Evidence map›Paper›PMID 2444218›Full record

ArticleThe Biochemical journal1987

Production and characterization of monoclonal antibodies to insulin secretory granule membranes.

K A Grimaldi, J C Hutton, K Siddle

Abstract read
In one paragraph

Article in The Biochemical journal, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
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  11. Endocytosis of activated TrkA: evidence that nerve growth factor induces formation of signaling endosomes.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1996
    Article
  12. Article
  13. Review
  14. Sorting and processing of secretory proteins.The Biochemical journal · 1994
    Review
  15. Article
  16. Article
  17. Article
  18. The insulin secretory granule.Diabetologia · 1989
    Review
  19. Article
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

3 authors.

K A GrimaldiDepartment of Clinical Biochemistry, University of Cambridge, Addenbrooke's Hospital, U.K.
J C Hutton
K Siddle

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Monoclonal antibodies to insulin secretory granule membranes were obtained following immunization of mice with granule membranes purified from a rat transplantable insulinoma. The specificities of the antibodies were investigated by using binding assays with different insulinoma subcellular fractions, by indirect immunofluorescence studies with intact and permeabilized cells, and by immunoblotting of granule membrane proteins fractionated by SDS/polyacrylamide-gel electrophoresis. Fifty-six antibodies were characterized initially, and 21 representative cell lines were cloned. The antibodies fell into four categories: (1) binding preferentially to secretory granules, and reacting with a component of approx. 80,000 Da on immunoblots (antigen designated SGM 80); (2) binding preferentially to secretory granules, and reacting with components of approx. 110,000 and 50,000 Da on immunoblots (antigen designated SGM 110); (3) binding preferentially to secretory granules but unreactive on immunoblots; (4) binding to membrane antigen(s) with a widespread intracellular distribution which included granules and plasma membranes. The antigens SGM 80 and SGM 110 were studied in more detail and both were shown to be integral membrane glycoproteins with antigenic determinants located on the internal face of the secretory granule membrane. These antigens were also present in normal rat islets of Langerhans and similar components were detected by immunoblotting in secretory granules from anterior pituitary and adrenal medulla. Proteins which were immunologically related to SGM 80 and SGM 110, but distinct in molecular size, were also identified in liver. It is concluded that secretory granules contain specific components which are restricted in subcellular location but widespread in tissue distribution. The antibodies obtained will be valuable reagents in the further investigation of the biogenesis and turnover of insulin secretory granules.

Indexed as

Adenoma, Islet CellAnimalsAntibodies, MonoclonalAntibody SpecificityAntigens, NeoplasmBinding SitesCytoplasmic GranulesElectrophoresis, Polyacrylamide GelEpitopesGlycosylationImmunoelectrophoresisInsulinInsulinomaInsulin SecretionMembrane GlycoproteinsPancreatic NeoplasmsAntibodies, MonoclonalAntigens, NeoplasmEpitopesInsulininsulin secretory granule membrane glycoprotein 110Membrane Glycoproteins

Identifiers

PMID2444218
PMCPMC1148158

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.