Carboxy-terminal PTH fragments stimulate [3H]thymidine incorporation in vascular endothelial cells

Ke Hong Ding; Qing Zhong; Ding Xie; Jianrui Xu; Roni J. Bollag; Wendy B. Bollag; Carlos M. Isales

doi:10.1016/j.peptides.2005.01.002

Carboxy-terminal PTH fragments stimulate [³H]thymidine incorporation in vascular endothelial cells

Ke Hong Ding, Qing Zhong, Ding Xie, Jianrui Xu, Roni J. Bollag, Wendy B. Bollag, Carlos M. Isales

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

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	https://doi.org/10.1016/j.peptides.2005.01.002
State	Published - May 2005

Keywords

Calcium
Endothelial cells
PTH
Proliferation
Receptors
Signaling

ASJC Scopus subject areas

Biochemistry
Physiology
Endocrinology
Cellular and Molecular Neuroscience

Access to Document

10.1016/j.peptides.2005.01.002

Fingerprint Dive into the research topics of 'Carboxy-terminal PTH fragments stimulate [<sup>3</sup>H]thymidine incorporation in vascular endothelial cells'. Together they form a unique fingerprint.

Cite this

@article{700a62a5079d44738fdef27be4d12e14,

title = "Carboxy-terminal PTH fragments stimulate [3H]thymidine incorporation in vascular endothelial cells",

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.",

keywords = "Calcium, Endothelial cells, PTH, Proliferation, Receptors, Signaling",

author = "Ding, {Ke Hong} and Qing Zhong and Ding Xie and Jianrui Xu and Bollag, {Roni J.} and Bollag, {Wendy B.} and Isales, {Carlos M.}",

note = "Funding Information: This work was supported in part by grants from the National Institutes of Health RO1-DK58680 (CMI) and the Veterans Affairs Merit Review Program (CMI). Copyright: Copyright 2017 Elsevier B.V., All rights reserved.",

year = "2005",

month = may,

doi = "10.1016/j.peptides.2005.01.002",

language = "English (US)",

volume = "26",

pages = "853--862",

journal = "Peptides",

issn = "0196-9781",

publisher = "Elsevier Inc.",

number = "5",

}

TY - JOUR

T1 - Carboxy-terminal PTH fragments stimulate [3H]thymidine incorporation in vascular endothelial cells

AU - Ding, Ke Hong

AU - Zhong, Qing

AU - Xie, Ding

AU - Xu, Jianrui

AU - Bollag, Roni J.

AU - Bollag, Wendy B.

AU - Isales, Carlos M.

N1 - Funding Information: This work was supported in part by grants from the National Institutes of Health RO1-DK58680 (CMI) and the Veterans Affairs Merit Review Program (CMI). Copyright: Copyright 2017 Elsevier B.V., All rights reserved.

PY - 2005/5

Y1 - 2005/5

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 -