ReviewWorld journal of gastroenterology2005
Proteolytic-antiproteolytic balance and its regulation in carcinogenesis.
Review in World journal of gastroenterology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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.
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.
Who cites it
44 citing papers in PubMed, 170 citations in OpenAlex.
- Molecular characterization, expression and immune functional analysis of cystatin 10 in turbot.Molecular biology reports · 2024Article
- Targeting Cathepsin L in Cancer Management: Leveraging Machine Learning, Structure-Based Virtual Screening, and Molecular Dynamics Studies.International journal of molecular sciences · 2023Article
- The Role of Cysteine Protease Cathepsins B, H, C, and X/Z in Neurodegenerative Diseases and Cancer.International journal of molecular sciences · 2023Review
- The roles of proteases in prostate cancer.IUBMB life · 2023Review
- The Role of Cathepsin B in Pathophysiologies of Non-tumor and Tumor tissues: A Systematic Review.Journal of Cancer · 2023Review
- Global Protease Activity Profiling Identifies HER2-Driven Proteolysis in Breast Cancer.ACS chemical biology · 2021Article
- E-cigarettes, nicotine, the lung and the brain: multi-level cascading pathophysiology.The Journal of physiology · 2020Review
- Chronic E-Cigarette Use Increases Neutrophil Elastase and Matrix Metalloprotease Levels in the Lung.American journal of respiratory and critical care medicine · 2019Article
- Sensitive molecular detection of small nodal metastasis in uterine cervical cancer using HPV16-E6/CK19/MUC1 cancer biomarkers.Oncotarget · 2018Article
- Can components of the plasminogen activation system predict the outcome of kidney transplants?Central-European journal of immunology · 2018Review
- The Kunitz Domain I of Hepatocyte Growth Factor Activator Inhibitor-2 Inhibits Matriptase Activity and Invasive Ability of Human Prostate Cancer Cells.Scientific reports · 2017Article
- Addition of 2-(ethylamino)acetonitrile group to nitroxoline results in significantly improved anti-tumor activityOncotarget · 2017Article
- Vitamin D/vitamin D receptor axis regulates DNA repair during oncogene-induced senescence.Oncogene · 2016Article
- A Comparative Study of Cathepsin D Expression in Peripheral and Central Giant Cell Granuloma of the Jaws by Immunohistochemistry Technique.Journal of dentistry (Shiraz, Iran) · 2016Article
- Downregulation of discoidin domain receptor 2 decreases tumor growth of hepatocellular carcinoma.Journal of cancer research and clinical oncology · 2015Article
- Inhibition of cathepsin B activity by 2,3,7,8-tetrachlorodibenzo-p-dioxin.Environmental science and pollution research international · 2015Article
- Differential expression of degradome components in cutaneous squamous cell carcinomas.Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc · 2014Article
- Activity of cathepsin D and α1-antitrypsin in blood of men with malignant melanoma.Postepy dermatologii i alergologii · 2014Article
- IGFBP-4 anti-angiogenic and anti-tumorigenic effects are associated with anti-cathepsin B activity.Neoplasia (New York, N.Y.) · 2013Article
- BRCA1 loss activates cathepsin L-mediated degradation of 53BP1 in breast cancer cells.The Journal of cell biology · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cancer development is essentially a tissue remodeling process in which normal tissue is substituted with cancer tissue. A crucial role in this process is attributed to proteolytic degradation of the extracellular matrix (ECM). Degradation of ECM is initiated by proteases, secreted by different cell types, participating in tumor cell invasion and increased expression or activity of every known class of proteases (metallo-, serine-, aspartyl-, and cysteine) has been linked to malignancy and invasion of tumor cells. Proteolytic enzymes can act directly by degrading ECM or indirectly by activating other proteases, which then degrade the ECM. They act in a determined order, resulting from the order of their activation. When proteases exert their action on other proteases, the end result is a cascade leading to proteolysis. Presumable order of events in this complicated cascade is that aspartyl protease (cathepsin D) activates cysteine proteases (e.g. cathepsin B) that can activate pro-uPA. Then active uPA can convert plasminogen into plasmin. Cathepsin B as well as plasmin are capable of degrading several components of tumor stroma and may activate zymogens of matrix metalloproteinases, the main family of ECM degrading proteases. The activities of these proteases are regulated by a complex array of activators, inhibitors and cellular receptors. In physiological conditions the balance exists between proteases and their inhibitors. Proteolytic-antiproteolytic balance may be of major significance in the cancer development. One of the reasons for such a situation is enhanced generation of free radicals observed in many pathological states. Free radicals react with main cellular components like proteins and lipids and in this way modify proteolytic-antiproteolytic balance and enable penetration damaging cellular membrane. All these lead to enhancement of proteolysis and destruction of ECM proteins and in consequence to invasion and metastasis.
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Registered trials
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.