NDLI: Characterization of a new plasma membrane-associated ecto-5′-phosphodiesterase/nucleotide-pyrophosphatase from rat hepatocarcinoma AS-30D cells

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Characterization of a new plasma membrane-associated ecto-5′-phosphodiesterase/nucleotide-pyrophosphatase from rat hepatocarcinoma AS-30D cells

Content Provider	Springer Nature Link
Author	Garcia Nieto, R. M. Jose, E. San Martín Nieto, J. Villalobo, A.
Copyright Year	2001
Abstract	We have identified in plasma membrane fractions isolated from rat hepatocarcinoma AS-30D ascites cells three glycoproteins of 125 kDa, 115 kDa and 105 kDa (gp125, gp115 and gp105) which become adenylylated using ATP as substrate, most readily in the presence of EDTA. The gp115 becomes also phosphorylated. The adenylylation of these tumor glycoproteins was much lower than that of a group of analogous adenylylatable glycoproteins (gp130, gp120-gp110 dimer and gp100) present in normal rat liver plasma membrane. The tumor glycoproteins were reversibly O-adenylylated at threonine residues, as was the case for their normal rat liver counterparts. The tumor gp115, and the gp120-gp110 dimer from normal rat liver were both isolated using either ATP-affinity chromatography and/or AMP-affinity chromatography. The gp120-gp110 dimer from normal rat liver was identified as the plasma cell differentiation antigen-1 (PC-1 protein), an ecto-5′ phosphodiesterase/nucleotide-pyrophosphatase (5′-PDE/NPPase). The gp115 from tumor cells also exhibited Zn$^{2+}$-stimulated 5′-PDE and NPPase activities in alkaline conditions, although it appears to be distinct from the PC-1 protein. We have determined that the gp115 is an ecto-enzyme that catalyzes the hydrolysis of extracellular ATP, since its adenylylation and phosphorylation were detected in intact cells using extracellularly added [α-$^{32}$P]ATP or [γ-$^{32}$P]ATP, respectively, in the absence of any permeabilizing agent.Se identifican en fracciones de membranas plasmáticas aisladas de células ascíticas AS-30D de hepatocarcinoma de rata, tres glicoproteínas de 125 kDa, 115 kDa y 105 kDa (gp125, gp115 y gpl05) que son adenililadas utilizando ATP como sustrato. Esta adenililación es más intensa en presencia de EDTA. La gp115 también se fosforila utilizando ATP como sustrato. La adenililación de estas glicoproteínas tumorales es mucho mas débil que la adenililación de un grupo análogo de glicoproteínas (gp130, dímero gp120-gp110 y gp100) presentes en membranas plasmáticas aisladas de hígado normal de rata. Las glicoproteínas de las células tumorales y de hígado normal se Oadenililan reversiblemente en residuos de treonina. La gp115 tumoral y el dímero gp120-gp110 de hígado normal se aíslan mediante cromatografías de afinidad usando ATP y/o AMP inmovilizado. El dímero gp120-gp110 de hígado normal se identifica como el antígeno de diferenciación-l de células plasmáticas (proteína PC-1), una ecto-5′-fosfodiesterasa/nucleótido-pirofosfatasa (5′-FDE/NPFasa). La gp115 de células tumorales también presenta actividades 5′-FDE y NPFasa estimuladas por Zn$^{2+}$ en condiciones alcalinas, aunque parece ser una proteína diferente a la proteína PC-1. Se ha determinado también que la gp115 es una ecto-enzima que cataliza la hidrólisis de ATP extracelular, ya que resulta adenililada y fosforilada en células intactas añadiendo al medio [α-$^{32}$P]ATP o [γ-$^{32}$P]ATP, respectivamente, en ausencia de agentes permeabilizantes.
Starting Page	31
Ending Page	40
Page Count	10
File Format	PDF
ISSN	11387548
Journal	Journal of Physiology and Biochemistry
Volume Number	57
Issue Number	1
e-ISSN	18778755
Language	Spanish
Publisher	Springer Netherlands
Publisher Date	2001-01-01
Publisher Institution	University of Navarra, Spain
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Adenylylation AS-30D tumor cells Ecto-5′-phosphodiesterase/nucleotidepyrophosphatase Hepatocarcinoma Biomedicine general Human Physiology Biochemistry Animal Physiology
Content Type	Text
Resource Type	Article
Subject	Physiology Medicine Biochemistry

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