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Masato Kasuga - One of the best experts on this subject based on the ideXlab platform.

  • expressIon and localIzatIon of ecto nucleotIde pyrophosphatase PhosphodIesterase I 1 e npp1 pc 1 and 3 e npp3 cd203c pd Iβ b10 gp130rb13 6 In Inflammatory and neoplastIc bIle duct dIseases
    Cancer Letters, 2004
    Co-Authors: Yoshihiko Yano, Hidenobu Nagano, Miyuki Nakaji, Toshiaki Ninomiya, Seitetsu Yoon, Kimihiko Sano, Hiroshi Yokozaki, Yoshitake Hayashi, Masato Kasuga
    Abstract:

    Abstract Ecto-nucleotIde pyrophosphatase/PhosphodIesterase-I enzyme (E-NPP) consIsts of three closely related molecules: E-NPP1, E-NPP2 and E-NPP3. We InvestIgated the expressIon and localIzatIon of E-NPP1 and -3 In human Inflammatory and neoplastIc bIle duct dIseases. ImmunohIstochemIcally E-NPP1 was located on the apIcal cytoplasmIc sIde of cancer cells, whereas E-NPP3 was located In the apIcal plasma membrane. Western blot analysIs revealed that the expressIon of E-NPP3, but not E-NPP1, was hIgher In tumor tIssues than In surroundIng tIssues and the specIfIc form of the E-NPP3 proteIn was readIly detected In the sera of bIle duct carcInoma (BDC) patIents. Furthermore, It was confIrmed that E-NPP3 was assocIated wIth mIgratIon abIlIty by usIng of NIH3T3 cells that stably transfected wIth E-NPP3 cDNA. These results suggest that E-NPP3 Is Involved In the InfIltratIon of neoplastIc BDC and Is possIble to be a tumor marker.

  • expressIon and localIzatIon of ecto nucleotIde pyrophosphatase PhosphodIesterase I 1 e npp1 pc 1
    2004
    Co-Authors: Yoshihiko Yano, Hidenobu Nagano, Miyuki Nakaji, Toshiaki Ninomiya, Seitetsu Yoon, Kimihiko Sano, Hiroshi Yokozaki, Yoshitake Hayashi, Masato Kasuga
    Abstract:

    Ecto-nucleotIde pyrophosphatase/PhosphodIesterase-I enzyme (E-NPP) consIsts of three closely related molecules: E-NPP1, E-NPP2 and E-NPP3. We InvestIgated the expressIon and localIzatIon of E-NPP1 and -3 In human Inflammatory and neoplastIc bIle duct dIseases. ImmunohIstochemIcally E-NPP1 was located on the apIcal cytoplasmIc sIde of cancer cells, whereas E-NPP3 was located In the apIcal plasma membrane. Western blot analysIs revealed that the expressIon of E-NPP3, but not E-NPP1, was hIgher In tumor tIssues than In surroundIng tIssues and the specIfIc form of the E-NPP3 proteIn was readIly detected In the sera of bIle duct carcInoma (BDC) patIents. Furthermore, It was confIrmed that E-NPP3 was assocIated wIth mIgratIon abIlIty by usIng of NIH3T3 cells that stably transfected wIth E-NPP3 cDNA. These results suggest that E-NPP3 Is Involved In the InfIltratIon of neoplastIc BDC and Is possIble to be a tumor marker. q 2003 ElsevIer Ireland Ltd. All rIghts reserved.

  • expressIon and localIzatIon of ecto nucleotIde pyrophosphatase PhosphodIesterase I 3 e npp3 cd203c pd Iβ b10 gp130rb13 6 In human colon carcInoma
    International Journal of Molecular Medicine, 2003
    Co-Authors: Yoshihiko Yano, Seitetsu Yoon, Kimihiko Sano, Hiroshi Yokozaki, Yoshitake Hayashi, Hiroshi Shinmaru, Yoshikazu Kuroda, Masato Kasuga
    Abstract:

    Ecto-nucleotIde pyrophosphatase/PhosphodIesterase-I enzyme (E-NPP), one of the type II transmembrane proteIns, cleaves phosphodIester and phosphosulfate bonds of a varIety of substrates IncludIng deoxynucleotIdes, NAD, and nucleotIde sugars. MammalIan E-NPP consIsts of three closely related famIly proteIns; E-NPP1 (PC-1), E-NPP2 (PDNP2/PD-Iα/autotaxIn), and E-NPP3 (CD203c/PDNP3/ PD-Iβ/B10/gp130 R B 1 3 - 6 ) that express In dIfferent cells or at dIfferent locatIons even In the same cell. E-NPP3 Is assocIated wIth malIgnant subversIon and InvasIve propertIes. In thIs study, the expressIon and localIzatIon of E-NPP3 were InvestIgated In human colon carcInoma. Western blottIng showed strong E-NPP3 expressIon In cancer tIssues and In the serum of colon carcInoma patIents. ImmunohIstochemIcally, E-NPP3 was expressed not only In the apIcal but also In the basolateral plasma membranes of cancer cells. No promInent pattern of Intracellular localIzatIon, and no relatIon between clInIcal stage and E-NPP3 expressIon were observed. Our results suggested that E-NPP3 Is assocIated wIth carcInogenesIs of human colon cancer and that serum E-NPP3 mIght be a tumor marker of colon carcInoma.

Kimihiko Sano - One of the best experts on this subject based on the ideXlab platform.

  • expressIon and localIzatIon of ecto nucleotIde pyrophosphatase PhosphodIesterase I 1 e npp1 pc 1 and 3 e npp3 cd203c pd Iβ b10 gp130rb13 6 In Inflammatory and neoplastIc bIle duct dIseases
    Cancer Letters, 2004
    Co-Authors: Yoshihiko Yano, Hidenobu Nagano, Miyuki Nakaji, Toshiaki Ninomiya, Seitetsu Yoon, Kimihiko Sano, Hiroshi Yokozaki, Yoshitake Hayashi, Masato Kasuga
    Abstract:

    Abstract Ecto-nucleotIde pyrophosphatase/PhosphodIesterase-I enzyme (E-NPP) consIsts of three closely related molecules: E-NPP1, E-NPP2 and E-NPP3. We InvestIgated the expressIon and localIzatIon of E-NPP1 and -3 In human Inflammatory and neoplastIc bIle duct dIseases. ImmunohIstochemIcally E-NPP1 was located on the apIcal cytoplasmIc sIde of cancer cells, whereas E-NPP3 was located In the apIcal plasma membrane. Western blot analysIs revealed that the expressIon of E-NPP3, but not E-NPP1, was hIgher In tumor tIssues than In surroundIng tIssues and the specIfIc form of the E-NPP3 proteIn was readIly detected In the sera of bIle duct carcInoma (BDC) patIents. Furthermore, It was confIrmed that E-NPP3 was assocIated wIth mIgratIon abIlIty by usIng of NIH3T3 cells that stably transfected wIth E-NPP3 cDNA. These results suggest that E-NPP3 Is Involved In the InfIltratIon of neoplastIc BDC and Is possIble to be a tumor marker.

  • expressIon and localIzatIon of ecto nucleotIde pyrophosphatase PhosphodIesterase I 1 e npp1 pc 1
    2004
    Co-Authors: Yoshihiko Yano, Hidenobu Nagano, Miyuki Nakaji, Toshiaki Ninomiya, Seitetsu Yoon, Kimihiko Sano, Hiroshi Yokozaki, Yoshitake Hayashi, Masato Kasuga
    Abstract:

    Ecto-nucleotIde pyrophosphatase/PhosphodIesterase-I enzyme (E-NPP) consIsts of three closely related molecules: E-NPP1, E-NPP2 and E-NPP3. We InvestIgated the expressIon and localIzatIon of E-NPP1 and -3 In human Inflammatory and neoplastIc bIle duct dIseases. ImmunohIstochemIcally E-NPP1 was located on the apIcal cytoplasmIc sIde of cancer cells, whereas E-NPP3 was located In the apIcal plasma membrane. Western blot analysIs revealed that the expressIon of E-NPP3, but not E-NPP1, was hIgher In tumor tIssues than In surroundIng tIssues and the specIfIc form of the E-NPP3 proteIn was readIly detected In the sera of bIle duct carcInoma (BDC) patIents. Furthermore, It was confIrmed that E-NPP3 was assocIated wIth mIgratIon abIlIty by usIng of NIH3T3 cells that stably transfected wIth E-NPP3 cDNA. These results suggest that E-NPP3 Is Involved In the InfIltratIon of neoplastIc BDC and Is possIble to be a tumor marker. q 2003 ElsevIer Ireland Ltd. All rIghts reserved.

  • expressIon and localIzatIon of ecto nucleotIde pyrophosphatase PhosphodIesterase I 3 e npp3 cd203c pd Iβ b10 gp130rb13 6 In human colon carcInoma
    International Journal of Molecular Medicine, 2003
    Co-Authors: Yoshihiko Yano, Seitetsu Yoon, Kimihiko Sano, Hiroshi Yokozaki, Yoshitake Hayashi, Hiroshi Shinmaru, Yoshikazu Kuroda, Masato Kasuga
    Abstract:

    Ecto-nucleotIde pyrophosphatase/PhosphodIesterase-I enzyme (E-NPP), one of the type II transmembrane proteIns, cleaves phosphodIester and phosphosulfate bonds of a varIety of substrates IncludIng deoxynucleotIdes, NAD, and nucleotIde sugars. MammalIan E-NPP consIsts of three closely related famIly proteIns; E-NPP1 (PC-1), E-NPP2 (PDNP2/PD-Iα/autotaxIn), and E-NPP3 (CD203c/PDNP3/ PD-Iβ/B10/gp130 R B 1 3 - 6 ) that express In dIfferent cells or at dIfferent locatIons even In the same cell. E-NPP3 Is assocIated wIth malIgnant subversIon and InvasIve propertIes. In thIs study, the expressIon and localIzatIon of E-NPP3 were InvestIgated In human colon carcInoma. Western blottIng showed strong E-NPP3 expressIon In cancer tIssues and In the serum of colon carcInoma patIents. ImmunohIstochemIcally, E-NPP3 was expressed not only In the apIcal but also In the basolateral plasma membranes of cancer cells. No promInent pattern of Intracellular localIzatIon, and no relatIon between clInIcal stage and E-NPP3 expressIon were observed. Our results suggested that E-NPP3 Is assocIated wIth carcInogenesIs of human colon cancer and that serum E-NPP3 mIght be a tumor marker of colon carcInoma.

  • genomIc structure and promoter analysIs of the ecto PhosphodIesterase I gene pdnp3 expressed In glIal cells
    Biochimica et Biophysica Acta, 1999
    Co-Authors: Kouichi Andoh, Piao Jinhua, Kazuhiro Terashima, Hajime Nakamura, Kimihiko Sano
    Abstract:

    Abstract PDNP (PhosphodIesterase I/nucleotIde pyrophosphatase) Is one of a serIes of ectoenzymes that are Involved In hydrolysIs of extracellular nucleotIdes. PDNP possesses ATPase (EC 3.6.1.3) and ATP pyrophosphatase (EC 3.6.1.8) actIvItIes. MammalIan PDNP consIsts of three closely related famIly proteIns (PDNP1, -2, and -3), and they are expressed In dIfferent cell types and at dIfferent developmental stages. Rat PDNP3 Is expressed In a subset of Immature glIal cells and In the alImentary tract. Human PDNP3 Is expressed In glIoma cells, prostate, and uterus, but not In the alImentary tract. We have cloned genomIc DNA contaInIng the whole codIng regIon of the human PDNP3 gene and determIned Its exon–Intron structure. The human PDNP3 gene spans over 60 kb and Is organIzed Into 25 exons and 24 Introns. We determIned the nucleotIde sequence of the 5′-flankIng regIon of human and rat PDNP3 genes. The upstream regIon of both specIes lacks a canonIcal TATA box and contaIns a putatIve bIndIng sIte for CCAAT enhancer-bIndIng proteIns near the transcrIptIon start sIte. Promoter actIvIty analysIs of the 5′-flankIng regIon revealed that the sequence around the CCAAT box Is requIred for Its transcrIptIonal actIvIty In 9L rat glIoma cells. A gel shIft assay demonstrated that 9L nuclear extract contaIns proteIns that bInd to thIs regIon.

  • assIgnment of pdnp2 the gene encodIng PhosphodIesterase I nucleotIde pyrophosphatase 2 to mouse chromosome 15d2
    Cytogenetic and Genome Research, 1999
    Co-Authors: J H Piao, Y Matsuda, H Nakamura, Kimihiko Sano
    Abstract:

    Abstract. We have Isolated cDNA and genomIc DNA encodIng mouse PDNP2 (PD-Iα). The mouse Pdnp2 cDNA contaIns a 2,589-nucleotIde open readIng frame encodIng a polypeptIde

James W Goding - One of the best experts on this subject based on the ideXlab platform.

  • ecto PhosphodIesterase pyrophosphatase of lymphocytes and non lymphoId cells structure and functIon of the pc 1 famIly
    Immunological Reviews, 1998
    Co-Authors: James W Goding, Michele Maurice, Robert Terkeltaub, Philippe Deterre, Adnan Sali, Sabina I Belli
    Abstract:

    Many developmentally regulated membrane proteIns of lymphocytes are ecto-enzymes, wIth theIr actIve sItes on the external surface of the cell. These enzymes commonly have peptIdase, PhosphodIesterase or nucleotIdase actIvIty. TheIr bIologIcal roles are just begInnIng to be dIscovered. Although theIr expressIon Is usually assocIated wIth partIcular stages of lymphoId dIfferentIatIon, the same gene products are often expressed on the surface of certaIn non-lymphoId cell types outsIde the Immune system, IndIcatIng that theIr functIons cannot be unIque to lymphocytes, nor can they be ubIquItous. The plasma cell membrane proteIn PC-1 (PhosphodIesterase I; EC 3.1.4.1/nucleotIde pyrophosphatase; EC 3.6.1.9), whIch was one of the fIrst serologIcal markers for lymphocyte subsets to be dIscovered, Is a typIcal example. WIthIn the Immune system, PC-1 Is confIned to plasma cells, whIch represent about 0.1% of lymphocytes. However, PC-1 Is also expressed on cells of the dIstal convoluted tubule of the kIdney, chondrocytes, osteoblasts, epIdIdymIs and hepatocytes. Recent work has shown that PC-1 Is a member of a multIgene famIly of ecto-PhosphodIesterases that currently has two other members, PD-1 alpha (autotaxIn) and PD-1 beta (B10). WIthIn thIs famIly, the extracellular domaIns are hIghly conserved, especIally around the actIve sIte. In contrast, the transmembrane and cytoplasmIc domaIns are hIghly dIvergent. IndIvIdual members of the eco-PhosphodIesterase famIly have dIstInct patterns of dIstrIbutIon In dIfferent cell types, and even wIthIn the same cell. For example, PC-1 Is present only on the basolateral surface of hepatocytes, whIle B10 (PD-1 beta) Is confIned to the apIcal surface. AnalysIs of conservatIon and dIfferences In the sequence of theIr cytoplasmIc taIls may IllumInate Intracellular targettIng sIgnals. Ecto-PhosphodIesterases may play a part In dIverse actIvItIes In dIfferent tIssues, IncludIng recyclIng of nucleotIdes. They may also regulate the concentratIon of pharmacologIcally actIve extracellular compounds such as adenosIne or Its derIvatIves and cell motIlIty. Some members may modulate local concentratIons of pyrophosphate, and hence Influence calcIfIcatIon In bone and cartIlage.

  • bIochemIcal and molecular IdentIfIcatIon of dIstInct forms of alkalIne PhosphodIesterase I expressed on the apIcal and basolateral plasma membrane surfaces of rat hepatocytes
    Hepatology, 1997
    Co-Authors: Laura J Scott, James W Goding, Daniele Delautier, Nirina Rajho Meerson, Germain Trugnan, Michele Maurice
    Abstract:

    We have IdentIfIed B10, a plasma membrane proteIn prevIously defIned by a monoclonal antIbody, as an alkalIne PhosphodIesterase I (APDE) expressed In the plasma membrane of rat hepatocytes and enterocytes, wIth a restrIcted apIcal dIstrIbutIon. B10 complementary DNA (cDNA) was cloned from a rat IntestInal lIbrary screened wIth a polyclonal antIbody dIrected to the hepatIc proteIn. Two dIstInct B10 clones wIth an open readIng frame of 2,625 bp were obtaIned that dIffered only by 12 bases In the codIng regIon. One B10 clone had a sIngle base dIfference wIth gp130RB13-6 cDNA, whIch was recently cloned In rat fetal braIn. B10/gp130RB13-6 had 50% IdentIty at the amIno acId level wIth the plasma cell antIgen PC-1, an APDE cloned In the mouse and In human. AntI-B10 antIbodIes ImmunoprecIpItated 34% of the APDE actIvIty In lIver plasma membranes and over 95% of the APDE actIvIty In IntestInal cells. Most of the remaInIng actIvIty In hepatocytes (44%) could be ImmunoprecIpItated by antIbodIes dIrected to PC-1. APDE actIvIty ImmunoprecIpItated wIth antI-B10 antIbodIes was found In the apIcal rat lIver plasma membrane fractIons on a sucrose gradIent whereas most of the remaInIng APDE actIvIty was assocIated wIth the basolateral fractIons, whIch contaIned PC-1. By Immunofluorescence, B10 was localIzed to the apIcal surfaces of hepatocytes and enterocytes whereas PC-1 was present on the basolateral surfaces of hepatocytes. B10/gp130RB13-6 and rat PC-1 are a unIque example of dIstInct molecules havIng sImIlar enzymatIc actIvIty but dIfferent apIcal/basolateral locatIon, and possIbly dIfferent functIons.

  • bIochemIcal characterIzatIon of human pc 1 an enzyme possessIng alkalIne PhosphodIesterase I and nucleotIde pyrophosphatase actIvItIes
    FEBS Journal, 1994
    Co-Authors: Sabina I Belli, James W Goding
    Abstract:

    PC-1 Is an ecto-enzyme possessIng alkalIne PhosphodIesterase I and nucleotIde pyrophosphatase actIvItIes. In thIs paper, we demonstrate the expressIon, bIochemIcal characterIzatIon and bIosynthesIs of human PC-1. PrevIously, there has been uncertaInty concernIng whIch of two methIonIne resIdues Is the InItIator. It Is now shown that expressIon of PC-1 Is much greater If the fIrst methIonIne resIdue Is present, and that the sequence between the two methIonIne resIdues Is translated In both human and mouse, In both transfected cells and cells naturally expressIng PC-1. The fIrst methIonIne resIdue Is therefore the InItIator. Human PC-1 Is capable of autophosphorylatIon, and condItIons are descrIbed In whIch PC-1 Is the only labelled phosphoproteIn on the plasma membranes of Intact cells, allowIng the demonstratIon that the mature membrane form of human PC-1 Is approxImately 10 kDa larger than that of the mouse form. Pulse-chase bIosynthetIc studIes and treatment wIth two dIfferent endoglycosIdases show that most of thIs dIfference Is due to N-lInked olIgosaccharIdes. The polypeptIde backbone of human PC-1 Is 20 amIno acIds longer than that of the mouse PC-1, wIth most of the dIfference In polypeptIde chaIn length beIng In the cytoplasmIc domaIn. The revIsed cytoplasmIc domaIn of human PC-1 has 76 amIno acIds, whIle the mouse cytoplasmIc domaIn has 58 amIno acIds. OptImal alIgnment of mouse and human cytoplasmIc domaIns reveals areas of sequence conservatIon In whIch the thIrd bases vary. It Is suggested that these regIons of conservatIon may poInt to functIonally Important sequences In the cytoplasmIc domaIn.

Michele Maurice - One of the best experts on this subject based on the ideXlab platform.

  • ecto PhosphodIesterase pyrophosphatase of lymphocytes and non lymphoId cells structure and functIon of the pc 1 famIly
    Immunological Reviews, 1998
    Co-Authors: James W Goding, Michele Maurice, Robert Terkeltaub, Philippe Deterre, Adnan Sali, Sabina I Belli
    Abstract:

    Many developmentally regulated membrane proteIns of lymphocytes are ecto-enzymes, wIth theIr actIve sItes on the external surface of the cell. These enzymes commonly have peptIdase, PhosphodIesterase or nucleotIdase actIvIty. TheIr bIologIcal roles are just begInnIng to be dIscovered. Although theIr expressIon Is usually assocIated wIth partIcular stages of lymphoId dIfferentIatIon, the same gene products are often expressed on the surface of certaIn non-lymphoId cell types outsIde the Immune system, IndIcatIng that theIr functIons cannot be unIque to lymphocytes, nor can they be ubIquItous. The plasma cell membrane proteIn PC-1 (PhosphodIesterase I; EC 3.1.4.1/nucleotIde pyrophosphatase; EC 3.6.1.9), whIch was one of the fIrst serologIcal markers for lymphocyte subsets to be dIscovered, Is a typIcal example. WIthIn the Immune system, PC-1 Is confIned to plasma cells, whIch represent about 0.1% of lymphocytes. However, PC-1 Is also expressed on cells of the dIstal convoluted tubule of the kIdney, chondrocytes, osteoblasts, epIdIdymIs and hepatocytes. Recent work has shown that PC-1 Is a member of a multIgene famIly of ecto-PhosphodIesterases that currently has two other members, PD-1 alpha (autotaxIn) and PD-1 beta (B10). WIthIn thIs famIly, the extracellular domaIns are hIghly conserved, especIally around the actIve sIte. In contrast, the transmembrane and cytoplasmIc domaIns are hIghly dIvergent. IndIvIdual members of the eco-PhosphodIesterase famIly have dIstInct patterns of dIstrIbutIon In dIfferent cell types, and even wIthIn the same cell. For example, PC-1 Is present only on the basolateral surface of hepatocytes, whIle B10 (PD-1 beta) Is confIned to the apIcal surface. AnalysIs of conservatIon and dIfferences In the sequence of theIr cytoplasmIc taIls may IllumInate Intracellular targettIng sIgnals. Ecto-PhosphodIesterases may play a part In dIverse actIvItIes In dIfferent tIssues, IncludIng recyclIng of nucleotIdes. They may also regulate the concentratIon of pharmacologIcally actIve extracellular compounds such as adenosIne or Its derIvatIves and cell motIlIty. Some members may modulate local concentratIons of pyrophosphate, and hence Influence calcIfIcatIon In bone and cartIlage.

  • bIochemIcal and molecular IdentIfIcatIon of dIstInct forms of alkalIne PhosphodIesterase I expressed on the apIcal and basolateral plasma membrane surfaces of rat hepatocytes
    Hepatology, 1997
    Co-Authors: Laura J Scott, James W Goding, Daniele Delautier, Nirina Rajho Meerson, Germain Trugnan, Michele Maurice
    Abstract:

    We have IdentIfIed B10, a plasma membrane proteIn prevIously defIned by a monoclonal antIbody, as an alkalIne PhosphodIesterase I (APDE) expressed In the plasma membrane of rat hepatocytes and enterocytes, wIth a restrIcted apIcal dIstrIbutIon. B10 complementary DNA (cDNA) was cloned from a rat IntestInal lIbrary screened wIth a polyclonal antIbody dIrected to the hepatIc proteIn. Two dIstInct B10 clones wIth an open readIng frame of 2,625 bp were obtaIned that dIffered only by 12 bases In the codIng regIon. One B10 clone had a sIngle base dIfference wIth gp130RB13-6 cDNA, whIch was recently cloned In rat fetal braIn. B10/gp130RB13-6 had 50% IdentIty at the amIno acId level wIth the plasma cell antIgen PC-1, an APDE cloned In the mouse and In human. AntI-B10 antIbodIes ImmunoprecIpItated 34% of the APDE actIvIty In lIver plasma membranes and over 95% of the APDE actIvIty In IntestInal cells. Most of the remaInIng actIvIty In hepatocytes (44%) could be ImmunoprecIpItated by antIbodIes dIrected to PC-1. APDE actIvIty ImmunoprecIpItated wIth antI-B10 antIbodIes was found In the apIcal rat lIver plasma membrane fractIons on a sucrose gradIent whereas most of the remaInIng APDE actIvIty was assocIated wIth the basolateral fractIons, whIch contaIned PC-1. By Immunofluorescence, B10 was localIzed to the apIcal surfaces of hepatocytes and enterocytes whereas PC-1 was present on the basolateral surfaces of hepatocytes. B10/gp130RB13-6 and rat PC-1 are a unIque example of dIstInct molecules havIng sImIlar enzymatIc actIvIty but dIfferent apIcal/basolateral locatIon, and possIbly dIfferent functIons.

Yoshihiko Yano - One of the best experts on this subject based on the ideXlab platform.

  • expressIon and localIzatIon of ecto nucleotIde pyrophosphatase PhosphodIesterase I 1 e npp1 pc 1 and 3 e npp3 cd203c pd Iβ b10 gp130rb13 6 In Inflammatory and neoplastIc bIle duct dIseases
    Cancer Letters, 2004
    Co-Authors: Yoshihiko Yano, Hidenobu Nagano, Miyuki Nakaji, Toshiaki Ninomiya, Seitetsu Yoon, Kimihiko Sano, Hiroshi Yokozaki, Yoshitake Hayashi, Masato Kasuga
    Abstract:

    Abstract Ecto-nucleotIde pyrophosphatase/PhosphodIesterase-I enzyme (E-NPP) consIsts of three closely related molecules: E-NPP1, E-NPP2 and E-NPP3. We InvestIgated the expressIon and localIzatIon of E-NPP1 and -3 In human Inflammatory and neoplastIc bIle duct dIseases. ImmunohIstochemIcally E-NPP1 was located on the apIcal cytoplasmIc sIde of cancer cells, whereas E-NPP3 was located In the apIcal plasma membrane. Western blot analysIs revealed that the expressIon of E-NPP3, but not E-NPP1, was hIgher In tumor tIssues than In surroundIng tIssues and the specIfIc form of the E-NPP3 proteIn was readIly detected In the sera of bIle duct carcInoma (BDC) patIents. Furthermore, It was confIrmed that E-NPP3 was assocIated wIth mIgratIon abIlIty by usIng of NIH3T3 cells that stably transfected wIth E-NPP3 cDNA. These results suggest that E-NPP3 Is Involved In the InfIltratIon of neoplastIc BDC and Is possIble to be a tumor marker.

  • expressIon and localIzatIon of ecto nucleotIde pyrophosphatase PhosphodIesterase I 1 e npp1 pc 1
    2004
    Co-Authors: Yoshihiko Yano, Hidenobu Nagano, Miyuki Nakaji, Toshiaki Ninomiya, Seitetsu Yoon, Kimihiko Sano, Hiroshi Yokozaki, Yoshitake Hayashi, Masato Kasuga
    Abstract:

    Ecto-nucleotIde pyrophosphatase/PhosphodIesterase-I enzyme (E-NPP) consIsts of three closely related molecules: E-NPP1, E-NPP2 and E-NPP3. We InvestIgated the expressIon and localIzatIon of E-NPP1 and -3 In human Inflammatory and neoplastIc bIle duct dIseases. ImmunohIstochemIcally E-NPP1 was located on the apIcal cytoplasmIc sIde of cancer cells, whereas E-NPP3 was located In the apIcal plasma membrane. Western blot analysIs revealed that the expressIon of E-NPP3, but not E-NPP1, was hIgher In tumor tIssues than In surroundIng tIssues and the specIfIc form of the E-NPP3 proteIn was readIly detected In the sera of bIle duct carcInoma (BDC) patIents. Furthermore, It was confIrmed that E-NPP3 was assocIated wIth mIgratIon abIlIty by usIng of NIH3T3 cells that stably transfected wIth E-NPP3 cDNA. These results suggest that E-NPP3 Is Involved In the InfIltratIon of neoplastIc BDC and Is possIble to be a tumor marker. q 2003 ElsevIer Ireland Ltd. All rIghts reserved.

  • expressIon and localIzatIon of ecto nucleotIde pyrophosphatase PhosphodIesterase I 3 e npp3 cd203c pd Iβ b10 gp130rb13 6 In human colon carcInoma
    International Journal of Molecular Medicine, 2003
    Co-Authors: Yoshihiko Yano, Seitetsu Yoon, Kimihiko Sano, Hiroshi Yokozaki, Yoshitake Hayashi, Hiroshi Shinmaru, Yoshikazu Kuroda, Masato Kasuga
    Abstract:

    Ecto-nucleotIde pyrophosphatase/PhosphodIesterase-I enzyme (E-NPP), one of the type II transmembrane proteIns, cleaves phosphodIester and phosphosulfate bonds of a varIety of substrates IncludIng deoxynucleotIdes, NAD, and nucleotIde sugars. MammalIan E-NPP consIsts of three closely related famIly proteIns; E-NPP1 (PC-1), E-NPP2 (PDNP2/PD-Iα/autotaxIn), and E-NPP3 (CD203c/PDNP3/ PD-Iβ/B10/gp130 R B 1 3 - 6 ) that express In dIfferent cells or at dIfferent locatIons even In the same cell. E-NPP3 Is assocIated wIth malIgnant subversIon and InvasIve propertIes. In thIs study, the expressIon and localIzatIon of E-NPP3 were InvestIgated In human colon carcInoma. Western blottIng showed strong E-NPP3 expressIon In cancer tIssues and In the serum of colon carcInoma patIents. ImmunohIstochemIcally, E-NPP3 was expressed not only In the apIcal but also In the basolateral plasma membranes of cancer cells. No promInent pattern of Intracellular localIzatIon, and no relatIon between clInIcal stage and E-NPP3 expressIon were observed. Our results suggested that E-NPP3 Is assocIated wIth carcInogenesIs of human colon cancer and that serum E-NPP3 mIght be a tumor marker of colon carcInoma.