Differential accessibility of the tail domain of nuclear lamin A in interphase and mitotic cells.
Human autoantibodies reactive against the tail domain exclusive to lamin A and absent from lamin C have been used for immunofluorescence studies on human fibroblast and epithelial cells. These autoantibodies were seen to react on mitotic cells where lamin A is present in a soluble depolymerized form and to react against lamin A in assembled interphase nuclear lamina after in situ extraction of chromatin. Taken together, these results support the suggestion that the tail domain of lamin A may be involved in the putative interaction of lamin A with chromatin.
Collard
J F
JF
Institut du Cancer de Montréal, Hôpital Notre-Dame, Québec, Canada.
Senécal
J L
JL
Raymond
Y
Y
D000818:Animals; D001323:Autoantibodies; D002460:Cell Line; D002467:Cell Nucleus / Q000187:drug effects / Q000648:ultrastructure*; D004247:DNA / Q000032:analysis; D004847:Epithelial Cells; D005347:Fibroblasts / Q000166:cytology; D005455:Fluorescent Antibody Technique; D006801:Humans; D007106:Immune Sera; D007399:Interphase; D034904:Lamin Type A; D034882:Lamins; D008099:Liver / Q000737:chemistry; D008938:Mitosis; D015739:Nocodazole / Q000494:pharmacology; D009687:Nuclear Proteins / Q000032:analysis* / Q000276:immunology; D051381:Rats
D001323:Autoantibodies; D007106:Immune Sera; D034904:Lamin Type A; D034882:Lamins; D009687:Nuclear Proteins; C440308:lamin C; D004247:DNA; D015739:Nocodazole