NDLI: EGF-stimulated aldosterone secretion is mediated by tyrosine phosphorylation but not by phospholipase C in cultured porcine adrenal glomerulosa cells.

Content Provider	PubMed Central
Author	Kim, S. Y. Park, D. J. Lee, H. K.
Abstract	We examined the effect of EGF and angiotensin II (AII) on the formation of inositol phosphates and aldosterone secretion, and observed the role of tyrosine phosphorylation in EGF or AII-mediated aldosterone secretion. As cultured glomerulosa cells were incubated with increasing concentrations of EGF (0.01-100 ng/mL), aldosterone secretion increased and reached a plateau at EGF concentration of 10-50 ng/mL. Although EGF alone did increase aldosterone secretion in glomerulosa cells, it did not enhance AII-induced aldosterone secretion when both EGF and AII were added. EGF-induced tyrosine phosphorylation peaked at around 1 min after stimulation and at a concentration of 10-50 ng/mL. AII stimulated tyrosine phosphorylation, but the stimulatory effect was less than that observed in the presence of EGF. Although the latter induced tyrosine phosphorylation of various proteins, it failed to stimulate the formation of inositol phosphates. On the other hand, AII stimulated the production of inositol phosphates in a dose-dependent manner, with maximal stimulation at 10(-8)M. The addition of 10 ng/mL EGF did not affect the AII-induced formation of inositol phosphates. In conclusion, EGF-stimulated aldosterone secretion might be mediated by tyrosine kinase. However, since EGF did not stimulate inositol phospholipid hydrolysis in cultured porcine adrenal glomerulosa cells, its effect does not seem to be mediated by phospholipase C.
Related Links	http://dx.doi.org/10.3346/jkms.1998.13.6.629
Starting Page	629
File Format	PDF
ISSN	10118934
e-ISSN	15986357
Journal	Journal of Korean Medical Science
Issue Number	6
Volume Number	13
Language	English
Publisher	Korean Academy of Medical Sciences
Publisher Date	1998-01-01
Access Restriction	Open
Rights Holder	Korean Academy of Medical Sciences
Subject Keyword	Medicine(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Medicine

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Inhibition of agonist-stimulated aldosterone production from adrenal zona glomerulosa cells by ANP is mediated by GC-A

Phospholipase D2 Mediates Acute Aldosterone Secretion in Response to Angiotensin II in Adrenal Glomerulosa Cells

Roles of Na and Cl ions in Basal and Angiotesin II-Stimulated Aldosterone Secretion in Vitro by Bovine Adrenal Glomerulosa Cells

Phospholipase D2 Mediates Acute Aldosterone Secretion in Response to Angiotensin II in Adrenal Glomerulosa Cells

Phospholipase D2 Mediates Acute Aldosterone Secretion in Response to Angiotensin II in Adrenal Glomerulosa Cells

Activation of phospholipase C in human B cells is dependent on tyrosine phosphorylation.

Pyridine nucleotide redox state parallels production of aldosterone in potassium-stimulated adrenal glomerulosa cells.

Tyrosine phosphorylation is involved in receptor coupling to phospholipase D but not phospholipase C in the human neutrophil.

Tyrosine phosphorylation is involved in receptor coupling to phospholipase D but not phospholipase C in the human neutrophil

EGF-stimulated aldosterone secretion is mediated by tyrosine phosphorylation but not by phospholipase C in cultured porcine adrenal glomerulosa cells.

Similar Documents

Inhibition of agonist-stimulated aldosterone production from adrenal zona glomerulosa cells by ANP is mediated by GC-A

Phospholipase D2 Mediates Acute Aldosterone Secretion in Response to Angiotensin II in Adrenal Glomerulosa Cells

Roles of Na and Cl ions in Basal and Angiotesin II-Stimulated Aldosterone Secretion in Vitro by Bovine Adrenal Glomerulosa Cells

Phospholipase D2 Mediates Acute Aldosterone Secretion in Response to Angiotensin II in Adrenal Glomerulosa Cells

Phospholipase D2 Mediates Acute Aldosterone Secretion in Response to Angiotensin II in Adrenal Glomerulosa Cells

Activation of phospholipase C in human B cells is dependent on tyrosine phosphorylation.

Pyridine nucleotide redox state parallels production of aldosterone in potassium-stimulated adrenal glomerulosa cells.

Tyrosine phosphorylation is involved in receptor coupling to phospholipase D but not phospholipase C in the human neutrophil.

Tyrosine phosphorylation is involved in receptor coupling to phospholipase D but not phospholipase C in the human neutrophil

EGF-stimulated aldosterone secretion is mediated by tyrosine phosphorylation but not by phospholipase C in cultured porcine adrenal glomerulosa cells.