Identification and characterization of a cytosolic 30 kDa histamine stimulated phosphoprotein in parietal cell cytosol

Margret Oddsdottir; James R. Goldenring; Thomas E. Adrian; Michael J. Zdon; Karl A. Zucker; Irvin M. Modlin

doi:10.1016/0006-291X(88)90166-0

Identification and characterization of a cytosolic 30 kDa histamine stimulated phosphoprotein in parietal cell cytosol

Margret Oddsdottir
, James R. Goldenring
, Thomas E. Adrian
, Michael J. Zdon
, Karl A. Zucker
, Irvin M. Modlin

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

7 Citations (Scopus)

Abstract

Histamine stimulated acid secretion is mediated by an increase in intracellular cAMP. Cytosolic protein phosphorylation stimulated by histamine was investigated in isolated rabbit parietal cells. Histamine stimulated the phosphorylation of a 30 kDa phosphoprotein with an isoelectric point of 5.6. Cimetidine completely inhibited histamine-stimulated pp30 phosphorylation. However, omeprazole had no effect on the phosphorylation of pp30. Forskolin and 8-bromo-cAMP also stimulated the phosphorylation of pp30. The results suggest that pp30 is a histamine-stimulated, cAMP-dependently phosphorylated protein substrate in parietal cell cytosol.

Original language	English
Pages (from-to)	489-496
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	154
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(88)90166-0
Publication status	Published - Jul 29 1988
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/0006-291X(88)90166-0

Cite this

@article{7960c0032acd4f6690c83d89d537779e,

title = "Identification and characterization of a cytosolic 30 kDa histamine stimulated phosphoprotein in parietal cell cytosol",

abstract = "Histamine stimulated acid secretion is mediated by an increase in intracellular cAMP. Cytosolic protein phosphorylation stimulated by histamine was investigated in isolated rabbit parietal cells. Histamine stimulated the phosphorylation of a 30 kDa phosphoprotein with an isoelectric point of 5.6. Cimetidine completely inhibited histamine-stimulated pp30 phosphorylation. However, omeprazole had no effect on the phosphorylation of pp30. Forskolin and 8-bromo-cAMP also stimulated the phosphorylation of pp30. The results suggest that pp30 is a histamine-stimulated, cAMP-dependently phosphorylated protein substrate in parietal cell cytosol.",

author = "Margret Oddsdottir and Goldenring, \{James R.\} and Adrian, \{Thomas E.\} and Zdon, \{Michael J.\} and Zucker, \{Karl A.\} and Modlin, \{Irvin M.\}",

year = "1988",

month = jul,

day = "29",

doi = "10.1016/0006-291X(88)90166-0",

language = "English",

volume = "154",

pages = "489--496",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier B.V.",

number = "2",

}

TY - JOUR

T1 - Identification and characterization of a cytosolic 30 kDa histamine stimulated phosphoprotein in parietal cell cytosol

AU - Oddsdottir, Margret

AU - Goldenring, James R.

AU - Adrian, Thomas E.

AU - Zdon, Michael J.

AU - Zucker, Karl A.

AU - Modlin, Irvin M.

PY - 1988/7/29

Y1 - 1988/7/29

N2 - Histamine stimulated acid secretion is mediated by an increase in intracellular cAMP. Cytosolic protein phosphorylation stimulated by histamine was investigated in isolated rabbit parietal cells. Histamine stimulated the phosphorylation of a 30 kDa phosphoprotein with an isoelectric point of 5.6. Cimetidine completely inhibited histamine-stimulated pp30 phosphorylation. However, omeprazole had no effect on the phosphorylation of pp30. Forskolin and 8-bromo-cAMP also stimulated the phosphorylation of pp30. The results suggest that pp30 is a histamine-stimulated, cAMP-dependently phosphorylated protein substrate in parietal cell cytosol.

AB - Histamine stimulated acid secretion is mediated by an increase in intracellular cAMP. Cytosolic protein phosphorylation stimulated by histamine was investigated in isolated rabbit parietal cells. Histamine stimulated the phosphorylation of a 30 kDa phosphoprotein with an isoelectric point of 5.6. Cimetidine completely inhibited histamine-stimulated pp30 phosphorylation. However, omeprazole had no effect on the phosphorylation of pp30. Forskolin and 8-bromo-cAMP also stimulated the phosphorylation of pp30. The results suggest that pp30 is a histamine-stimulated, cAMP-dependently phosphorylated protein substrate in parietal cell cytosol.

UR - https://www.scopus.com/pages/publications/0023803079

UR - https://www.scopus.com/pages/publications/0023803079#tab=citedBy

U2 - 10.1016/0006-291X(88)90166-0

DO - 10.1016/0006-291X(88)90166-0

M3 - Article

C2 - 2840899

AN - SCOPUS:0023803079

SN - 0006-291X

VL - 154

SP - 489

EP - 496

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

Identification and characterization of a cytosolic 30 kDa histamine stimulated phosphoprotein in parietal cell cytosol

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this