Premium
Presence of different phospholipase C isoforms in the nucleus and their activation during compensatory liver growth
Author(s) -
Crljen Vladiana,
Višnjić Dora,
Banfić Hrvoje
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.06.051
Subject(s) - phosphorylation , gene isoform , phospholipase c , nuclear matrix , enzyme , phospholipase a2 , phospholipase , chromatin , chemistry , biochemistry , biology , microbiology and biotechnology , medicine , dna , gene
Phospholipase C (PLC) was purified from the membrane‐depleted rat liver nuclei. About 60% of the total PLC‐activity corresponded to β 1b isoform, 30% to PLC‐γ 1 and less than 10% to PLC‐δ 1 . PLC‐β 1b and ‐γ 1 were found in the nuclear matrix, while PLC‐δ 1 was detected in the chromatin. Two peaks of an increase in the total PLC‐activity were detected occurring at 6 and 20 h after partial hepatectomy. An early increase in PLC‐β 1b activity in the nuclear matrix was associated with serine phosphorylation of the enzyme, while the later increase paralleled the increase in the amount of protein. The increase in the PLC‐γ 1 activity measured at 6 and 20 h after partial hepatectomy was associated with tyrosine phosphorylation of the enzyme. The activity of PLC‐δ 1 and the amount of the protein found in the chromatin was increased only at 20 h after partial hepatectomy.