Molecular cloning and functional expression of rat leukotriene A4hydrolase using the polymerase chain reaction

Naomasa Makitala; Colin D. Funku; Enyu Imaic; Richard L. Hoover; Kamal F. Badra

doi:10.1016/0014-5793(92)80130-9

Molecular cloning and functional expression of rat leukotriene A4hydrolase using the polymerase chain reaction

Naomasa Makitala
, Colin D. Funku
, Enyu Imaic
, Richard L. Hoover
, Kamal F. Badra

Research output: Contribution to journal › Article › peer-review

29 Scopus citations

Abstract

We isolated a cDNA encoding rat leukotriene A₄ (LTA₄) hydrolase from mesangial cells by the polymerase chain reaction according to the human amino acid sequence. The deduced amino acid sequence shows that rat LTA, hydrolase is a 609 amino acid protein with an M, 69 kDa. Comparison of human LTA₄ hydrolase revealed 93% homology, and include zinc-binding motifs of aminopeptidases. COS-7 cells transfected with the cDNA revealed substantial LTA₄ hydrolase activity, and their activities were abolished by preincubation with captopril, representing the first reported cDNA expression of recombinant enzyme in mammalian cells. RNA blot analysis indicated that LTA₄ hydrolase was expressed in glomerular endothelial, epithelial and mesangial cells.

Original language	English (US)
Pages (from-to)	273-277
Number of pages	5
Journal	FEBS Letters
Volume	299
Issue number	3
DOIs	https://doi.org/10.1016/0014-5793(92)80130-9
State	Published - 1992
Externally published	Yes

Keywords

Captopril
cDNA cloning
Glomerular cell
Leukotricne A hydrolase
PCR (polymerase chain reaction)

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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10.1016/0014-5793(92)80130-9

Cite this

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title = "Molecular cloning and functional expression of rat leukotriene A4hydrolase using the polymerase chain reaction",

abstract = "We isolated a cDNA encoding rat leukotriene A4 (LTA4) hydrolase from mesangial cells by the polymerase chain reaction according to the human amino acid sequence. The deduced amino acid sequence shows that rat LTA, hydrolase is a 609 amino acid protein with an M, 69 kDa. Comparison of human LTA4 hydrolase revealed 93\% homology, and include zinc-binding motifs of aminopeptidases. COS-7 cells transfected with the cDNA revealed substantial LTA4 hydrolase activity, and their activities were abolished by preincubation with captopril, representing the first reported cDNA expression of recombinant enzyme in mammalian cells. RNA blot analysis indicated that LTA4 hydrolase was expressed in glomerular endothelial, epithelial and mesangial cells.",

keywords = "Captopril, cDNA cloning, Glomerular cell, Leukotricne A hydrolase, PCR (polymerase chain reaction)",

author = "Naomasa Makitala and Funku, \{Colin D.\} and Enyu Imaic and Hoover, \{Richard L.\} and Badra, \{Kamal F.\}",

year = "1992",

doi = "10.1016/0014-5793(92)80130-9",

language = "English (US)",

volume = "299",

pages = "273--277",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

number = "3",

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TY - JOUR

T1 - Molecular cloning and functional expression of rat leukotriene A4hydrolase using the polymerase chain reaction

AU - Makitala, Naomasa

AU - Funku, Colin D.

AU - Imaic, Enyu

AU - Hoover, Richard L.

AU - Badra, Kamal F.

PY - 1992

Y1 - 1992

N2 - We isolated a cDNA encoding rat leukotriene A4 (LTA4) hydrolase from mesangial cells by the polymerase chain reaction according to the human amino acid sequence. The deduced amino acid sequence shows that rat LTA, hydrolase is a 609 amino acid protein with an M, 69 kDa. Comparison of human LTA4 hydrolase revealed 93% homology, and include zinc-binding motifs of aminopeptidases. COS-7 cells transfected with the cDNA revealed substantial LTA4 hydrolase activity, and their activities were abolished by preincubation with captopril, representing the first reported cDNA expression of recombinant enzyme in mammalian cells. RNA blot analysis indicated that LTA4 hydrolase was expressed in glomerular endothelial, epithelial and mesangial cells.

AB - We isolated a cDNA encoding rat leukotriene A4 (LTA4) hydrolase from mesangial cells by the polymerase chain reaction according to the human amino acid sequence. The deduced amino acid sequence shows that rat LTA, hydrolase is a 609 amino acid protein with an M, 69 kDa. Comparison of human LTA4 hydrolase revealed 93% homology, and include zinc-binding motifs of aminopeptidases. COS-7 cells transfected with the cDNA revealed substantial LTA4 hydrolase activity, and their activities were abolished by preincubation with captopril, representing the first reported cDNA expression of recombinant enzyme in mammalian cells. RNA blot analysis indicated that LTA4 hydrolase was expressed in glomerular endothelial, epithelial and mesangial cells.

KW - Captopril

KW - cDNA cloning

KW - Glomerular cell

KW - Leukotricne A hydrolase

KW - PCR (polymerase chain reaction)

UR - https://www.scopus.com/pages/publications/0026533451

UR - https://www.scopus.com/pages/publications/0026533451#tab=citedBy

U2 - 10.1016/0014-5793(92)80130-9

DO - 10.1016/0014-5793(92)80130-9

M3 - Article

C2 - 1544505

AN - SCOPUS:0026533451

SN - 0014-5793

VL - 299

SP - 273

EP - 277

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

Molecular cloning and functional expression of rat leukotriene A4hydrolase using the polymerase chain reaction

Abstract

Keywords

ASJC Scopus subject areas

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