Molecular characterization of cDNA for phospholipase A2-activating protein

A. K. Chopra; D. A. Ribardo; T. G. Wood; D. J. Prusak; X. J. Xu; J. W. Peterson

doi:10.1016/S0167-4781(98)00249-8

Molecular characterization of cDNA for phospholipase A₂-activating protein

A. K. Chopra
, D. A. Ribardo
, T. G. Wood
, D. J. Prusak
, X. J. Xu
, J. W. Peterson

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

13 Scopus citations

Abstract

A phospholipase A₂-activating protein (PLAP) cDNA was cloned and sequenced from a human monocyte cDNA library, and expressed as a histidine- tagged fusion protein. The DNA-deduced aa sequence of human PLAP was 80,826 Da; however, SDS-PAGE analysis revealed a 72-74 kDa protein which matched the size of native PLAP from human monocytes. Anti-sense plap oligonucleotide blocked cholera toxin-induced release of ³H-labeled arachidonic acid from cells, indicating a potential role for PLAP in regulating phospholipase A₂ activity.

Original language	English (US)
Pages (from-to)	125-130
Number of pages	6
Journal	Biochimica et Biophysica Acta - Gene Structure and Expression
Volume	1444
Issue number	1
DOIs	https://doi.org/10.1016/S0167-4781(98)00249-8
State	Published - Jan 18 1999

Keywords

3'-Rapid amplification of cDNA ends
Anti-sense plap oligonucleotide
CDNA cloning sequencing, and expression
Phospholipase A-activating protein
Phospholipase A-activating protein cDNA
Reverse transcriptase polymerase chain reaction

ASJC Scopus subject areas

Structural Biology
Biophysics
Biochemistry
Genetics

Access to Document

10.1016/S0167-4781(98)00249-8

Cite this

@article{66573c87da334efebbbc4de96db0faf3,

title = "Molecular characterization of cDNA for phospholipase A2-activating protein",

abstract = "A phospholipase A2-activating protein (PLAP) cDNA was cloned and sequenced from a human monocyte cDNA library, and expressed as a histidine- tagged fusion protein. The DNA-deduced aa sequence of human PLAP was 80,826 Da; however, SDS-PAGE analysis revealed a 72-74 kDa protein which matched the size of native PLAP from human monocytes. Anti-sense plap oligonucleotide blocked cholera toxin-induced release of 3H-labeled arachidonic acid from cells, indicating a potential role for PLAP in regulating phospholipase A2 activity.",

keywords = "3'-Rapid amplification of cDNA ends, Anti-sense plap oligonucleotide, CDNA cloning sequencing, and expression, Phospholipase A-activating protein, Phospholipase A-activating protein cDNA, Reverse transcriptase polymerase chain reaction",

author = "Chopra, \{A. K.\} and Ribardo, \{D. A.\} and Wood, \{T. G.\} and Prusak, \{D. J.\} and Xu, \{X. J.\} and Peterson, \{J. W.\}",

note = "Funding Information: This work was supported by Research Grants R01 A121463 from the National Institutes of Health, Bethesda, MD, and Crohn{\textquoteright}s and Colitis Foundation of America. Steve Smith from the Core Protein Chemistry Laboratory, UTMB, is acknowledged for computer analysis of the sequences and Mardelle Susman for editorial comments. ",

year = "1999",

month = jan,

day = "18",

doi = "10.1016/S0167-4781(98)00249-8",

language = "English (US)",

volume = "1444",

pages = "125--130",

journal = "Biochimica et Biophysica Acta - Gene Structure and Expression",

issn = "0167-4781",

publisher = "Elsevier B.V.",

number = "1",

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TY - JOUR

T1 - Molecular characterization of cDNA for phospholipase A2-activating protein

AU - Chopra, A. K.

AU - Ribardo, D. A.

AU - Wood, T. G.

AU - Prusak, D. J.

AU - Xu, X. J.

AU - Peterson, J. W.

N1 - Funding Information: This work was supported by Research Grants R01 A121463 from the National Institutes of Health, Bethesda, MD, and Crohn’s and Colitis Foundation of America. Steve Smith from the Core Protein Chemistry Laboratory, UTMB, is acknowledged for computer analysis of the sequences and Mardelle Susman for editorial comments.

PY - 1999/1/18

Y1 - 1999/1/18

N2 - A phospholipase A2-activating protein (PLAP) cDNA was cloned and sequenced from a human monocyte cDNA library, and expressed as a histidine- tagged fusion protein. The DNA-deduced aa sequence of human PLAP was 80,826 Da; however, SDS-PAGE analysis revealed a 72-74 kDa protein which matched the size of native PLAP from human monocytes. Anti-sense plap oligonucleotide blocked cholera toxin-induced release of 3H-labeled arachidonic acid from cells, indicating a potential role for PLAP in regulating phospholipase A2 activity.

AB - A phospholipase A2-activating protein (PLAP) cDNA was cloned and sequenced from a human monocyte cDNA library, and expressed as a histidine- tagged fusion protein. The DNA-deduced aa sequence of human PLAP was 80,826 Da; however, SDS-PAGE analysis revealed a 72-74 kDa protein which matched the size of native PLAP from human monocytes. Anti-sense plap oligonucleotide blocked cholera toxin-induced release of 3H-labeled arachidonic acid from cells, indicating a potential role for PLAP in regulating phospholipase A2 activity.

KW - 3'-Rapid amplification of cDNA ends

KW - Anti-sense plap oligonucleotide

KW - CDNA cloning sequencing, and expression

KW - Phospholipase A-activating protein

KW - Phospholipase A-activating protein cDNA

KW - Reverse transcriptase polymerase chain reaction

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UR - https://www.scopus.com/pages/publications/0033579973#tab=citedBy

U2 - 10.1016/S0167-4781(98)00249-8

DO - 10.1016/S0167-4781(98)00249-8

M3 - Article

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AN - SCOPUS:0033579973

SN - 0167-4781

VL - 1444

SP - 125

EP - 130

JO - Biochimica et Biophysica Acta - Gene Structure and Expression

JF - Biochimica et Biophysica Acta - Gene Structure and Expression

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