Evidence map›Paper›PMID 30869121›Full record

ArticleGlycobiology2019

Establishment and characterization of Drosophila cell lines mutant for heparan sulfate modifying enzymes.

Eriko Nakato, Xin Liu, Inger Eriksson, Maki Yamamoto, Akiko Kinoshita-Toyoda, Hidenao Toyoda, Lena Kjellén, Jin-Ping Li, Hiroshi Nakato

Abstract read
In one paragraph

Article in Glycobiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. The Pathophysiological Functions of Heparanases: From Evolution, Structural and Tissue-Specific Perspectives.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
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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

9 authors.

Eriko NakatoFrom the Department of Genetics, Cell Biology and Development, University of Minnesota, 6-160 Jackson Hall, 321 Church St SE, Minneapolis, MN, USA.
Xin LiuDepartment of Medical Biochemistry and Microbiology, Husargatan 3, 75123 Uppsala University, Uppsala, Sweden.
Inger ErikssonDepartment of Medical Biochemistry and Microbiology, Husargatan 3, 75123 Uppsala University, Uppsala, Sweden.
Maki YamamotoFaculty of Pharmaceutical Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga, Japan.
Akiko Kinoshita-ToyodaFaculty of Pharmaceutical Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga, Japan.
Hidenao ToyodaFaculty of Pharmaceutical Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga, Japan.
Lena KjellénDepartment of Medical Biochemistry and Microbiology, Husargatan 3, 75123 Uppsala University, Uppsala, Sweden.
Jin-Ping LiDepartment of Medical Biochemistry and Microbiology, Husargatan 3, 75123 Uppsala University, Uppsala, Sweden.
Hiroshi NakatoFrom the Department of Genetics, Cell Biology and Development, University of Minnesota, 6-160 Jackson Hall, 321 Church St SE, Minneapolis, MN, USA.

Funding

Heparan sulfate proteoglycans in signaling and developmentR35GM131688 · NIGMS · UNIVERSITY OF MINNESOTA · PI Hiroshi Nakato · 2019 to 2026
$2.6M
Genetic Study of Heparan Sulfate Function in DevelopmentR01GM115099 · NIGMS · UNIVERSITY OF MINNESOTA · PI NAKATO, HIROSHI · 2015 to 2018
$1.2M
NIGMS NIH HHS R01 GM115099NIGMS NIH HHS R35 GM131688
6 · The paper itself

Abstract

A class of carbohydrate-modified proteins, heparan sulfate proteoglycans (HSPGs), play critical roles both in normal development and during disease. Genetic studies using a model organism, Drosophila, have been contributing to understanding the in vivo functions of HSPGs. Despite the many strengths of the Drosophila model for in vivo studies, biochemical analysis of Drosophila HS is somewhat limited, mainly due to the insufficient amount of the material obtained from the animal. To overcome this obstacle, we generated mutant cell lines for four HS modifying enzymes that are critical for the formation of ligand binding sites on HS, Hsepi, Hs2st, Hs6st and Sulf1, using a recently established method. Morphological and immunological analyses of the established lines suggest that they are spindle-shaped cells of mesodermal origin. The disaccharide profiles of HS from these cell lines showed characteristics of lack of each enzyme as well as compensatory modifications by other enzymes. Metabolic radiolabeling of HS allowed us to assess chain length and net charge of the total population of HS in wild-type and Hsepi mutant cell lines. We found that Drosophila HS chains are significantly shorter than those from mammalian cells. BMP signaling assay using Hs6st cells indicates that molecular phenotypes of these cell lines are consistent with previously known in vivo phenomena. The established cell lines will provide us with a direct link between detailed structural information of Drosophila HS and a wealth of knowledge on biological phenotypic data obtained over the last two decades using this animal model.

Indexed as

Cell LineDrosophila melanogasterMutationAnimalsCarbohydrate EpimerasesDrosophila ProteinsHeparan Sulfate ProteoglycansPhenotypeSulfatasesSulfotransferasesCarbohydrate EpimerasesDrosophila Proteinsheparan-sulfate 2-sulfotransferaseheparan sulfate 6-O-sulfotransferaseheparan sulfate C5-epimerase, DrosophilaHeparan Sulfate ProteoglycansSULF1 protein, DrosophilaSulfatasesSulfotransferasescell cultureDrosophilaheparan sulfatemutant

Identifiers

PMID30869121
PMCPMC6521943

What OpenQuestion holds

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Registered trials

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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.