carboxy-terminal PTH is (or contains) the bioactive fragment responsible for the changes in intracellular calcium and thymidine incorporation in HUVEC stimulated with the intact PTH molecule.
KW - Calcium
KW - Endothelial cells
KW - PTH
KW - Proliferation
KW - Receptors
KW - Signaling
UR - http://www.scopus.com/inward/record.url?scp=16244396442&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=16244396442&partnerID=8YFLogxK
U2 - 10.1016/j.peptides.2005.01.002
DO - 10.1016/j.peptides.2005.01.002
M3 - Article
C2 - 15808916
AN - SCOPUS:16244396442
VL - 26
SP - 853
EP - 862
JO - Peptides
JF - Peptides
SN - 0196-9781
IS - 5
ER -