Aim: The retention of angiotensin converting enzyme (ACE) in the plasma membrane is regulated by casein kinase II (CK2)-mediated phosphorylation. The endothelial cells treated with CK2 inhibitor decreased the ACE phosphorylation and increased its shedding. Seminal plasma peptide (pGlu-Val-Ala-Asp-Ser-Asp-Gln-Asn), synthesized following data obtained from biochemical and mass spectrometry analysis of highly purified fraction from bovine seminal plasma, was demonstrated to be a substrate of CK2. The aim of our research was to study whether synthetic seminal plasma peptide competes with ACE in CK2 phosphorylation influencing ACE shedding. Methods: GC-1spg, mouse spermatogonia cell line, and ECV304, human umbilical cord transformed endothelium, expressing testicular ACE and somatic ACE, respectively, were incubated for 24 h at 37°C with increased doses of synthetic seminal plasma peptide. ACE activity was measured by following the hydrolyzing activity of the cell homogenates on FAPGG, a synthetic substrate of somatic and testicular ACE. Results: The preliminary data show a dose-dependent decrease of ACE activity in both cell lines after the treatment with synthetic seminal plasma peptide. This residual activity is lower in GC-1spg cell line (33% of ACE activity vs control at 10-8M peptide concentration) than in ECV304 cell line (54% of ACE activity vs control at 10-8M peptide concentration). Conclusions: These preliminary results suggest the possible role of synthetic seminal plasma peptide in the control on testicular and somatic ACE release from plasma membrane.

Synthetic seminal plasma peptide influences angiotensin converting enzyme retention in the plasma membrane

QUASSINTI, Luana;MACCARI, Ennio;MURRI, Oretta;BRAMUCCI, Massimo
2006

Abstract

Aim: The retention of angiotensin converting enzyme (ACE) in the plasma membrane is regulated by casein kinase II (CK2)-mediated phosphorylation. The endothelial cells treated with CK2 inhibitor decreased the ACE phosphorylation and increased its shedding. Seminal plasma peptide (pGlu-Val-Ala-Asp-Ser-Asp-Gln-Asn), synthesized following data obtained from biochemical and mass spectrometry analysis of highly purified fraction from bovine seminal plasma, was demonstrated to be a substrate of CK2. The aim of our research was to study whether synthetic seminal plasma peptide competes with ACE in CK2 phosphorylation influencing ACE shedding. Methods: GC-1spg, mouse spermatogonia cell line, and ECV304, human umbilical cord transformed endothelium, expressing testicular ACE and somatic ACE, respectively, were incubated for 24 h at 37°C with increased doses of synthetic seminal plasma peptide. ACE activity was measured by following the hydrolyzing activity of the cell homogenates on FAPGG, a synthetic substrate of somatic and testicular ACE. Results: The preliminary data show a dose-dependent decrease of ACE activity in both cell lines after the treatment with synthetic seminal plasma peptide. This residual activity is lower in GC-1spg cell line (33% of ACE activity vs control at 10-8M peptide concentration) than in ECV304 cell line (54% of ACE activity vs control at 10-8M peptide concentration). Conclusions: These preliminary results suggest the possible role of synthetic seminal plasma peptide in the control on testicular and somatic ACE release from plasma membrane.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11581/115420
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