Regulation of nuclear scaffold protease activity by calcium

Kenneth R. Madsen, Gary Fiskum, Gary Clawson

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


Recent investigations have disclosed protease activity which is intimately associated with the nuclear scaffold. This protease activity shows a marked selectivity for lamins A/C, and from them may produce the 46-kDa NTPase thought to participate in nucleocytoplasmic RNA transport. Preliminary characterizations suggested that the protease activity might require Ca2+. In this report, we present evidence showing that nuclear scaffold protease activity is stringently regulated by Ca2+ within the physiologic range. Further, calmodulin antagonists such as calmidazolium and chlorpromazine produce marked inhibition of the protease activity, suggesting modulation by calmodulin or calmodulin-like factors.

Original languageEnglish (US)
Pages (from-to)343-345
Number of pages3
JournalExperimental Cell Research
Issue number2
StatePublished - Apr 1990

All Science Journal Classification (ASJC) codes

  • Cell Biology


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