Affinity Purification and cDNA Cloning of Rat Neural Differentiation and Tumor Cell Surface Antigen gp130RB13-6 Reveals Relationship to Human and Murine PC-1

Deissler, Helmut; Lottspeich, Friedrich; Rajewsky, Manfred F.

doi:10.1074/jbc.270.17.9849

Cited by 72 publications

(57 citation statements)

References 36 publications

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“…NPP1 was first identified as a surface-located plasma cell differentiation antigen (PC-1) of mouse B lymphocytes [392] and subsequently further characterized [393] and cloned and sequenced from mouse [394,395] and human cDNA libraries [396,397]. NPP3 was identified as the target of the monoclonal antibody RB13-6 in rat brain glial precursor cells and cloned from rat [398] and a human prostate cDNA library [399].…”

Section: General Molecular Propertiesmentioning

confidence: 99%

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Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

878

922

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Ecto-nucleotidases play a pivotal role in purinergic signal transmission. They hydrolyze extracellular nucleotides and thus can control their availability at purinergic P2 receptors. They generate extracellular nucleosides for cellular reuptake and salvage via nucleoside transporters of the plasma membrane. The extracellular adenosine formed acts as an agonist of purinergic P1 receptors. They also can produce and hydrolyze extracellular inorganic pyrophosphate that is of major relevance in the control of bone mineralization. This review discusses and compares four major groups of ectonucleotidases: the ecto-nucleoside triphosphate diphosphohydrolases, ecto-5′-nucleotidase, ecto-nucleotide pyrophosphatase/phosphodiesterases, and alkaline phosphatases. Only recently and based on crystal structures, detailed information regarding the spatial structures and catalytic mechanisms has become available for members of these four ecto-nucleotidase families. This permits detailed predictions of their catalytic mechanisms and a comparison between the individual enzyme groups. The review focuses on the principal biochemical, cell biological, catalytic, and structural properties of the enzymes and provides brief reference to tissue distribution, and physiological and pathophysiological functions.

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Section: General Molecular Propertiesmentioning

confidence: 99%

“…Glycosylation N-glycosylation of E-NPPs accounts for up to 20 kDa of the molecular weights of NPP1-NPP3 [398,417,418]. N-glycosylation is not required for the apical targeting of NPP3 [419].…”

Section: General Molecular Propertiesmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

878

922

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“…This view had to be modified in 1994, when a second family member (named autotaxin or PD-1␣) was cloned independently in the human [44] and rat [45], respectively. The following year, a third member was identified in the rat and named gp130 RB13-6 [46]. A splice variant of this gene encoding a form of the enzyme expressed in rat liver (B10) was identified in 1997, and the corresponding human cDNA (named PD-1␤ or PDNP3) was independently cloned in the same year [47].…”

Section: Ecto-phosphodiesterase/ Pyrophosphatase: the Pc-1 Family Hismentioning

confidence: 99%

Ecto-enzymes: physiology meets pathology

Goding

2000

Journal of Leukocyte Biology

101

111

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Ecto-enzymes are catalytic membrane proteins with their active sites outside the cell. They include cholinesterase, which inactivates acetylcholine, and angiotensin-converting enzyme, which converts angiotensin I to biologically active angiotensin II, and numerous other peptidases, transpeptidases, nucleotidases, phosphodiesterases, and phosphatases. Many CD antigens of leukocytes are ecto-enzymes; some CD antigens for which no function is currently known are probably ectoenzymes. Expression is highly regulated and correlated with differentiation and activation. Some are highly restricted in distribution; others are ubiquitous. Many are shared between leukocytes and non-hematogenous cells. Biological functions appear to depend on the type and location of the cell in which expression occurs, and include recycling of nutrients, local control of response to cytokines and hormones, bone formation, cell mobility, invasion, and metastasis. Many novel regulatory functions of ecto-enzymes remain to be discovered, and may reveal new mechanisms of local extracellular control of cellular function.

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“…16 A protein that has 85% identity with autotaxin has also been cloned in the rat 17 and is probably the rat homologue of autotaxin. Another protein with APDE activity is B10, a 130-kd integral plasma membrane protein located at the bile canalicular membrane of rat hepatocytes which we have identified and cloned in our laboratory, 14,18 and which was also identified by others 19 in rat fetal brain and brain tumors as gp130 . B10 has a 50% identity with PC-1 at the protein level; however, contrary to PC-1, B10 is expressed on the apical surface of hepatocytes 14,18 and biliary cells.…”

mentioning

confidence: 99%

Identification of B10, an alkaline phosphodiesterase of the apical plasma membrane of hepatocytes and biliary cells, in rat serum: Increased levels following bile duct ligation and during the development of cholangiocarcinoma

et al. 1998

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Alkaline phosphodiesterase (APDE) is associated with the cellular plasma membrane of many organs. Several isoforms are also detected in normal human serum and their respective amounts vary in liver diseases but their significance is unknown. The aims of this study were: 1) to identify a serum form of B10, an APDE exclusively localized at the apical pole of the plasma membrane of rat hepatocytes and biliary cells; 2) to gain insight into its origin; and 3) to investigate its behavior, in two liver diseases in which an abnormal membrane expression of B10 has been reported, namely cholestasis and cholangiocarcinoma. A soluble form of B10 was immunoprecipitated from normal rat serum, which amounted to 13% of total serum APDE activity. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the size of the serum enzyme was 125 kd, which is slightly lower than that found in the plasma membrane (130 kd). In bile, a 120-kd and a 130-kd form was found. A sixfold and fivefold increase of B10 APDE activity was observed in the serum of bile duct-ligated rats and in the Long-Evans Cinnamon (LEC) rats which spontaneously develop cholangiocarcinoma. The molecular size of the form present in serum was unchanged. A threefold increase was also observed in LEC rats which had not yet developed a cholangiocarcinoma. In conclusion, we identified a soluble form of B10 in normal rat serum. The increase in serum B10 in the experimental and pathological conditions investigated does not seem to result from passage of the biliary form to the serum but seems to be caused by increased cleavage of the membrane form. Its rise early during the onset of cholangiocarcinoma suggests that B10 in the serum might be a marker of carcinogenesis and/or be involved in the development of cholangiocarcinoma.

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Affinity Purification and cDNA Cloning of Rat Neural Differentiation and Tumor Cell Surface Antigen gp130RB13-6 Reveals Relationship to Human and Murine PC-1

Cited by 72 publications

References 36 publications

Cellular function and molecular structure of ecto-nucleotidases

Cellular function and molecular structure of ecto-nucleotidases

Ecto-enzymes: physiology meets pathology

Identification of B10, an alkaline phosphodiesterase of the apical plasma membrane of hepatocytes and biliary cells, in rat serum: Increased levels following bile duct ligation and during the development of cholangiocarcinoma

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