Evidence map›Paper›PMID 3922993›Full record

ArticleThe Journal of cell biology1985

Glycoproteins of the lysosomal membrane.

V Lewis, S A Green, M Marsh, P Vihko, A Helenius, I Mellman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1985. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
8.8field-weighted citation impact, top 1% 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

108 citing papers in PubMed, 300 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Lysosome quality control in health and neurodegenerative diseases.Cellular & molecular biology letters · 2024
    Review
  12. Article
  13. Endocytosis in anaerobic parasitic protists.Memorias do Instituto Oswaldo Cruz · 2024
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

48 more citing papers are in PubMed but not listed here.

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.

V Lewis
S A Green
M Marsh
P Vihko
A Helenius
I Mellman

Funding

MOLECULAR SORTING DURING INTRACELLULAR TRANSPORTR01GM029765 · NIGMS · YALE UNIVERSITY · PI MELLMAN, IRA S · 1985 to 2006
$2.6M
NIGMS NIH HHS GM-29765PHS HHS AL-18582PHS HHS AL-18599
6 · The paper itself

Abstract

Three glycoprotein antigens (120, 100, and 80 kD) were detected by mono- and/or polyclonal antibodies generated by immunization with highly purified rat liver lysosomal membranes. All of the antigens were judged to be integral membrane proteins based on the binding of Triton X-114. By immunofluorescence on normal rat kidney cells, a mouse monoclonal antibody to the 120-kD antigen co-stained with a polyclonal rabbit antibody that detected the 100- and 80-kD antigens as well as with antibodies to acid phosphatase, indicating that these antigens are preferentially localized in lysosomes. Few 120-kD-positive structures were found to be negative for acid phosphatase, suggesting that the antigen was not concentrated in organelles such as endosomes, which lack acid phosphatase. Immunoperoxidase cytochemistry also showed little reactivity in Golgi cisternae, coated vesicles, or on the plasma membrane. Digestion with endo-beta-N-acetylglucosaminidase H (Endo H) and endo-beta-N-acetylglucosaminidase F (Endo F) demonstrated that each of the antigens contained multiple N-linked oligosaccharide chains, most of which were of the complex (Endo H-resistant) type. The 120-kD protein was very heavily glycosylated, having at least 18 N-linked chains. It was also rich in sialic acid, since neuraminidase digestion increased the pI of the 120-kD protein from less than 4 to greater than 8. Taken together, these results strongly suggest that the glycoprotein components of the lysosomal membrane are synthesized in the rough endoplasmic reticulum and terminally glycosylated in the Golgi before delivery to lysosomes. We have provisionally designated these antigens lysosomal membrane glycoproteins lgp120, lgp100, lgp80.

Indexed as

AnimalsAntibodies, MonoclonalAntigensCell LineFemaleFibroblastsFluorescent Antibody TechniqueGlycoproteinsGlycoside HydrolasesImmunoenzyme TechniquesIntracellular MembranesKidneyLysosomesMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMiceMice, Inbred BALB CAntibodies, MonoclonalAntigensGlycoproteinsGlycoside HydrolasesMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseNeuraminidase

Identifiers

PMID3922993
PMCPMC2113609
OpenAlexW2159153404

What OpenQuestion holds

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LicenceCC BY-NC-SA
Read underepoch 390

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.