Modulation of substance P signaling by dipeptidyl peptidase-IV enzymatic activity in human glioma cell lines

Title:

Modulation of substance P signaling by dipeptidyl peptidase-IV enzymatic activity in human glioma cell lines

Creator:

Petr Bušek, Jarmila Stremeňová, Evžen Křepela, and Aleksi Šedo

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:726f79d5-3aad-46e8-8e0f-b4ba024c106c
uuid:726f79d5-3aad-46e8-8e0f-b4ba024c106c
issn:0862-8408

Subject:

Biochemie. Molekulární biologie. Biofyzika, fyziologie, gliomy, vápník, physiology, gliomas, calcium, dipeptidyl peptidase, substance P, NK1 receptor, calcium signaling, 2, and 577

Type:

article, články, model:article, and TEXT

Format:

print, bez média, and svazek

Description:

Dipeptidyl peptidase-IV (DPP-IV, CD26) is a serine protease almost ubiquitously expressed on cell surface and present in body fluids. DPP-IV has been suggested to proteolytically modify a number of biologically active peptides including substance P (SP) and the chemokine stro mal cell derived factor-1α (SDF-1α, CXCL12). SP and SDF-1α have been implicated in the regulation of multiple biological processes and also induce responses that may be relevant for glioma progression. Both SP and SDF-1α are signaling through cell surface receptors and use intracellular calcium as a second messenger. The effect of DPP-IV on intracellular calcium mobilization mediated by SP and SDF- α was monitored in suspension of wild type U373 and DPP-IV transfected U373DPPIV glioma cells using indicator FURA-2. Nanomolar concentrations of SP triggered a transient dose dependent increase in intracellular calcium rendering the cells refractory to repeated stimulation, while SDF-1α had no measurable effect. SP signaling in DPP-IV overexpressing U373DPPIV cells was not substantially different from that in wild type cells. However, preincubation of SP with the DPP-IV overexpressing cells lead to the loss of its signaling potential, which could be prevented with DPP-IV inhibitors. Taken together, DPP-IV may proteolytically inactivate local mediators involved in gliomagenesis., P. Bušek, J, Stremeňová, E. Křepela, A. Šedo., and Obsahuje bibliografii a bibliografické odkazy

Language:

English

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Source:

Physiological research | 2008 Volume:57 | Number:3

Harvested from:

CDK

Metadata only:

false