Evidence map›Paper›PMID 18487610›Full record

ArticleThe Journal of biological chemistry2008

Mapping of SPARC/BM-40/osteonectin-binding sites on fibrillar collagens.

Camilla Giudici, Nicolas Raynal, Hanna Wiedemann, Wayne A Cabral, Joan C Marini, Rupert Timpl, Hans Peter Bächinger, Richard W Farndale, Takako Sasaki, Ruggero Tenni

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
6.6field-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

53 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Triple Helical-Peptides: Collagen-Mimicking Tools for Tissue Engineering.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  3. Article
  4. Article
  5. Lung extracellular matrix modulates KRT5Nature communications · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Prokaryotic Collagen-Like Proteins as Novel Biomaterials.Frontiers in bioengineering and biotechnology · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

10 authors at 4 institutions in 4 countries.

Camilla GiudiciMax-Planck-Institut für Biochemie, Am Klopferspitz 18, 82152 Martinsried, Germany.
Nicolas Raynal
Hanna Wiedemann
Wayne A Cabral
Joan C Marini
Rupert Timpl
Hans Peter Bächinger
Richard W Farndale
Takako Sasaki
Ruggero Tenni
Oregon Health & Science University · USNational Institutes of Health · USUniversity of Cambridge · GBUniversity of Pavia · IT

Funding

Heritable Disorders Of Connective TissueZIAHD000408 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI MARINI, JOAN C · 2009 to 2023
$13.4M
PATHOPHYSIOLOGY AND TREATMENT OF HUMAN GENETIC DISEASESZ01HD000408 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI MARINI, JOAN C · 1985 to 2008
$1.8M
Medical Research Council G0400701Wellcome Trust
6 · The paper itself

Abstract

The 33-kDa matrix protein SPARC (BM-40, osteonectin) binds several collagen types with moderate affinity. The collagen-binding site resides in helix alphaA of the extracellular calcium-binding domain of SPARC and is partially masked by helix alphaC. Previously, we found that the removal of helix alphaC caused a 10-fold increase in the affinity of SPARC for collagen, and we identified amino acids crucial for binding by site-directed mutagenesis. In this study, we used rotary shadowing, CNBr peptides, and synthetic peptides to map binding sites of SPARC onto collagens I, II, and III. Rotary shadowing and electron microscopy of SPARC-collagen complexes identified a major binding site approximately 180 nm from the C terminus of collagen. SPARC binding was also detected with lower frequency near the matrix metalloproteinase cleavage site. These data fit well with our analysis of SPARC binding to CNBr peptides, denaturation of which abolished binding, indicating triple-helical conformation of collagen to be essential. SPARC binding was substantially decreased in two of seven alpha2(I) mutant procollagen I samples and after N-acetylation of Lys/Hyl side chains in wild-type collagen. Synthetic peptides of collagen III were used to locate the binding sites, and we found SPARC binding activity in a synthetic triple-helical peptide containing the sequence GPOGPSGPRGQOGVMGFOGPKGNDGAO (where O indicates 4-hydroxyproline), with affinity for SPARC comparable with that of procollagen III. This sequence is conserved among alpha chains of collagens I, II, III, and V. In vitro collagen fibrillogenesis was delayed in the presence of SPARC, suggesting that SPARC might modulate collagen fibril assembly in vivo.

Indexed as

Peptide MappingAcetylationAnimalsBinding SitesCattleFibrillar CollagensHumansHydroxyprolineMutationOsteonectinPeptidesProtein BindingProtein Structure, SecondaryFibrillar CollagensHydroxyprolineOsteonectinPeptides

Identifiers

PMID18487610
PMCPMC2443679
OpenAlexW2152905528

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.