Evidence map›Paper›PMID 1531535›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1992

GP-2/THP gene family encodes self-binding glycosylphosphatidylinositol-anchored proteins in apical secretory compartments of pancreas and kidney.

S Fukuoka, S D Freedman, H Yu, V P Sukhatme, G A Scheele

Erratum issuedOpen access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

25 citing papers in PubMed, 96 citations in OpenAlex.

  1. Review
  2. Glycoprotein 2 in health and disease: lifting the veil.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2021
    Review
  3. Review
  4. Article
  5. Review
  6. Signal transduction and chemotaxis in mast cells.European journal of pharmacology · 2016
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. A duplicated motif controls assembly of zona pellucida domain proteins.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  14. New concepts in understanding the pathophysiology of chronic pancreatitis.International journal of pancreatology : official journal of the International Association of Pancreatology · 1998
    Review
  15. Article
  16. Article
  17. Article
  18. The pathogenesis of chronic pancreatitis.Postgraduate medical journal · 1995
    Review
  19. A 92-kDa human immunostimulatory protein.Proceedings of the National Academy of Sciences of the United States of America · 1994
    Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

S FukuokaLaboratory of Cell and Molecular Biology, Charles A. Dana Research Institute, Thorndike Laboratory, Boston, MA 02215.
S D Freedman
H Yu
V P Sukhatme
G A Scheele
Dana (United States) · US

Funding

MOLECULAR BASIS OF SECRETION IN THE EXOCRINE PANCREASR01DK018532 · NIDDK · ROCKEFELLER UNIVERSITY · PI SCHEELE, GEORGE A · 1986 to 1995
–
NIDDK NIH HHS DDK-18532-17
6 · The paper itself

Abstract

A family of homologous genes is shown to encode GP-2, the major glycosylphosphatidylinositol (GPI)-linked glycoprotein of pancreatic zymogen granule membranes, and Tamm-Horsfall protein (THP), a GPI-linked glycoprotein associated with apical vesicles in kidney thick ascending limb of Henle (TALH) cells. The C-terminal regions of GP-2 (Asp54-Phe530) and THP (Asp175-His644) from rat show 53% identity, 86% similarity, and 26 conserved cysteine residues including one epidermal growth factor motif. The unique N-terminal domain of rat THP (unique-THP, Pro29-Gln174) shows four conserved epidermal growth factor motifs, three in tandem and one in reverse orientation. GP-2 homologues are observed in a wide variety of epithelial cells, several of which contain highly regulated secretory processes. GP-2 released from zymogen granule membranes with phosphatidylinositol phospholipase C reacts with anti-cross-reactive determinant antibody (anti-CRD), confirming the GPI nature of the pancreatic homologue. In contrast, GP-2 and THP, released endogenously from pancreas and kidney, respectively, do not react with anti-cross-reactive determinant antibody, suggesting alternative enzymatic mechanisms for their physiological release. Globular domains of GP-2 and THP, but not albumin, show pH- and ion-dependent self-association in vitro. The GP-2/THP family appears to represent a newly discovered class of GPI-anchored proteins, which may utilize pH- and ion-dependent self-association mechanisms for establishing membrane (micro)domains targeted to intracellular secretory compartments.

Indexed as

Amino Acid SequenceAnimalsCells, CulturedDNADogsGene ExpressionGlycolipidsGlycosylphosphatidylinositolsHumansHydrogen-Ion ConcentrationKidneyMacromolecular SubstancesMembrane GlycoproteinsMolecular Sequence DataMucoproteinsMultigene FamilyDNAGlycolipidsglycoprotein-2, pancreasGlycosylphosphatidylinositolsMacromolecular SubstancesMembrane GlycoproteinsMucoproteinsPhosphatidylinositolsRNA, MessengerUMOD protein, humanUmod protein, ratUromodulin

Identifiers

PMID1531535
PMCPMC48414
OpenAlexW2066090262

What OpenQuestion holds

Textmetadata
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.