ELSEVIER Biochimica et Biophysica Acta 1309 (1996) 21-24
BIOCHIMICA ET BIOPHYSICA ACTA
BBI
Short sequence-paper
Cloning and expression of the cDNA for mouse NAD +-dependent
15-hydroxyprostaglandin dehydrogenase
Muneaki Matsuo, Charles Mark Ensor, Hsin-Hsiung Tai *
Division of Medicinal Chemisto, and Pharmaceutics, College of Pharmacy, University of Kentucky, Lexington, KY 40536, USA
Received 12 January 1996; revised 5 June 1996; accepted 7 June 1996
Abstract
The cDNA for mouse NAD + dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) was isolated from a lung
cDNA library. The cDNA contains a 798 bp open reading frame that codes for a protein of 266 amino acids (M r 28775)
which shares 87% identity with the human 15-PGDH protein. The regions that are believed to form the NAD + binding site
and the active site are conserved in the mouse and human enzymes. The authenticity of the mouse cDNA was confirmed by
expression of an active 15-PGDH in Escherichia coli. Northern blot analysis demonstrated that 15-PGDH mRNA is
expressed primarily in lung, intestine, stomach and liver.
Keywords: NAD + dependent 15-hydroxyprostaglandin dehydrogenase; cDNA; Gene expression; Lung; (Mouse)
NAD+-dependent 15-hydroxyprostaglandin dehy-
drogenase (15-PGDH) is considered to be a key
catabolic enzyme that controls the biological activity
of prostaglandins [1,2]. The 15-PGDH cDNA has
been previously cloned from human placenta [3].
Although the enzyme is ubiquitous in mammalian
tissues [2], the extent of structural similarity of the
enzyme from different tissues and species remains
unknown. In addition, little is known about the bio-
synthetic regulation of 15-PGDH or its precise in
vivo role. Since a 15-PGDH-deficient mouse model,
created by the gene targeting technology, would be
valuable for a better understanding of the in vivo role
of 15-PGDH, we have cloned the cDNA for mouse
lung 15-PGDH by hybridization screening
* Corresponding author. Fax: + 1 (606) 2577585.
The 789 bp coding sequence from the human
15-PGDH cDNA was radiolabeled and used to screen
a hgtll mouse lung cDNA library (Clontech, Palo
Alto, CA) by plaque hybridization [4]. One positive
clone was plaque purified from 1.2 X l0 s phage and
the cDNA insert was amplified by the polymerase
chain reaction (PCR) using )tgtll primers which
flank the insertion site of the cDNA and sequenced.
Fig. 1 shows the nucleotide sequence of the mouse
lung 15-PGDH cDNA and the deduced amino acid
sequence. The cDNA contains the complete coding
sequence plus 24 bp of 5' untranslated region and
482 bp of the 3' untranslated region. The coding
sequence is 798 bp long and codes for a protein of
266 amino acids with a calculated molecular weight
of 28775. In Fig. 2 the deduced amino acid se-
quences of the mouse lung 15-PGDH and the human
placental 15-PGDH are compared. Both contain 266
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