Document Detail


Molecular mechanisms of glioma invasiveness: the role of proteases.
MedLine Citation:
PMID:  12835669     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The invasive nature of brain-tumour cells makes an important contribution to the ineffectiveness of current treatment modalities, as the remaining tumour cells inevitably infiltrate the surrounding normal brain tissue, which leads to tumour recurrence. Such local invasion remains an important cause of mortality and underscores the need to understand in more detail the mechanisms of tumour invasiveness. Several proteases influence the malignant characteristics of gliomas--could their inhibition prove to be a useful therapeutic strategy?
Authors:
Jasti S Rao
Related Documents :
19789639 - Inhibitory effects of the ruthenium complex kp1019 in models of mammary cancer cell mig...
2884029 - Transformation of a rat liver cell line: neoplastic phenotype and regulation of gamma g...
8438089 - Micronuclei expression in tumors as a test for radiation sensitivity.
17456059 - The number of tumour-infiltrating tia-1+ cytotoxic t cells but not foxp3+ regulatory t ...
6591709 - Implications of dna characterization of human acoustic neuromas.
19840009 - Molecular events in germ cell tumours: linking chromosome-12 gain, acquisition of pluri...
19951459 - The role of autophagy in tumour development and cancer therapy.
17624619 - A cell culturing system that integrates the cell loading function on a single platform ...
24896309 - Nucleic acid aptamers for living cell analysis.
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.; Review    
Journal Detail:
Title:  Nature reviews. Cancer     Volume:  3     ISSN:  1474-175X     ISO Abbreviation:  Nat. Rev. Cancer     Publication Date:  2003 Jul 
Date Detail:
Created Date:  2003-07-01     Completed Date:  2003-08-26     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  101124168     Medline TA:  Nat Rev Cancer     Country:  England    
Other Details:
Languages:  eng     Pagination:  489-501     Citation Subset:  IM    
Affiliation:
Program of Cancer Biology, Department of Neurosurgery, University of Illinois College of Medicine-Peoria, 1 Illini Drive, Peoria, Illinois 61656, USA. jsrao@uic.edu
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Cathepsin B / metabolism
Central Nervous System Neoplasms / metabolism*,  pathology*,  physiopathology
Endopeptidases / physiology*
Glioma / metabolism*,  pathology*,  physiopathology
Humans
Matrix Metalloproteinases / metabolism
Neoplasm Invasiveness
Neoplasm Recurrence, Local / metabolism
Plasminogen Activators / metabolism
Receptors, Cell Surface / metabolism
Receptors, Urokinase Plasminogen Activator
Urokinase-Type Plasminogen Activator / metabolism
Chemical
Reg. No./Substance:
0/PLAUR protein, human; 0/Receptors, Cell Surface; 0/Receptors, Urokinase Plasminogen Activator; EC 3.4.-/Endopeptidases; EC 3.4.21.-/Plasminogen Activators; EC 3.4.21.73/Urokinase-Type Plasminogen Activator; EC 3.4.22.1/Cathepsin B; EC 3.4.24.-/Matrix Metalloproteinases
Comments/Corrections
Comment In:
Nat Rev Cancer. 2003 Jul;3(7):doi:10.1038/nrc1121-c1   [PMID:  19006840 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Occurrence of leukaemia following gene therapy of X-linked SCID.
Next Document:  Ovarian cancer: strategies for overcoming resistance to chemotherapy.