title: The septin-binding protein anillin is overexpressed in diverse human tumors.
abstract: Anillin is an actin-binding protein that can bind septins and is a component of the cytokinetic ring. We assessed the anillin expression in 7,579 human tissue samples and cell lines by DNA microarray analysis. Anillin is expressed ubiquitously but with variable levels of expression, being highest in the central nervous system. The median level of anillin mRNA expression was higher in tumors than normal tissues (median fold increase 2.58; 95% confidence intervals, 2.19-5.68, P < 0.0001) except in the central nervous system where anillin mRNA levels were lower in tumors. We developed a sensitive reverse transcription-PCR strategy to show that anillin mRNA is expressed in cell lines and in cDNA panels derived from fetal and adult tissues, thus validating the microarray data. We compared anillin with Ki67 mRNA expression and found a significant linear relationship between anillin and Ki67 mRNA expression (Spearmann r approximately 0.6, P < 0.0001). Anillin mRNA expression was analyzed during tumor progression in breast, ovarian, kidney, colorectal, hepatic, lung, endometrial, and pancreatic tumors and in all tissues there was progressive increase in anillin mRNA expression from normal to benign to malignant to metastatic disease. Finally, we used anti-anillin sera and found nuclear anillin immunoreactivity to be widespread in normal tissues, often not correlating with proliferative compartments. These data provide insight into the existence of nonproliferation-associated activities of anillin and roles in interphase nuclei. Thus, anillin is overexpressed in diverse common human tumors, but not simply as a consequence of being a proliferation marker. Anillin may have potential as a novel biomarker.
authors.affiliation: Centre for Cancer Research and Cell Biology, Queens University Belfast, Belfast City Hospital, Belfast, Northern Ireland, United Kingdom. peter.hall@qub.ac.uk
authors.forename: Peter A
authors.initials: PA
authors.lastname: Hall
authors.forename: Christopher B
authors.initials: CB
authors.lastname: Todd
authors.forename: Paula L
authors.initials: PL
authors.lastname: Hyland
authors.forename: Simon S
authors.initials: SS
authors.lastname: McDade
authors.forename: Heike
authors.initials: H
authors.lastname: Grabsch
authors.forename: Mit
authors.initials: M
authors.lastname: Dattani
authors.forename: Kenneth J
authors.initials: KJ
authors.lastname: Hillan
authors.forename: S E Hilary
authors.initials: SE
authors.lastname: Russell
mesh_terms: D000199:Actins / Q000378:metabolism; D014408:Biomarkers, Tumor; D015152:Blotting, Northern; D018797:Cell Cycle Proteins / Q000378:metabolism; D045744:Cell Line, Tumor; D002467:Cell Nucleus / Q000378:metabolism; D002490:Central Nervous System / Q000196:embryology; D003001:Cloning, Molecular; D003285:Contractile Proteins / Q000737:chemistry* / Q000502:physiology*; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D018076:DNA, Complementary / Q000378:metabolism; D005091:Exons; D015972:Gene Expression Regulation, Neoplastic; D006367:HeLa Cells; D006801:Humans; D007150:Immunohistochemistry; D019394:Ki-67 Antigen / Q000096:biosynthesis; D008840:Microfilament Proteins / Q000378:metabolism; D024101:Mitochondrial Proteins / Q000378:metabolism; D009369:Neoplasms / Q000378:metabolism*; D020411:Oligonucleotide Array Sequence Analysis; D016133:Polymerase Chain Reaction; D011485:Protein Binding; D012333:RNA, Messenger / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D014018:Tissue Distribution; D014158:Transcription, Genetic
chemical_list: D000199:Actins; D014408:Biomarkers, Tumor; D018797:Cell Cycle Proteins; D003285:Contractile Proteins; D003598:Cytoskeletal Proteins; D018076:DNA, Complementary; D019394:Ki-67 Antigen; D008840:Microfilament Proteins; D024101:Mitochondrial Proteins; D012333:RNA, Messenger; C095886:anillin