Evidence map›Paper›PMID 18396408›Full record

ReviewCritical reviews in oncology/hematology2008

Cathepsin D--many functions of one aspartic protease.

Petr Benes, Vaclav Vetvicka, Martin Fusek

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in oncology/hematology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 296 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
296citing papers in PubMed, 1 pooled it
12.0field-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

296 citing papers in PubMed, 1 synthesis or guideline pooled it, 636 citations in OpenAlex.

  1. Pooled it
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  15. Design and Preclinical Evaluation of FirstJournal of medicinal chemistry · 2025
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236 more citing papers are in PubMed but not listed here.

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.

Petr BenesLaboratory of Cell Differentiation, Department of Experimental Biology, Faculty of Science, Masaryk University, ILBIT A3, Kamenice 3, Brno 625 00, Czech Republic. pbenes@sci.muni.cz
Vaclav Vetvicka
Martin Fusek
Czech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZMasaryk University · CZ

Funding

Regulation of breast cancer growth by activation peptideR01CA082159 · NCI · UNIVERSITY OF LOUISVILLE · PI VETVICKA, VACLAV · 2002 to 2006
$1.1M
NCI NIH HHS R01 CA082159
6 · The paper itself

Abstract

For years, it has been held that cathepsin D (CD) is involved in rather non-specific protein degradation in a strongly acidic milieu of lysosomes. Studies with CD knock-out mice revealed that CD is not necessary for embryonal development, but it is indispensable for postnatal tissue homeostasis. Mutation that abolishes CD enzymatic activity causes neuronal ceroid lipofuscinosis (NCL) characterized by severe neurodegeneration, developmental regression, visual loss and epilepsy in both animals and humans. In the last decade, however, an increasing number of studies demonstrated that enzymatic function of CD is not restricted solely to acidic milieu of lysosomes with important consequences in regulation of apoptosis. In addition to CD enzymatic activity, it has been shown that apoptosis is also regulated by catalytically inactive mutants of CD which suggests that CD interacts with other important molecules and influences cell signaling. Moreover, procathepsin D (pCD), secreted from cancer cells, acts as a mitogen on both cancer and stromal cells and stimulates their pro-invasive and pro-metastatic properties. Numerous studies found that pCD/CD level represents an independent prognostic factor in a variety of cancers and is therefore considered to be a potential target of anti-cancer therapy. Studies dealing with functions of cathepsin D are complicated by the fact that there are several simultaneous forms of CD in a cell-pCD, intermediate enzymatically active CD and mature heavy and light chain CD. It became evident that these forms may differently regulate the above-mentioned processes. In this article, we review the possible functions of CD and its various forms in cells and organisms during physiological and pathological conditions.

Indexed as

Alzheimer DiseaseAnimalsAntineoplastic AgentsApoptosisAtherosclerosisBiomarkers, TumorCathepsin DEnzyme PrecursorsHumansIsoenzymesMiceMice, TransgenicNeoplasmsProtease InhibitorsTreatment OutcomeAntineoplastic AgentsBiomarkers, TumorCathepsin DEnzyme PrecursorsIsoenzymesProtease Inhibitors

Identifiers

PMID18396408
PMCPMC2635020
OpenAlexW2112355597

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.