메뉴 건너뛰기




Volumn 204, Issue 1-2, 1997, Pages 5-16

Characterization and chromosomal localization of PTPRO, a novel receptor protein tyrosine phosphatase, expressed in hematopoietic stem cells

Author keywords

Hematopoietic stem cells; Homotypically adherent protein tyrosine phosphatases; Tyrosine phosphatases

Indexed keywords

CD34 ANTIGEN; COMPLEMENTARY DNA; DNA; FLUOROURACIL; PROTEIN TYROSINE PHOSPHATASE; RECEPTOR PROTEIN;

EID: 0031578834     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(97)00420-4     Document Type: Article
Times cited : (17)

References (41)
  • 2
    • 0026730776 scopus 로고
    • Interaction of human bone marrow fibroblasts with megakaryocytes: Role of the c-kit ligand
    • Avraham H., Scadden D.T., Chi S., Broudy V., Zsebo K., Groopman J.E. Interaction of human bone marrow fibroblasts with megakaryocytes: role of the c-kit ligand. Blood. 80:1992;1679-1684.
    • (1992) Blood , vol.80 , pp. 1679-1684
    • Avraham, H.1    Scadden, D.T.2    Chi, S.3    Broudy, V.4    Zsebo, K.5    Groopman, J.E.6
  • 3
    • 0027296921 scopus 로고
    • Homophilic binding of PTPμ, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation
    • Brady-Kalnay S.M., Flint A.J., Tonks N.K. Homophilic binding of PTPμ, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation. J. Cell Biol. 122:1993;961-972.
    • (1993) J. Cell Biol. , vol.122 , pp. 961-972
    • Brady-Kalnay, S.M.1    Flint, A.J.2    Tonks, N.K.3
  • 4
    • 0027756206 scopus 로고
    • Purification and characterization of the human protein tyrosine phosphatase, PTPu, from a baculovirus expression system
    • Brady-Kalnay, S.M., Tonks, N.K. 1993. Purification and characterization of the human protein tyrosine phosphatase, PTPu, from a baculovirus expression system. Mol. Cell. Biol. 127/128, 131-141.
    • (1993) Mol. Cell. Biol. , vol.127-128 , pp. 131-141
    • Brady-Kalnay, S.M.1    Tonks, N.K.2
  • 5
    • 0027938304 scopus 로고
    • Identification of the homophilic binding site of the receptor protein tyrosine phosphatase PTPμ
    • Brady-Kalnay S.M., Tonks N.K. Identification of the homophilic binding site of the receptor protein tyrosine phosphatase PTPμ J. Biol. Chem. 269:1994;28472-28477.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28472-28477
    • Brady-Kalnay, S.M.1    Tonks, N.K.2
  • 6
    • 0029149746 scopus 로고
    • Receptor protein tyrosine phosphatase PTPμ associates with cadherins and catenins in vivo
    • Brady-Kalnay S.M., Rimm D.L., Tonks N.K. Receptor protein tyrosine phosphatase PTPμ associates with cadherins and catenins in vivo. J. Cell Biol. 130:1995;977-986.
    • (1995) J. Cell Biol. , vol.130 , pp. 977-986
    • Brady-Kalnay, S.M.1    Rimm, D.L.2    Tonks, N.K.3
  • 9
    • 0027723985 scopus 로고
    • Stromal cells in long-term cultures: Keys to the elucidation of hematopoietic development?
    • Deryugina E., Muller-Sieberg C. Stromal cells in long-term cultures: keys to the elucidation of hematopoietic development? Crit. Rev. Immunol. 13:1993;115-150.
    • (1993) Crit. Rev. Immunol. , vol.13 , pp. 115-150
    • Deryugina, E.1    Muller-Sieberg, C.2
  • 10
    • 0025817934 scopus 로고
    • Cell adhesion molecules: Implications for a molecular histology
    • Edelman G.M., Crossin K.L. Cell adhesion molecules: implications for a molecular histology. Annu. Rev. Biochem. 60:1991;155-190.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 155-190
    • Edelman, G.M.1    Crossin, K.L.2
  • 12
    • 0026584285 scopus 로고
    • The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence
    • Frangioni J.V., Beahm P.H., Shifrin V., Jost C.A., Neel B.G. The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence. Cell. 68:1992;545-560.
    • (1992) Cell , vol.68 , pp. 545-560
    • Frangioni, J.V.1    Beahm, P.H.2    Shifrin, V.3    Jost, C.A.4    Neel, B.G.5
  • 14
    • 0027753294 scopus 로고
    • Purification and characterization of the cytoplasmic domain of human receptor-like protein tyrosine phosphatase RPTPμ
    • Gebbink M.F.B.G., Verheijen M.H.G., Zondag G.C.M., van Etten I., Moolenaar W.H. Purification and characterization of the cytoplasmic domain of human receptor-like protein tyrosine phosphatase RPTPμ Biochemistry. 32:1993;13516-13522.
    • (1993) Biochemistry , vol.32 , pp. 13516-13522
    • Gebbink, M.F.B.G.1    Verheijen, M.H.G.2    Zondag, G.C.M.3    Van Etten, I.4    Moolenaar, W.H.5
  • 16
    • 0027034047 scopus 로고
    • The haematopoietic stem cells: Properties and control mechanisms
    • Graham G., Pragnell I.B. The haematopoietic stem cells: properties and control mechanisms. Semin. Cell Biol. 3:1992;423-434.
    • (1992) Semin. Cell Biol. , vol.3 , pp. 423-434
    • Graham, G.1    Pragnell, I.B.2
  • 18
    • 0027312030 scopus 로고
    • Cloning and characterization of R-PTP-κ, a new member of the receptor protein tyrosine phosphatase family with a proteolytically cleaved cellular adhesion molecule-like extracellular region
    • Jiang Y.-P., Wang H., D'Eustachio P., Musacchio J.M., Schlessinger J., Sap J. Cloning and characterization of R-PTP-κ, a new member of the receptor protein tyrosine phosphatase family with a proteolytically cleaved cellular adhesion molecule-like extracellular region. Mol. Cell. Biol. 13:1993;2942-2951.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2942-2951
    • Jiang, Y.-P.1    Wang, H.2    D'Eustachio, P.3    Musacchio, J.M.4    Schlessinger, J.5    Sap, J.6
  • 19
    • 0025146562 scopus 로고
    • Structural diversity and evolution of human receptor-like protein tyrosine phosphatases
    • Krueger N.X., Streuli M., Saito H. Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. EMBO J. 9:1990;3241-3252.
    • (1990) EMBO J. , vol.9 , pp. 3241-3252
    • Krueger, N.X.1    Streuli, M.2    Saito, H.3
  • 20
    • 0027432407 scopus 로고
    • Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor
    • Lechleider R.J., Sugimoto S., Bennett A.M., Kashishian A.S., Cooper J.A., Shoelson S.E., Walsh C.T., Neel B.G. Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor. J. Biol. Chem. 268:1993;21478-21481.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21478-21481
    • Lechleider, R.J.1    Sugimoto, S.2    Bennett, A.M.3    Kashishian, A.S.4    Cooper, J.A.5    Shoelson, S.E.6    Walsh, C.T.7    Neel, B.G.8
  • 21
    • 0025138652 scopus 로고
    • 5-Fluorouracil spares hemopoietic stem cells responsible for long-term repopulation
    • Lerner C., Harrison D.E. 5-Fluorouracil spares hemopoietic stem cells responsible for long-term repopulation. Exp. Hematol. 18:1990;114-118.
    • (1990) Exp. Hematol. , vol.18 , pp. 114-118
    • Lerner, C.1    Harrison, D.E.2
  • 22
    • 0026742211 scopus 로고
    • Characterization of hematopoietic intracellular protein tyrosine phosphatases: Description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences
    • Matthews R.J., Bowne D.B., Flores E., Thomas M.L. Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences. Mol. Cell. Biol. 12:1992;2396-2405.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2396-2405
    • Matthews, R.J.1    Bowne, D.B.2    Flores, E.3    Thomas, M.L.4
  • 25
    • 0029796633 scopus 로고    scopus 로고
    • Long-term lymphohematopoietic reconstitution by a single CD34-low/negative hematopoietic stem cell
    • Osawa M., Hanada K., Hamada H., Nakauchi H. Long-term lymphohematopoietic reconstitution by a single CD34-low/negative hematopoietic stem cell. Science. 273:1996;242-245.
    • (1996) Science , vol.273 , pp. 242-245
    • Osawa, M.1    Hanada, K.2    Hamada, H.3    Nakauchi, H.4
  • 26
    • 0028051306 scopus 로고
    • Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density
    • Ostman A., Yang Q., Tonks N.K. Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density. Proc. Natl. Acad. Sci. USA. 91:1994;9680-9684.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9680-9684
    • Ostman, A.1    Yang, Q.2    Tonks, N.K.3
  • 27
    • 0029349179 scopus 로고
    • Receptor tyrosine kinases and the regulation of hematopoiesis
    • Paulson R.F., Bernstein A. Receptor tyrosine kinases and the regulation of hematopoiesis. Semin. Immunol. 7:1995;267-277.
    • (1995) Semin. Immunol. , vol.7 , pp. 267-277
    • Paulson, R.F.1    Bernstein, A.2
  • 28
    • 0026038524 scopus 로고
    • Cloning, bacterial expression, purification, and characterization of the cytoplasmic domain of rat LAR, a receptor-like protein tyrosine phosphatase
    • Pot D.A., Woodford T.A., Remboutsika E., Huan R.S., Dixon J.E. Cloning, bacterial expression, purification, and characterization of the cytoplasmic domain of rat LAR, a receptor-like protein tyrosine phosphatase. J. Biol. Chem. 266:1991;19688-19696.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19688-19696
    • Pot, D.A.1    Woodford, T.A.2    Remboutsika, E.3    Huan, R.S.4    Dixon, J.E.5
  • 29
    • 0029417204 scopus 로고
    • The LAR/PTPδ/PTPσ subfamily of transmembrane protein-tyrosine-phosphatases: Multiple human LAR, PTPδ, and PTPσ isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1
    • Pulido R., Serra-Pages C., Tang M., Streuli M. The LAR/PTPδ/PTPσ subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTPδ, and PTPσ isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1. Proc. Natl. Acad. Sci. USA. 92:1995;11686-11690.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11686-11690
    • Pulido, R.1    Serra-Pages, C.2    Tang, M.3    Streuli, M.4
  • 31
  • 33
    • 0025016163 scopus 로고
    • Resting and activated subsets of mouse multipotent hematopoietic stem cells
    • Spangrude G.J., Johnson G.R. Resting and activated subsets of mouse multipotent hematopoietic stem cells. Proc. Natl. Acad. Sci. USA. 87:1990;7433-7437.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7433-7437
    • Spangrude, G.J.1    Johnson, G.R.2
  • 34
    • 0023636055 scopus 로고
    • Differential usage of three exams generates at least five different mRNAs encoding human leukocyte common antigens
    • Streuli M., Hall L.R., Saga Y., Schlossman S.F., Saito H. Differential usage of three exams generates at least five different mRNAs encoding human leukocyte common antigens. J. Exp. Med. 166:1987;1548-1566.
    • (1987) J. Exp. Med. , vol.166 , pp. 1548-1566
    • Streuli, M.1    Hall, L.R.2    Saga, Y.3    Schlossman, S.F.4    Saito, H.5
  • 35
    • 0025277449 scopus 로고
    • Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR
    • Streuli M., Krueger N.X., Thai T., Tang M., Saito H. Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR. EMBO J. 9:1990;2399-2407.
    • (1990) EMBO J. , vol.9 , pp. 2399-2407
    • Streuli, M.1    Krueger, N.X.2    Thai, T.3    Tang, M.4    Saito, H.5
  • 36
    • 0028149381 scopus 로고
    • The coordinated action of protein tyrosine phosphatases and kinases in cell signaling
    • Sun H., Tonks N.K. The coordinated action of protein tyrosine phosphatases and kinases in cell signaling. Trends Biochem. Sci. 19:1994;480-485.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 480-485
    • Sun, H.1    Tonks, N.K.2
  • 37
    • 0028072331 scopus 로고
    • An adhesion molecule-like protein that interacts with and is a substrate for a Drosophila receptor-linked protein tyrosine phosphatase
    • Tian S.-S., Zinn K. An adhesion molecule-like protein that interacts with and is a substrate for a Drosophila receptor-linked protein tyrosine phosphatase. J. Biol. Chem. 269:1994;28476-28486.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28476-28486
    • Tian, S.-S.1    Zinn, K.2
  • 39
    • 0030010991 scopus 로고    scopus 로고
    • Characterization of PCP-2, a novel receptor protein tyrosine phosphatase of the MAM domain family
    • Wang H., Lian Z., Lerch M.M., Chen Z., Xie W., Ullrich A. Characterization of PCP-2, a novel receptor protein tyrosine phosphatase of the MAM domain family. Oncogene. 12:1996;2555-2562.
    • (1996) Oncogene , vol.12 , pp. 2555-2562
    • Wang, H.1    Lian, Z.2    Lerch, M.M.3    Chen, Z.4    Xie, W.5    Ullrich, A.6
  • 40
    • 0026922667 scopus 로고
    • The murine pallid mutation is a platelet storage pool disease associated with the protein 4.4 (pallidin) gene
    • White R.A., Peters L.L., Adkison L.R., Korsgren C., Cohen C.M., Lux S.E. The murine pallid mutation is a platelet storage pool disease associated with the protein 4.4 (pallidin) gene. Nature Genet. 2:1992;80-83.
    • (1992) Nature Genet. , vol.2 , pp. 80-83
    • White, R.A.1    Peters, L.L.2    Adkison, L.R.3    Korsgren, C.4    Cohen, C.M.5    Lux, S.E.6
  • 41
    • 0029005270 scopus 로고
    • Homophilic interactions mediated by receptor tyrosine phosphatases μ and κ: A critical role for the novel extracellular MAM domain
    • Zondag G.C.M., Koningstein G.M., Jiang Y.-P., Sap J., Moolenaar W.H., Gebbink M.F.B.G. Homophilic interactions mediated by receptor tyrosine phosphatases μ and κ: a critical role for the novel extracellular MAM domain. J. Biol. Chem. 270:1995;14247-14250.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14247-14250
    • Zondag, G.C.M.1    Koningstein, G.M.2    Jiang, Y.-P.3    Sap, J.4    Moolenaar, W.H.5    Gebbink, M.F.B.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.