Evidence map›Paper›PMID 2847914›Full record

ArticleThe EMBO journal1988

Biosynthesis, secretion and extracellular localization of anchorin CII, a collagen-binding protein of the calpactin family.

M Pfäffle, F Ruggiero, H Hofmann, M P Fernández, O Selmin, Y Yamada, R Garrone, K von der Mark

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1988. 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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
20.6field-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

22 citing papers in PubMed, 123 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Annexin A5 is not essential for skeletal development.Molecular and cellular biology · 2003
    Article
  5. Article
  6. Article
  7. Proteins in unexpected locations.Molecular biology of the cell · 1996
    Review
  8. Article
  9. Annexins of plant cells.Plant physiology · 1995
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

M PfäffleMax-Planck-Institut für Biochemie, Department of Connective Tissue Research, Martinsried, FRG.
F Ruggiero
H Hofmann
M P Fernández
O Selmin
Y Yamada
R Garrone
K von der Mark
Max Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The amino acid sequence of anchorin CII, a collagen-binding protein isolated originally from chondrocyte membranes, was previously determined by sequencing of cDNA and proteolytic fragments of the protein. Computer analysis of the protein sequence revealed four internal repeats of approximately 70-80 residues, each containing a highly conserved consensus sequence of 17 residues. These repeats show considerable homology with sequences in human and bovine calpactin, lipocortin, endonexin and protein II, which are members of a family of Ca2+- and phospholipid-binding proteins, as well as major substrates of tyrosine kinases. While these proteins have been located at the inner side of the plasma membrane of fibroblasts and epithelial cells, here we present experimental evidence that anchorin CII is at least partially released from cells and binds to the outer cell surface. Biosynthesis studies in cell-free systems and in cell culture indicate that anchorin CII is not processed, which is consistent with the absence of signal sequences from the protein. Yet, pulse-chase experiments show that anchorin is released into the culture medium of fibroblasts after 30 min, and in chondrocyte cultures after 20 h. Anchorin CII was located to the outer cell surface of chondrocytes by lactoperoxidase-catalyzed cell surface iodination as well as by antibody labeling both at light- and electron-microscopical level. The pericellular localization of anchorin CII is consistent with the notion that this protein is involved in the interaction of chondrocytes and fibroblasts with extracellular collagen.

Indexed as

Amino Acid SequenceAnimalsAnnexin A4AnnexinsCalcium-Binding ProteinsCartilageCell-Free SystemCell MembraneCells, CulturedChick EmbryoCollagenCytoskeletal ProteinsFibroblastsGlycoproteinsImmunohistochemistryMicroscopy, ElectronAnnexin A4AnnexinsCalcium-Binding ProteinsCollagenCytoskeletal ProteinsGlycoproteinsReceptors, Cell SurfaceReceptors, Collagen

Identifiers

PMID2847914
PMCPMC457098
OpenAlexW15342544

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.