TY - JOUR
T1 - NPP-type ectophosphodiesterases
T2 - Unity in diversity
AU - Stefan, Cristiana
AU - Jansen, Silvia
AU - Bollen, Mathieu
N1 - Funding Information:
The authors' work on NPPs is supported by the Fund for Scientific Research-Flanders (grant G.0082.02). S.J. is a Research Assistant of the Fund for Scientific Research.
PY - 2005/10
Y1 - 2005/10
N2 - Nucleotide pyrophosphatase/phosphodiesterase (NPP)-type ectophosphodiesterases are found at the cell surface as type-I or type-II transmembrane proteins, but are also found extracellularly as secreted or shedded enzymes. They hydrolyze pyrophosphate or phosphodiester bonds in a variety of extracellular compounds including nucleotides, (lyso)phospholipids and choline phosphate esters. Despite their structurally related catalytic domain, each enzyme has well-defined substrate specificity. Catalysis by NPPs affects processes as diverse as cell proliferation and motility, angiogenesis, bone mineralization and digestion. In addition, there is emerging evidence for non-catalytic functions of NPPs in cell signaling. NPP-type ectophosphodiesterases are also implicated in the pathophysiology of cancer, insulin resistance and calcification diseases, and they hold great promise as easily accessible therapeutic targets.
AB - Nucleotide pyrophosphatase/phosphodiesterase (NPP)-type ectophosphodiesterases are found at the cell surface as type-I or type-II transmembrane proteins, but are also found extracellularly as secreted or shedded enzymes. They hydrolyze pyrophosphate or phosphodiester bonds in a variety of extracellular compounds including nucleotides, (lyso)phospholipids and choline phosphate esters. Despite their structurally related catalytic domain, each enzyme has well-defined substrate specificity. Catalysis by NPPs affects processes as diverse as cell proliferation and motility, angiogenesis, bone mineralization and digestion. In addition, there is emerging evidence for non-catalytic functions of NPPs in cell signaling. NPP-type ectophosphodiesterases are also implicated in the pathophysiology of cancer, insulin resistance and calcification diseases, and they hold great promise as easily accessible therapeutic targets.
UR - http://www.scopus.com/inward/record.url?scp=25144473903&partnerID=8YFLogxK
U2 - 10.1016/j.tibs.2005.08.005
DO - 10.1016/j.tibs.2005.08.005
M3 - Review article
C2 - 16125936
AN - SCOPUS:25144473903
SN - 0968-0004
VL - 30
SP - 542
EP - 550
JO - Trends in biochemical sciences
JF - Trends in biochemical sciences
IS - 10
ER -