Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2002-5-17
pubmed:abstractText
The interactions of CD44 with hyaluronan are thought to be crucial for tumor cell attachment to the extracellular matrix, migration, and invasion. For migration to occur, however, the interactions between hyaluronan and cell surface receptors need to be transient. Hyaluronidases may facilitate the degradation of hyaluronan bound to the cell surface and thus reduce the interactions of the cells with the matrix, whereas the overproduction of hyaluronan in the absence of hyaluronidase activity may prevent cells from proliferating or invading normal surrounding tissue.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acetylglucosaminidase, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm, http://linkedlifedata.com/resource/pubmed/chemical/Glucuronosyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/HAS2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Has2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Hyaluronic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Hyaluronoglucosaminidase, http://linkedlifedata.com/resource/pubmed/chemical/MGEA5 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms, http://linkedlifedata.com/resource/pubmed/chemical/beta-N-Acetylhexosaminidases
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0148-396X
pubmed:author
pubmed:issnType
Print
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1311-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:12015850-Acetylglucosaminidase, pubmed-meshheading:12015850-Animals, pubmed-meshheading:12015850-Antigens, Neoplasm, pubmed-meshheading:12015850-Astrocytoma, pubmed-meshheading:12015850-Brain Neoplasms, pubmed-meshheading:12015850-Carcinogenicity Tests, pubmed-meshheading:12015850-Cell Division, pubmed-meshheading:12015850-Gene Expression, pubmed-meshheading:12015850-Glioblastoma, pubmed-meshheading:12015850-Glioma, pubmed-meshheading:12015850-Glucuronosyltransferase, pubmed-meshheading:12015850-Histone Acetyltransferases, pubmed-meshheading:12015850-Humans, pubmed-meshheading:12015850-Hyaluronic Acid, pubmed-meshheading:12015850-Hyaluronoglucosaminidase, pubmed-meshheading:12015850-Mice, pubmed-meshheading:12015850-Neoplasm Proteins, pubmed-meshheading:12015850-Neoplasm Transplantation, pubmed-meshheading:12015850-Protein Isoforms, pubmed-meshheading:12015850-Skin Neoplasms, pubmed-meshheading:12015850-Transfection, pubmed-meshheading:12015850-Tumor Cells, Cultured, pubmed-meshheading:12015850-beta-N-Acetylhexosaminidases
pubmed:year
2002
pubmed:articleTitle
Overexpression of hyaluronan synthase-2 reduces the tumorigenic potential of glioma cells lacking hyaluronidase activity.
pubmed:affiliation
Departments of Surgery, University of Melbourne, Royal Melbourne Hospital, Parkville, Victoria, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't