Evidence map›Paper›PMID 18329945›Full record

ReviewThe international journal of biochemistry & cell biology2008

Leukocyte cell surface proteinases: regulation of expression, functions, and mechanisms of surface localization.

Caroline A Owen

Open access · greenAbstract readReview
In one paragraph

Review in The international journal of biochemistry & cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed, 1 pooled it
3.7field-weighted citation impact, top 6% 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

30 citing papers in PubMed, 1 synthesis or guideline pooled it, 79 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Review
  5. Article
  6. Article
  7. ADAM15 expression is increased in lung CD8Respiratory research · 2020
    Article
  8. Alpha-1 Antitrypsin Deficiency: Have We Got the Right Proteinase?Chronic obstructive pulmonary diseases (Miami, Fla.) · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. An agonist antibody that blocks autoimmunity by inducing anti-inflammatory macrophages.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Article
  18. Matrix metalloproteinases as therapeutic targets for idiopathic pulmonary fibrosis.American journal of respiratory cell and molecular biology · 2015
    Review
  19. Article
  20. Proteases, neutrophils, and periodontitis: the NET effect.The Journal of clinical investigation · 2014
    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

1 author at 1 institution in 1 country.

Caroline A OwenDivision of Pulmonary and Critical Care Medicine, Brigham and Women's Hospital and Harvard Medical School, 905 Thorn Building, 75 Francis Street, Boston, MA 02115, United States. cowen@rics.bwh.harvard.edu
Brigham and Women's Hospital · US

Funding

Novel Roles for MMP-8 in Acute Lung InjuryR01HL063137 · NHLBI · UNIVERSITY OF UTAH · PI OWEN, CAROLINE A · 1999 to 2008
$2.6M
Novel Roles for ADAM15 in Acute Lung InjuryR01HL086814 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI OWEN, CAROLINE A · 2007 to 2010
$1.6M
NHLBI NIH HHS R01 HL063137NHLBI NIH HHS R01 HL086814
6 · The paper itself

Abstract

A number of proteinases are expressed on the surface of leukocytes including members of the serine, metallo-, and cysteine proteinase superfamilies. Some proteinases are anchored to the plasma membrane of leukocytes by a transmembrane domain or a glycosyl phosphatidyl inositol (GPI) anchor. Other proteinases bind with high affinity to classical receptors, or with lower affinity to integrins, proteoglycans, or other leukocyte surface molecules. Leukocyte surface levels of proteinases are regulated by: (1) cytokines, chemokines, bacterial products, and growth factors which stimulate synthesis and/or release of proteinases by cells; (2) the availability of surface binding sites for proteinases; and/or (3) internalization or shedding of surface-bound proteinases. The binding of proteinases to leukocyte surfaces serves many functions including: (1) concentrating the activity of proteinases to the immediate pericellular environment; (2) facilitating pro-enzyme activation; (3) increasing proteinase stability and retention in the extracellular space; (4) regulating leukocyte function by proteinases signaling through cell surface binding sites or other surface proteins; and (5) protecting proteinases from inhibition by extracellular proteinase inhibitors. There is strong evidence that membrane-associated proteinases on leukocytes play critical roles in wound healing, inflammation, extracellular matrix remodeling, fibrinolysis, and coagulation. This review will outline the biology of membrane-associated proteinases expressed by leukocytes and their roles in physiologic and pathologic processes.

Indexed as

Gene Expression Regulation, EnzymologicAnimalsHumansLeukocytesMembrane ProteinsPeptide HydrolasesMembrane ProteinsPeptide Hydrolases

Identifiers

PMID18329945
PMCPMC2425676
OpenAlexW1989073297

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.