Evidence map›Paper›PMID 31478242›Full record

ArticleJournal of cellular biochemistry2020

α-Amylase expressed in human small intestinal epithelial cells is essential for cell proliferation and differentiation.

Kimie Date, Tomomi Yamazaki, Yoko Toyoda, Kumi Hoshi, Haruko Ogawa

Open access · hybridAbstract read
In one paragraph

Article in Journal of cellular biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
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  5. Journal of diabetes and metabolic disorders · 2024
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  7. Article
  8. Article
  9. Review
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  11. Review
  12. [A Systematic Approach to Patients with Elevated Levels of Serum Amylase or Lipase].The Korean journal of gastroenterology = Taehan Sohwagi Hakhoe chi · 2023
    Review
  13. Effect of α-Amylase on the Structure of Chia Seed Mucilage.Biomimetics (Basel, Switzerland) · 2022
    Article
  14. Article
  15. Article
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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

5 authors at 2 institutions in 1 country.

Kimie DateInstitute for Human Life Innovation, Ochanomizu University, Ohtsuka, Bunkyo-ku, Tokyo, Japan.ORCID 0000-0003-4311-0544
Tomomi YamazakiNational Institute of Health and Nutrition, National Institutes of Biomedical Innovation, Health and Nutrition, Toyama, Shinjuku-ku, Tokyo, Japan.ORCID 0000-0003-4973-9140
Yoko ToyodaGraduate School of Humanities and Sciences, Ochanomizu University, Ohtsuka, Bunkyo-ku, Tokyo, Japan.
Kumi HoshiGraduate School of Humanities and Sciences, Ochanomizu University, Ohtsuka, Bunkyo-ku, Tokyo, Japan.
Haruko OgawaInstitute for Human Life Innovation, Ochanomizu University, Ohtsuka, Bunkyo-ku, Tokyo, Japan.
Ochanomizu University · JPNational Institute of Infectious Diseases · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Amylase, which plays an essential role in starch degradation, is expressed mainly in the pancreas and salivary glands. Human α-amylase is also detected in other tissues, but it is unclear whether the α-amylase is endogenously expressed in each tissue or mixed exogenously with one expressed by the pancreas or salivary glands. Furthermore, the biological significance of these α-amylases detected in tissues other than the pancreas and salivary glands has not been elucidated. We discovered that human α-amylase is expressed in intestinal epithelial cells and analyzed the effects of suppressing α-amylase expression. α-Amylase was found to be expressed at the second-highest messenger RNA level in the duodenum in human normal tissues after the pancreas. α-Amylase was detected in the cell extract of Caco-2 intestinal epithelial cells but not secreted into the culture medium. The amount of α-amylase expressed increased depending on the length of the culture of Caco-2 cells, suggesting that α-amylase is expressed in small intestine epithelial cells rather than the colon because the cells differentiate spontaneously upon reaching confluence in culture to exhibit the characteristics of small intestinal epithelial cells rather than colon cells. The α-amylase expressed in Caco-2 cells had enzymatic activity and was identified as AMY2B, one of the two isoforms of pancreatic α-amylase. The suppression of α-amylase expression by small interfering RNA inhibited cell differentiation and proliferation. These results demonstrate for the first time that α-amylase is expressed in human intestinal epithelial cells and affects cell proliferation and differentiation. This α-amylase may induce the proliferation and differentiation of small intestine epithelial cells, supporting a rapid turnover of cells to maintain a healthy intestinal lumen.

Indexed as

Caco-2 CellsCell DifferentiationCell ProliferationEpithelial CellsGene ExpressionHumansIntestine, SmallPancreasPancreatic alpha-AmylasesRNA InterferenceRNA, MessengerSalivary alpha-AmylasesSalivary GlandsTransfectionAMY1A protein, humanAMY2A protein, humanAMY2B protein, humanPancreatic alpha-AmylasesRNA, MessengerSalivary alpha-Amylasescaco-2 cellsdifferentiationexpressionproliferationsmall intestineα-amylase

Identifiers

PMID31478242
PMCPMC6973164
OpenAlexW2972113525

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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.