Molecular cloning, expression, and chromosomal localization of a ubiquitously expressed human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene (PFKFB3)

A. Manzano, J. L. Rosa, F. Ventura, J. X. Pérez, M. Nadal, Xavier P. Estivill, S. Ambrosio, J. Gil, R. Bartrons

Research output: Contribution to journalArticle

57 Citations (Scopus)

Abstract

We report the identification of a human 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase gene (PFKFB3) isolated from a human fetal brain cDNA library. The gene was localized to 10p15→p14 by fluorescence in situ hybridization. The entire cDNA (4322 bp) codes for a polypeptide of 520 amino acid residues (molecular weight, 59.571 kDa). Structural analysis showed the presence of a kinase domain located at the amino terminus and a bisphosphatase domain at the carboxy terminus, characteristic of previously described 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase isozymes. In addition, a phosphorylation site for cAMP-dependent protein kinase was found at the carboxy terminus. Northern blot analysis showed the presence of a unique 4.8-kb mRNA expressed in the different tissues studied. In mammalian COS-1 cells, this cDNA drives the expression of an active isozyme. Taken together, these results identify the presence of a gene coding for a human 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase isozyme which is ubiquitously expressed.

Original languageEnglish
Pages (from-to)214-217
Number of pages4
JournalCytogenetics and Cell Genetics
Volume83
Issue number3-4
Publication statusPublished - 1998
Externally publishedYes

Fingerprint

Molecular Cloning
Isoenzymes
Complementary DNA
Phosphofructokinase-2
Genes
COS Cells
Cyclic AMP-Dependent Protein Kinases
Fluorescence In Situ Hybridization
Gene Library
Northern Blotting
Phosphotransferases
Molecular Weight
Phosphorylation
Amino Acids
Messenger RNA
Peptides
Brain
human PFKFB3 protein

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

Cite this

Molecular cloning, expression, and chromosomal localization of a ubiquitously expressed human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene (PFKFB3). / Manzano, A.; Rosa, J. L.; Ventura, F.; Pérez, J. X.; Nadal, M.; Estivill, Xavier P.; Ambrosio, S.; Gil, J.; Bartrons, R.

In: Cytogenetics and Cell Genetics, Vol. 83, No. 3-4, 1998, p. 214-217.

Research output: Contribution to journalArticle

Manzano, A. ; Rosa, J. L. ; Ventura, F. ; Pérez, J. X. ; Nadal, M. ; Estivill, Xavier P. ; Ambrosio, S. ; Gil, J. ; Bartrons, R. / Molecular cloning, expression, and chromosomal localization of a ubiquitously expressed human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene (PFKFB3). In: Cytogenetics and Cell Genetics. 1998 ; Vol. 83, No. 3-4. pp. 214-217.
@article{774346b5cfcf4f9aba20540f254f4af4,
title = "Molecular cloning, expression, and chromosomal localization of a ubiquitously expressed human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene (PFKFB3)",
abstract = "We report the identification of a human 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase gene (PFKFB3) isolated from a human fetal brain cDNA library. The gene was localized to 10p15→p14 by fluorescence in situ hybridization. The entire cDNA (4322 bp) codes for a polypeptide of 520 amino acid residues (molecular weight, 59.571 kDa). Structural analysis showed the presence of a kinase domain located at the amino terminus and a bisphosphatase domain at the carboxy terminus, characteristic of previously described 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase isozymes. In addition, a phosphorylation site for cAMP-dependent protein kinase was found at the carboxy terminus. Northern blot analysis showed the presence of a unique 4.8-kb mRNA expressed in the different tissues studied. In mammalian COS-1 cells, this cDNA drives the expression of an active isozyme. Taken together, these results identify the presence of a gene coding for a human 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase isozyme which is ubiquitously expressed.",
author = "A. Manzano and Rosa, {J. L.} and F. Ventura and P{\'e}rez, {J. X.} and M. Nadal and Estivill, {Xavier P.} and S. Ambrosio and J. Gil and R. Bartrons",
year = "1998",
language = "English",
volume = "83",
pages = "214--217",
journal = "Cytogenetic and Genome Research",
issn = "1424-8581",
publisher = "S. Karger AG",
number = "3-4",

}

TY - JOUR

T1 - Molecular cloning, expression, and chromosomal localization of a ubiquitously expressed human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene (PFKFB3)

AU - Manzano, A.

AU - Rosa, J. L.

AU - Ventura, F.

AU - Pérez, J. X.

AU - Nadal, M.

AU - Estivill, Xavier P.

AU - Ambrosio, S.

AU - Gil, J.

AU - Bartrons, R.

PY - 1998

Y1 - 1998

N2 - We report the identification of a human 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase gene (PFKFB3) isolated from a human fetal brain cDNA library. The gene was localized to 10p15→p14 by fluorescence in situ hybridization. The entire cDNA (4322 bp) codes for a polypeptide of 520 amino acid residues (molecular weight, 59.571 kDa). Structural analysis showed the presence of a kinase domain located at the amino terminus and a bisphosphatase domain at the carboxy terminus, characteristic of previously described 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase isozymes. In addition, a phosphorylation site for cAMP-dependent protein kinase was found at the carboxy terminus. Northern blot analysis showed the presence of a unique 4.8-kb mRNA expressed in the different tissues studied. In mammalian COS-1 cells, this cDNA drives the expression of an active isozyme. Taken together, these results identify the presence of a gene coding for a human 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase isozyme which is ubiquitously expressed.

AB - We report the identification of a human 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase gene (PFKFB3) isolated from a human fetal brain cDNA library. The gene was localized to 10p15→p14 by fluorescence in situ hybridization. The entire cDNA (4322 bp) codes for a polypeptide of 520 amino acid residues (molecular weight, 59.571 kDa). Structural analysis showed the presence of a kinase domain located at the amino terminus and a bisphosphatase domain at the carboxy terminus, characteristic of previously described 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase isozymes. In addition, a phosphorylation site for cAMP-dependent protein kinase was found at the carboxy terminus. Northern blot analysis showed the presence of a unique 4.8-kb mRNA expressed in the different tissues studied. In mammalian COS-1 cells, this cDNA drives the expression of an active isozyme. Taken together, these results identify the presence of a gene coding for a human 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase isozyme which is ubiquitously expressed.

UR - http://www.scopus.com/inward/record.url?scp=0032461972&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032461972&partnerID=8YFLogxK

M3 - Article

C2 - 10072580

AN - SCOPUS:0032461972

VL - 83

SP - 214

EP - 217

JO - Cytogenetic and Genome Research

JF - Cytogenetic and Genome Research

SN - 1424-8581

IS - 3-4

ER -