Evidence map›Paper›PMID 9854027›Full record

ArticleThe Biochemical journal1999

Age-related changes in the synthesis of link protein and aggrecan in human articular cartilage: implications for aggregate stability.

M C Bolton, J Dudhia, M T Bayliss

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Regulatory mechanisms and clinical manifestations of musculoskeletal aging.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2019
    Review
  5. Review
  6. Article
  7. Review
  8. Events in articular chondrocytes with aging.Current osteoporosis reports · 2011
    Review
  9. Ultrasonic probe is useful for in vivo quantitative assessment of medial femoral condyle articular cartilage.Knee surgery, sports traumatology, arthroscopy : official journal of the ESSKA · 2011
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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 at 2 institutions in 1 country.

M C BoltonThe Kennedy Institute of Rheumatology, 1 Aspenlea Road, Hammersmith, London W6 8LH, U.K.
J Dudhia
M T Bayliss
Royal Veterinary College · GBHammersmith Hospital · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The rates of incorporation of radiolabelled leucine into aggrecan and link protein have been measured in human articular cartilage of different ages. Aggrecan and link protein were purified in the A1 fraction of CsCl gradients as a result of their ability to form high-buoyant-density proteoglycan aggregates with hyaluronic acid. Separation of the aggrecan from the link protein was achieved by Mono Q anion-exchange chromatography. The rates of synthesis of both aggrecan and link protein decreased with age. The age-related decrease in synthesis of aggrecan was paralleled by a decrease in the rate of sulphate incorporation into glycosaminoglycan chains. The synthesis of link protein decreased with age to a greater extent than that of aggrecan such that the ratio of the rates of link protein to aggrecan synthesis decreased from 1 in immature cartilage to 0.2 in mature cartilage. The age-related decrease in link protein synthesis is controlled at least in part by transcriptional or post-transcriptional mechanisms, as shown by the accompanying age-related decrease in link-protein mRNA. The absence of any age-related decrease in aggrecan mRNA suggests that the decrease in synthesis of aggrecan core protein is controlled by a translational mechanism. Measurement of the total tissue content of aggrecan and link protein by radioimmunoassay revealed an age-related increase in the accumulation of these matrix proteins, even though their de novo synthesis was decreasing. This illustrates the importance that the regulation of extracellular post-translational modification also has in controlling the overall turnover of the cartilage matrix.

Indexed as

Extracellular Matrix ProteinsProtein BiosynthesisAdolescentAdultAgedAggrecansAgingCartilage, ArticularChildHumansKineticsLectins, C-TypeLeucineMiddle AgedProteinsProteoglycan Link ProteinAggrecansExtracellular Matrix ProteinsLectins, C-TypeLeucineProteinsProteoglycan Link ProteinProteoglycansRNA, Messenger

Identifiers

PMID9854027
PMCPMC1219938
OpenAlexW2108740080

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.