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PMID: 2834825 Published · ppublish English Journal Article

Calpain II involvement in mitosis.

Science (New York, N.Y.) ·Vol. 240 ·No. 4854 ·1988-05-13 ·Pages 911-3

Schollmeyer JE

Abstract

Mitotic spindle disassembly requires major structural alterations in the associated cytoskeletal proteins and mitosis is known to be associated with Ca2+-sequestering phenomena and calcium transients. To examine the possible involvement of a ubiquitous Ca2+-activated protease, calpain II, in the mitotic process, synchronized PtK1 cells were monitored by immunofluorescence for the relocation of calpain II. The plasma membrane was the predominant location of calpain II in interphase. However, as mitosis progressed, calpain II relocated to (i) an association with mitotic chromosomes, (ii) a perinuclear location in anaphase, and (iii) a mid-body location in telophase. Microinjection of calpain II near the nucleus of a PtK1 cell promoted the onset of metaphase. Injection of calpain II at late metaphase promoted a precocious disassembly of the mitotic spindle and the onset of anaphase. These data suggest that calpain II is involved in mitosis.

MeSH Terms
Anaphase/drug effects Animals Calcium/pharmacology Calcium-Binding Proteins/pharmacology Calpain/antagonists & inhibitors,pharmacology,physiology Cell Line Cell Membrane/enzymology Cell Nucleus/enzymology Chromosomes/metabolism Enzyme Activation Fluorescent Antibody Technique Fluorescent Dyes Interphase Metaphase/drug effects Mitosis Muscles/enzymology Rhodamines Spindle Apparatus/drug effects Swine
Chemicals
Calcium-Binding Proteins Fluorescent Dyes Rhodamines calpastatin rhodamine isothiocyanate Calpain Calcium
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Schollmeyer J E
U.S. Department of Agriculture, Roman L. Hruska Meat Animal Research Center, Clay Center, NE 68933.
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1988-05-13
Pages
911-3
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Corrections
CommentIn
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