Linked Life Data

15915442

Source:http://linkedlifedata.com/resource/pubmed/id/15915442

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2005-6-9
pubmed:abstractText
The septins are an evolutionarily conserved family of GTP-binding proteins involved in diverse processes including vesicle trafficking, apoptosis, remodelling of the cytoskeleton, infection, neurodegeneration, and neoplasia. The present paper reports a comprehensive study of septin gene expression by DNA microarray methods in 10 360 samples of normal, diseased, and tumour tissues. A novel septin, SEPT13, has been identified and is shown to be related to SEPT7. It is shown that SEPT13 and the other known human septins are expressed in all tissue types but some show high expression in lymphoid (SEPT1, 6, 9, and 12) or brain tissues (SEPT2, 3, 4, 5, 7, 8, and 11). For a given septin, some isoforms are highly expressed in the brain and others are not. For example, SEPT8_v2 and v1, 1* and 3 are highly expressed in the brain and cluster with SEPT2, 3, 4, 5, 7, and 11. However, a probe set specific for SEPT8_v1 with low brain expression clusters away from this set. Similarly, SEPT4 has lymphoid and non-lymphoid forms; SEPT2 has lymphoid and central nervous system (CNS) forms; and SEPT6 and SEPT9 are elevated in lymphoid tissues but both have forms that cluster away from the lymphoid forms. Perturbation of septin expression was widespread in disease and tumours of the various tissues examined, particularly for conditions of the CNS, where alterations in all 13 septin genes were identified. This analysis provides a comprehensive catalogue of the septin family in health and disease. It is a key step in understanding the role of septins in physiological and pathological states and provides insight into the complexity of septin biology.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/SEPT10 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/SEPT11 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/SEPT4 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/SEPT5 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/SEPT6 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/SEPT7 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/SEPT8 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/SEPT9 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Septins, http://linkedlifedata.com/resource/pubmed/chemical/septin 3
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0022-3417
pubmed:author
pubmed:copyrightInfo
Copyright 2005 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.
pubmed:issnType
Print
pubmed:volume
206
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
269-78
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Expression profiling the human septin gene family.
pubmed:affiliation
Centre for Cancer Research and Cell Biology, Queen's University Belfast, University Floor, Tower Block, Belfast City Hospital, Belfast BT9 7AB, UK. peter.hall@qub.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't