Disease relevance of ANXA11

• Annexin XI isoforms were expressed in Sf9 cells using a baculovirus expression system [1].

High impact information on ANXA11

• Both studies by subcellular fractionation and by indirect immunofluorescence staining of the rat embryonic fibroblast cell line, 3Y1, revealed that CAP-50 mainly localized in nuclei [2].
• Moreover, between the cells at interphase and at mitotic phase, different distributions of CAP-50 were observed [2].
• In most rat tissues, except those in the central nervous systems and kidney, CAP-50 is expressed at a high or moderate level [2].
• Using specific polyclonal antibodies to bovine lung CAP-50, tissue distribution and subcellular distribution of CAP-50 were investigated [2].
• CAP-50 was found in isolated 3Y1 nuclei lacking outer nuclear membranes, and approximately 50% of CAP-50 was extracted from the nuclei by chelating calcium [2].

Biological context of ANXA11

• On the other hand, in the cells during mitosis, CAP-50 was concentrated at the loop-like structure around the mitotic apparatus [2].
• Two kinds of cDNAs were identified corresponding to annexin XI mRNA variants A and B, which are generated by alternative splicing of identical primary transcripts [3].
• Binding site of annexin XI on the calcyclin molecule [4].
• Since annexin XI isoforms differ in amino acid sequence only in the alternative splicing region of the N-terminal domain, these findings suggest that this domain has distinct biological significance in terms of aggregation and vesicle formation [1].
• Two isoforms of annexin XI, termed XI-A and XI-B, were previously identified by screening a bovine chondrocyte cDNA library [1].

Anatomical context of ANXA11

• CAP-50, a newly identified annexin, localizes in nuclei of cultured fibroblast 3Y1 cells [2].

Associations of ANXA11 with chemical compounds

• The wild type (wt) and mt1 mutant lacking three amino acids from N-terminal bound to annexin XI with phosphatidylserine and Ca2+, whereas mt2, mt3 and mt4 with seven, twelve and eighteen amino acids deleted, respectively, did not bind to annexin XI [4].
• The peptide fragment of calcyclin, CNBr-3 (residues 1-57), digested with cyanogen bromide completely inhibited the interaction of native calcyclin with annexin XI, while CNBr-1 (residues 83-90) and CNBr-2 (residues 58-82) did not affect the binding [4].

Analytical, diagnostic and therapeutic context of ANXA11

• This report describes an additional member of this family, bovine annexin XI, identified by cDNA cloning and sequence analysis [5].

References