Evidence map›Paper›PMID 18483181›Full record

ArticleAmerican journal of physiology. Gastrointestinal and liver physiology2008

Targeted disruption of the Lasp-1 gene is linked to increases in histamine-stimulated gastric HCl secretion.

Catherine S Chew, Xunsheng Chen, Roni J Bollag, Carlos Isales, Ke Hong Ding, Han Zhang

Abstract read
In one paragraph

Article in American journal of physiology. Gastrointestinal and liver physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.2field-weighted citation impact, top 24% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 29 citations in OpenAlex.

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  17. Update on the mechanisms of gastric acid secretion.Current gastroenterology reports · 2010
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 5 institutions in 3 countries.

Catherine S ChewInstitute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, GA 30912-3175, USA. cchew@mcg.edu
Xunsheng Chen
Roni J Bollag
Carlos Isales
Ke Hong Ding
Han Zhang
Augusta University · USAugusta University Health · USCenter for Neuroscience and Regenerative Medicine · USEndocrinology Research Center · RUWuhan University · CN

Funding

GASTRIC H+ ION TRANSPORT-CELLULAR CONTROL MECHANSIMSR01DK031900 · NIDDK · MOREHOUSE SCHOOL OF MEDICINE · PI CHEW, CATHERINE S · 1986 to 2008
$2.3M
GASTRIC HYDROGEN TRANSPORT--CELLULAR CONTROL MECHANISMSR37DK031900 · NIDDK · MOREHOUSE SCHOOL OF MEDICINE · PI CHEW, CATHERINE S · 1992 to 1999
–
NIDDK NIH HHS DK31900
6 · The paper itself

Abstract

Lasp-1 (LIM and SH3 domain protein 1) is a multidomain actin-binding protein that is differentially expressed within epithelial tissues and brain. In the gastric mucosa, Lasp-1 is highly expressed in the HCl-secreting parietal cell, where it is prominently localized within the F-actin-rich subcellular regions. Histamine-induced elevation of parietal cell [cAMP]i increases Lasp-1 phosphorylation, which is correlated with activation of HCl secretion. To determine whether Lasp-1 is involved in the regulation of HCl secretion in vivo, we generated a murine model with a targeted disruption of the Lasp-1 gene. Lasp-1-null mice had slightly lower body weights but developed normally and had no overt phenotypic abnormalities. Basal HCl secretion was unaffected by loss of Lasp-1, but histamine stimulation induced a more robust acid secretory response in Lasp-1-null mice compared with wild-type littermates. A similar effect of histamine was observed in isolated gastric glands on the basis of measurements of accumulation of the weak base [14C]aminopyrine. In addition, inhibition of the acid secretory response to histamine by H2 receptor blockade with ranitidine proceeded more slowly in glands from Lasp-1-null mice. These findings support the conclusion that Lasp-1 is involved in the regulation of parietal HCl secretion. We speculate that cAMP-dependent phosphorylation of Lasp-1 alters interactions with F-actin and/or endocytic proteins that interact with Lasp-1, thereby regulating the trafficking/activation of the H+, K+-ATPase (proton pump).

Indexed as

AgingAnimalsCytoskeletal ProteinsFemaleGastric AcidGastric MucosaGene DeletionHistamineHomeodomain ProteinsLIM Domain ProteinsMaleMiceMice, Inbred C57BLNeoplasm ProteinsOsteoclastsCytoskeletal ProteinsHistamineHomeodomain ProteinsLasp1 protein, mouseLIM Domain ProteinsNeoplasm Proteins

Identifiers

PMID18483181
PMCPMC2494726
OpenAlexW2106623386

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.