Evidence map›Paper›PMID 6093995›Full record

ReviewCancer metastasis reviews1984

Cysteine proteinases and metastasis.

B F Sloane, K V Honn

Abstract readReview
PubMed Publisher
In one paragraph

Review in Cancer metastasis reviews, 1984. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

51 citing papers in PubMed, 216 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Proteomic analysis of seminal fluid from men exhibiting oxidative stress.Reproductive biology and endocrinology : RB&E · 2013
    Article
  10. Article
  11. Matrix metalloproteinases in cytotoxic lymphocytes impact on tumour infiltration and immunomodulation.Cancer microenvironment : official journal of the International Cancer Microenvironment Society · 2011
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Cathepsin B in the rat eye.Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie · 2003
    Article
  19. Brain-metastatic melanoma: a neurotrophic perspective.Pathology oncology research : POR · 2003
    Review
  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

2 authors at 1 institution in 1 country.

B F Sloane
K V Honn
Wayne State University · US

Funding

CATHEPSIN B-LIKE CYSTEINE PROTEINASES AND TUMOR INVASIONR01CA036481 · NCI · WAYNE STATE UNIVERSITY · PI SLOANE, BONNIE F · 1985 to 2005
$1.7M
THROMBOXANES: ROLE IN TUMOR GROWTH AND METASTASISR01CA029997 · NCI · WAYNE STATE UNIVERSITY · PI HONN, KENNETH V · 1985 to 2008
$1.7M
NCI NIH HHS CA29997NCI NIH HHS CA36481
6 · The paper itself

Abstract

Cysteine proteinases are a subclass of endopeptidases which require activation by thiol reagents. A tumor cysteine proteinase which appears to be related to lysosomal cathepsin B has been implicated in the ability of tumor cells to invade the extracellular matrix and to metastasize to secondary sites. Lysosomal cathepsin B can degrade such components of the extracellular matrix as collagen, fibronectin and proteoglycans. Activity of this cathepsin B-like cysteine proteinase (CB) has been correlated with tumor malignancy in a number of tumor lines yet not in all tumor lines studied. CB activity in tumors seems to be associated with the viable tumor cells, probably with the plasma membrane of these tumor cells. CB activity has been measured in the sera, urine, ascites fluid and pancreatic fluid of tumor-bearing patients. CB is released from tumor explants and tumor cells in vitro as well as from normal subcutaneous tissue exposed to tumor-conditioned medium. Cathepsin B from normal tissues is rapidly inactivated above pH 7.0. Therefore, CB in tumor cell membranes or released from tumor cells (or from host cells in response to tumor cells) may not possess proteolytic activity at neutral pH and thus may not facilitate tumor cell invasion. However, CB exhibits enhanced stability at neutral or slightly alkaline pH's. There is not yet definitive proof that CB plays a role in tumor invasion and metastasis. There is, however, an increasing body of correlative evidence relating CB activity and tumor malignancy. This correlative evidence plus preliminary evidence that tumor CB can degrade components of the extracellular matrix in vitro suggests that CB may be one proteinase active in a proteolytic cascade resulting in tumor invasion and metastasis.

Indexed as

AnimalsCathepsin BCathepsinsCell MembraneCell MovementCells, CulturedCysteine EndopeptidasesEndopeptidasesHumansLysosomesMicrobial CollagenaseNeoplasm MetastasisNeoplasmsCathepsin BCathepsinsCysteine EndopeptidasesEndopeptidasesMicrobial Collagenase

Identifiers

PMID6093995
OpenAlexW1999808993

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.