Abstract：
:Phospholipase C-gamma1, a substrate for many growth factor receptor and nonreceptor tyrosine kinases, produces second messenger molecules that are elements of signal transduction pathways related to cell proliferation. The influence of deletion mutations, which do not intrude on the domains required for catalytic function, on the basal activity of this enzyme is reported. Removal of the first 74 amino-terminal residues increases phospholipase C activity, while deletion of the carboxy-terminal 81 residues decreases enzyme activity. Deletion of the SH2-SH2-SH3 central region, which separates the two domains (X, Y) responsible for catalytic function, also increases enzymatic activity. Interestingly, addition of a recombinant SH2-SH2-SH3 fragment of phospholipase C-gamma1 to the holoenzyme inhibits its phospholipase activity at pH 7.0, but not at pH 5.0. However, addition of individual SH2 or SH3 domains does not influence activity of the holoenzyme. All three deletion mutants, in contrast to the holoenzyme, are relatively resistant to V8 proteolysis and activation induced by the epidermal growth factor receptor tyrosine kinase, which require, respectively, specific proteolysis and phosphorylation sites within the SH region. This suggests a conformational change is induced in the SH region by deletion at either the amino- or carboxy-terminus.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Horstman DA,Chattopadhyay A,Carpenter Gdoi
10.1006/abbi.1998.0978subject
Has Abstractpub_date
1999-01-01 00:00:00pages
149-55issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(98)90978-Xjournal_volume
361pub_type
杂志文章abstract：:Reperfusion of ischemic myocardial tissue results in an increase in mitochondrial free radical production and declines in respiratory activity. The effects of ischemia and reperfusion on the activities of Krebs cycle enzymes, as well as enzymes involved in electron transport, were evaluated to provide insight into whe...
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journal_title：Archives of biochemistry and biophysics
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