A specific histamine-stimulated phosphoprotein in isolated parietal cells

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

doi:10.1016/0022-4804(87)90168-5

A specific histamine-stimulated phosphoprotein in isolated parietal cells

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

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

16 Citations (Scopus)

Abstract

Histamine-stimulated phosphorylation was studied in isolated rabbit parietal cells. Secretion of acid, as assessed by aminopyrine uptake, was linear at 15 min of stimulation with histamine. By utilizing two dimensional gels, a specific 30,000-Da protein (pp30) was identified whose phosphorylation was prominently stimulated by histamine after 15 min of incubation. The pp30 protein displayed an isoelectric point of 6.0. Furthermore, cAMP-dependent pp30 phosphorylation could also be demonstrated in vitro in a preparation of parietal cell cytosol. The results suggest that pp30 may represent an important histamine-stimulated cAMP-dependent phosphoprotein involved in the initiation or maintenance of parietal cell secretion.

Original language	English
Pages (from-to)	348-353
Number of pages	6
Journal	Journal of Surgical Research
Volume	42
Issue number	4
DOIs	https://doi.org/10.1016/0022-4804(87)90168-5
Publication status	Published - Apr 1987
Externally published	Yes

ASJC Scopus subject areas

Surgery

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10.1016/0022-4804(87)90168-5

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@article{6d266ccfc6c64f7f822aa46a8f132266,

title = "A specific histamine-stimulated phosphoprotein in isolated parietal cells",

abstract = "Histamine-stimulated phosphorylation was studied in isolated rabbit parietal cells. Secretion of acid, as assessed by aminopyrine uptake, was linear at 15 min of stimulation with histamine. By utilizing two dimensional gels, a specific 30,000-Da protein (pp30) was identified whose phosphorylation was prominently stimulated by histamine after 15 min of incubation. The pp30 protein displayed an isoelectric point of 6.0. Furthermore, cAMP-dependent pp30 phosphorylation could also be demonstrated in vitro in a preparation of parietal cell cytosol. The results suggest that pp30 may represent an important histamine-stimulated cAMP-dependent phosphoprotein involved in the initiation or maintenance of parietal cell secretion.",

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

note = "Funding Information: The authors thank Dr. Howard Rassmussen for invaluable guidance and criticisms of this work, and Dr. Robert DeLorenzo for the use of his Loats two-dimensional digitizing analyzer. This work was supported by a grant from the Veterans Administration to I.M.M.",

year = "1987",

month = apr,

doi = "10.1016/0022-4804(87)90168-5",

language = "English",

volume = "42",

pages = "348--353",

journal = "Journal of Surgical Research",

issn = "0022-4804",

publisher = "Academic Press Inc.",

number = "4",

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TY - JOUR

T1 - A specific histamine-stimulated phosphoprotein in isolated parietal cells

AU - Modlin, Irvin M.

AU - Oddsdottir, Margret

AU - Adrian, Thomas E.

AU - Zdon, Michael J.

AU - Zucker, Karl A.

AU - Goldenring, James R.

N1 - Funding Information: The authors thank Dr. Howard Rassmussen for invaluable guidance and criticisms of this work, and Dr. Robert DeLorenzo for the use of his Loats two-dimensional digitizing analyzer. This work was supported by a grant from the Veterans Administration to I.M.M.

PY - 1987/4

Y1 - 1987/4

N2 - Histamine-stimulated phosphorylation was studied in isolated rabbit parietal cells. Secretion of acid, as assessed by aminopyrine uptake, was linear at 15 min of stimulation with histamine. By utilizing two dimensional gels, a specific 30,000-Da protein (pp30) was identified whose phosphorylation was prominently stimulated by histamine after 15 min of incubation. The pp30 protein displayed an isoelectric point of 6.0. Furthermore, cAMP-dependent pp30 phosphorylation could also be demonstrated in vitro in a preparation of parietal cell cytosol. The results suggest that pp30 may represent an important histamine-stimulated cAMP-dependent phosphoprotein involved in the initiation or maintenance of parietal cell secretion.

AB - Histamine-stimulated phosphorylation was studied in isolated rabbit parietal cells. Secretion of acid, as assessed by aminopyrine uptake, was linear at 15 min of stimulation with histamine. By utilizing two dimensional gels, a specific 30,000-Da protein (pp30) was identified whose phosphorylation was prominently stimulated by histamine after 15 min of incubation. The pp30 protein displayed an isoelectric point of 6.0. Furthermore, cAMP-dependent pp30 phosphorylation could also be demonstrated in vitro in a preparation of parietal cell cytosol. The results suggest that pp30 may represent an important histamine-stimulated cAMP-dependent phosphoprotein involved in the initiation or maintenance of parietal cell secretion.

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DO - 10.1016/0022-4804(87)90168-5

M3 - Article

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AN - SCOPUS:0023255636

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VL - 42

SP - 348

EP - 353

JO - Journal of Surgical Research

JF - Journal of Surgical Research

IS - 4

ER -

A specific histamine-stimulated phosphoprotein in isolated parietal cells

Abstract

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