Kx. Chai et al., MOLECULAR-CLONING AND EXPRESSION OF RAT KALLISTATIN GENE, Biochimica et biophysica acta, N. Gene structure and expression, 1353(3), 1997, pp. 277-286
We have previously purified and cloned human kallistatin and rat kalli
krein-binding protein (RKBP), which are tissue kallikrein inhibitors b
elonging to the serine proteinase inhibitor superfamily. In this study
, we have cloned and sequenced the gene encoding rat kallistatin with
Phe-Phe-Ser-Ala-Gln at positions P2-P3', which is identical to the rea
ctive center of human kallistatin. Rat kallistatin is highly similar t
o human kallistatin, sharing 68% and 57% sequence identity at the cDNA
and the amino acid levels. The rat kallistatin gene exists in a singl
e copy and is located on chromosome 6. An SphI RFLP is found between S
HR and WKY rats at or near the rat kallistatin gene locus. Two amino a
cid polymorphisms of the rat kallistatin gene between these two strain
s were found by sequence analysis. A candidate promoter in the 5'-flan
king region (109 bp) of the rat kallistatin gene has been identified b
y reporter assays. The expression of rat kallistatin in the liver is g
rowth-dependent and down-regulated during acute phase inflammation. Re
combinant rat kallistatin produced in E. coli is able to bind to tissu
e kallikrein, and the interaction is inhibited by heparin. These chara
cteristics define rat kallistatin as the counterpart of human kallista
tin. (C) 1997 Elsevier Science B.V.