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Volumn 58, Issue 4, 2004, Pages 394-405

Cell Specific Expression of CD10/Neutral Endopeptidase 24.11 Gene in Human Prostatic Tissue and Cells

Author keywords

EP; Gene expression; Immunofluorescence; In situ RT PCR; Prostate

Indexed keywords

CELL EXTRACT; COMMON ACUTE LYMPHOBLASTIC LEUKEMIA ANTIGEN; MEMBRANE METALLOENDOPEPTIDASE; METALLOPROTEINASE;

EID: 1542347763     PISSN: 02704137     EISSN: None     Source Type: Journal    
DOI: 10.1002/pros.10345     Document Type: Article
Times cited : (11)

References (68)
  • 1
    • 0021750181 scopus 로고
    • Inactivation of neurotensin by rat brain synaptic membranes. Cleavage at the Pro1O-Tyr11 bond by endopeptidase 24.11 (enkephalinase) and a peptidase different from proline-endopeptidase
    • Checler F, Emson PC, Vincent JP, Kitabgi P. Inactivation of neurotensin by rat brain synaptic membranes. Cleavage at the Pro1O-Tyr11 bond by endopeptidase 24.11 (enkephalinase) and a peptidase different from proline-endopeptidase. J Neurochem 1984;43(5):1295-1301.
    • (1984) J Neurochem , vol.43 , Issue.5 , pp. 1295-1301
    • Checler, F.1    Emson, P.C.2    Vincent, J.P.3    Kitabgi, P.4
  • 2
    • 0027199490 scopus 로고
    • Endopeptidase-24.11: Putative substrates and possible roles
    • Kenny J. Endopeptidase-24.11: Putative substrates and possible roles. Biochem Soc Trans 1993;21(Pt 3)(3):663-668.
    • (1993) Biochem Soc Trans , vol.21 , Issue.3 PART 3 , pp. 663-668
    • Kenny, J.1
  • 3
    • 0025885695 scopus 로고
    • CD10/neutral endopeptidase 24.11 hydrolyzes bombesin-like peptides and regulates the growth of small cell carcinomas of the lung
    • Shipp MA, Tarr GE, Chen CY, Switzer SN, Hersh LB, Stein H, Sunday ME, Reinherz EL. CD10/neutral endopeptidase 24.11 hydrolyzes bombesin-like peptides and regulates the growth of small cell carcinomas of the lung. Proc Natl Acad Sci USA 1991;88(23):10662-10666.
    • (1991) Proc Natl Acad Sci USA , vol.88 , Issue.23 , pp. 10662-10666
    • Shipp, M.A.1    Tarr, G.E.2    Chen, C.Y.3    Switzer, S.N.4    Hersh, L.B.5    Stein, H.6    Sunday, M.E.7    Reinherz, E.L.8
  • 4
    • 0033709265 scopus 로고    scopus 로고
    • Immunohistochemical detection of CD10 in paraffin sections of hematopoietic neoplasms: A comparison with flow cytometry detection in 56 cases
    • Chu PG, Chang KL, Weiss LM, Arber DA. Immunohistochemical detection of CD10 in paraffin sections of hematopoietic neoplasms: A comparison with flow cytometry detection in 56 cases. Appl Immunohistochem Mol Morphol 2000;8(4):257-262.
    • (2000) Appl Immunohistochem Mol Morphol , vol.8 , Issue.4 , pp. 257-262
    • Chu, P.G.1    Chang, K.L.2    Weiss, L.M.3    Arber, D.A.4
  • 5
    • 0032895567 scopus 로고    scopus 로고
    • Breast cancer cell-associated endopeptidase EC 24.11 modulates proliferative response to bombesin
    • Burns DM, Walker B, Gray J, Nelson J. Breast cancer cell-associated endopeptidase EC 24.11 modulates proliferative response to bombesin. Br J Cancer 1999;79(2):214-220.
    • (1999) Br J Cancer , vol.79 , Issue.2 , pp. 214-220
    • Burns, D.M.1    Walker, B.2    Gray, J.3    Nelson, J.4
  • 6
    • 3643109367 scopus 로고    scopus 로고
    • Effects of recombinant neutral endopeptidase (EC 3.4.24.11) on the growth of lung cancer cell lines in vitro and in vivo
    • Bunn PA Jr., Helfrich BA, Brenner DG, Chan DC, Dykes DJ, Cohen AJ, Miller YE. Effects of recombinant neutral endopeptidase (EC 3.4.24.11) on the growth of lung cancer cell lines in vitro and in vivo. Clin Cancer Res 1998;4(11):2849-2858.
    • (1998) Clin Cancer Res , vol.4 , Issue.11 , pp. 2849-2858
    • Bunn Jr., P.A.1    Helfrich, B.A.2    Brenner, D.G.3    Chan, D.C.4    Dykes, D.J.5    Cohen, A.J.6    Miller, Y.E.7
  • 7
    • 0021811485 scopus 로고
    • Neutral metalloendopeptidase in human male genital tract. Comparison to angiotensin I-converting enzyme
    • Erdos EG, Schulz WW, Gafford JT, Defendini R. Neutral metalloendopeptidase in human male genital tract. Comparison to angiotensin I-converting enzyme. Lab Invest 1985;52(4): 437-447.
    • (1985) Lab Invest , vol.52 , Issue.4 , pp. 437-447
    • Erdos, E.G.1    Schulz, W.W.2    Gafford, J.T.3    Defendini, R.4
  • 8
    • 0035130537 scopus 로고    scopus 로고
    • Identification and characterization of neutral endopeptidase (EC 3. 4. 24. 11) from human prostasomes-Localization in prostatic tissue and cell lines
    • Renneberg H, Albrecht M, Kurek R, Krause E, Lottspeich F, Aumuller G, Wilhelm B. Identification and characterization of neutral endopeptidase (EC 3. 4. 24. 11) from human prostasomes-Localization in prostatic tissue and cell lines. Prostate 2001;46(3):173-183.
    • (2001) Prostate , vol.46 , Issue.3 , pp. 173-183
    • Renneberg, H.1    Albrecht, M.2    Kurek, R.3    Krause, E.4    Lottspeich, F.5    Aumuller, G.6    Wilhelm, B.7
  • 9
    • 0027102389 scopus 로고
    • CD10/neutral endopeptidase 24.11 in developing human fetal lung. Patterns of expression and modulation of peptide-mediated proliferation
    • Sunday ME, Hua J, Torday JS, Reyes B, Shipp MA. CD10/neutral endopeptidase 24.11 in developing human fetal lung. Patterns of expression and modulation of peptide-mediated proliferation. J Clin Invest 1992; 90(6):2517-2525.
    • (1992) J Clin Invest , vol.90 , Issue.6 , pp. 2517-2525
    • Sunday, M.E.1    Hua, J.2    Torday, J.S.3    Reyes, B.4    Shipp, M.A.5
  • 11
    • 0028276315 scopus 로고
    • Differential expression of mRNAs for endothelin-related proteins in human endometrium, myometrium and leiomyoma
    • Pekonen F, Nyman T, Rutanen EM. Differential expression of mRNAs for endothelin-related proteins in human endometrium, myometrium and leiomyoma. Mol Cell Endocrinol 1994;103(1-2):165-170.
    • (1994) Mol Cell Endocrinol , vol.103 , Issue.1-2 , pp. 165-170
    • Pekonen, F.1    Nyman, T.2    Rutanen, E.M.3
  • 12
    • 0027302155 scopus 로고
    • CD10/neutral endopeptidase 24.11 regulates fetal lung growth and maturation in utero by potentiating endogenous bombesin-like peptides
    • King KA, Hua J, Torday JS, Drazen JM, Graham SA, Shipp MA, Sunday ME. CD10/neutral endopeptidase 24.11 regulates fetal lung growth and maturation in utero by potentiating endogenous bombesin-like peptides. J Clin Invest 1993;91(5):1969-1973.
    • (1993) J Clin Invest , vol.91 , Issue.5 , pp. 1969-1973
    • King, K.A.1    Hua, J.2    Torday, J.S.3    Drazen, J.M.4    Graham, S.A.5    Shipp, M.A.6    Sunday, M.E.7
  • 13
    • 0032006924 scopus 로고    scopus 로고
    • Neurotensin is metabolized by endogenous proteases in prostate cancer cell lines
    • Moody TW, Mayr CA, Gillespie TJ, Davis TP. Neurotensin is metabolized by endogenous proteases in prostate cancer cell lines. Peptides 1998;19(2):253-258.
    • (1998) Peptides , vol.19 , Issue.2 , pp. 253-258
    • Moody, T.W.1    Mayr, C.A.2    Gillespie, T.J.3    Davis, T.P.4
  • 16
    • 0030030782 scopus 로고    scopus 로고
    • Expression of CD10/neutral endopeptidase in normal and malignant tissues of the human stomach and colon
    • Sato Y, Itoh F, Hinoda Y, Ohe Y, Nakagawa N, Ueda R, Yachi A, Imai K. Expression of CD10/neutral endopeptidase in normal and malignant tissues of the human stomach and colon. J Gastroenterol 1996;31(1):12-17.
    • (1996) J Gastroenterol , vol.31 , Issue.1 , pp. 12-17
    • Sato, Y.1    Itoh, F.2    Hinoda, Y.3    Ohe, Y.4    Nakagawa, N.5    Ueda, R.6    Yachi, A.7    Imai, K.8
  • 18
    • 0028830941 scopus 로고
    • Decreased expression of messenger RNAs encoding endothelin receptors and neutral endopeptidase 24.11 in endometrial cancer
    • Pekonen F, Nyman T, Ammala M, Rutanen EM. Decreased expression of messenger RNAs encoding endothelin receptors and neutral endopeptidase 24.11 in endometrial cancer. Br J Cancer 1995;71(1):59-63.
    • (1995) Br J Cancer , vol.71 , Issue.1 , pp. 59-63
    • Pekonen, F.1    Nyman, T.2    Ammala, M.3    Rutanen, E.M.4
  • 20
    • 0027244148 scopus 로고
    • Hematopoietic differentiation antigens that are membrane-associated enzymes: Cutting is the key!
    • Shipp MA, Look AT. Hematopoietic differentiation antigens that are membrane-associated enzymes: Cutting is the key! Blood 1993;82(4):1052-1070.
    • (1993) Blood , vol.82 , Issue.4 , pp. 1052-1070
    • Shipp, M.A.1    Look, A.T.2
  • 22
    • 0032861293 scopus 로고    scopus 로고
    • Apocrine secretion - Fact or artifact?
    • Aumuller G, Wilhelm B, Seitz J. Apocrine secretion - Fact or artifact? Anat Anz 1999;181(5):437-446.
    • (1999) Anat Anz , vol.181 , Issue.5 , pp. 437-446
    • Aumuller, G.1    Wilhelm, B.2    Seitz, J.3
  • 24
    • 0030894083 scopus 로고    scopus 로고
    • Immunohistochemistry of a prostate membrane specific protein during development and maturation of the human prostate
    • Renneberg H, Wennemuth G, Konrad L, Aumuller G. Immunohistochemistry of a prostate membrane specific protein during development and maturation of the human prostate. J Anat 1997;190(Pt 3):343-349.
    • (1997) J Anat , vol.190 , Issue.PART 3 , pp. 343-349
    • Renneberg, H.1    Wennemuth, G.2    Konrad, L.3    Aumuller, G.4
  • 25
    • 0023868637 scopus 로고
    • Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase)
    • Malfroy B, Kuang WJ, Seeburg PH, Mason AJ, Schofield PR. Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase). FEBS Lett 1988;229(1): 206-210.
    • (1988) FEBS Lett , vol.229 , Issue.1 , pp. 206-210
    • Malfroy, B.1    Kuang, W.J.2    Seeburg, P.H.3    Mason, A.J.4    Schofield, P.R.5
  • 27
    • 0032447132 scopus 로고    scopus 로고
    • Effect of prostatic neuropeptides on invasion and migration of PC-3 prostate cancer cells
    • Nagakawa O, Ogasawara M, Fujii H, Murakami K, Murata J, Fuse H, Saiki I. Effect of prostatic neuropeptides on invasion and migration of PC-3 prostate cancer cells. Cancer Lett 1998;133(1): 27-33.
    • (1998) Cancer Lett , vol.133 , Issue.1 , pp. 27-33
    • Nagakawa, O.1    Ogasawara, M.2    Fujii, H.3    Murakami, K.4    Murata, J.5    Fuse, H.6    Saiki, I.7
  • 28
    • 0028020030 scopus 로고
    • Grading prostate cancer
    • Bostwick DG. Grading prostate cancer. Am J Clin Pathol 1994;102(4 Suppl 1):S38-S56.
    • (1994) Am J Clin Pathol , vol.102 , Issue.4 SUPPL. 1
    • Bostwick, D.G.1
  • 31
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory. 726 p
    • Harlow E, Lane D. Cold Spring Harbor Laboratory. Antibodies: A laboratory manual, Vol. xiii. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory; 1988. 726 p.
    • (1988) Antibodies: A Laboratory Manual , vol.13
    • Harlow, E.1    Lane, D.2
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227(259): 680-685.
    • (1970) Nature , vol.227 , Issue.259 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Kyhse-Andersen J. Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J Biochem Biophys Methods 1984;10(3-4):203-209.
    • (1984) J Biochem Biophys Methods , vol.10 , Issue.3-4 , pp. 203-209
    • Kyhse-Andersen, J.1
  • 34
    • 0031019680 scopus 로고    scopus 로고
    • Detection of rare RNA sequences by single-enzyme in situ reverse transcription-polymerase chain reaction. High-resolution analyses of interleukin-6 mRNA in paraffin sections of lymph nodes
    • Peters J, Krams M, Wacker HH, Carstens A, Weisner D, Hamann K, Menke M, Harms D, Parwaresch R. Detection of rare RNA sequences by single-enzyme in situ reverse transcription-polymerase chain reaction. High-resolution analyses of interleukin-6 mRNA in paraffin sections of lymph nodes. Am J Pathol 1997;150(2):469-476.
    • (1997) Am J Pathol , vol.150 , Issue.2 , pp. 469-476
    • Peters, J.1    Krams, M.2    Wacker, H.H.3    Carstens, A.4    Weisner, D.5    Hamann, K.6    Menke, M.7    Harms, D.8    Parwaresch, R.9
  • 35
    • 0002984733 scopus 로고    scopus 로고
    • The foundations of successful RT in situ PCR
    • Nuovo GJ. The foundations of successful RT in situ PCR. Front Biosci 1996;1:c4-c15.
    • (1996) Front Biosci , vol.1
    • Nuovo, G.J.1
  • 36
    • 0036279668 scopus 로고    scopus 로고
    • Expression, localization and activity of neutral endopeptidase in cultured cells of benign prostatic hyperplasia and prostate cancer
    • Albrecht M, Gillen S, Wilhelm B, Doroszewicz J, Aumuller G. Expression, localization and activity of neutral endopeptidase in cultured cells of benign prostatic hyperplasia and prostate cancer. J Urol 2002;168(1):336-342.
    • (2002) J Urol , vol.168 , Issue.1 , pp. 336-342
    • Albrecht, M.1    Gillen, S.2    Wilhelm, B.3    Doroszewicz, J.4    Aumuller, G.5
  • 37
    • 0031604692 scopus 로고    scopus 로고
    • Neuroendocrine differentiation in prostatic carcinoma: An update
    • di Sant'Agnese PA. Neuroendocrine differentiation in prostatic carcinoma: An update. Prostate Suppl 1998;8:74-79.
    • (1998) Prostate Suppl , vol.8 , pp. 74-79
    • Di Sant'Agnese, P.A.1
  • 38
    • 0029684748 scopus 로고    scopus 로고
    • Neuroendocrine differentiation and hormone-refractory prostate cancer
    • Abrahamsson PA. Neuroendocrine differentiation and hormone-refractory prostate cancer. Prostate Suppl 1996;6:3-8.
    • (1996) Prostate Suppl , vol.6 , pp. 3-8
    • Abrahamsson, P.A.1
  • 40
    • 0029821174 scopus 로고    scopus 로고
    • Enzymatic digestion of bradykinin by rat Sertoli cell cultures
    • Monsees TK, Miska W, Schill WB. Enzymatic digestion of bradykinin by rat Sertoli cell cultures. J Androl 1996;17(4):375-381.
    • (1996) J Androl , vol.17 , Issue.4 , pp. 375-381
    • Monsees, T.K.1    Miska, W.2    Schill, W.B.3
  • 43
    • 0031741792 scopus 로고    scopus 로고
    • Identification of genes associated with stromal hyperplasia and glandular atrophy of the prostate by mRNA differential display
    • Walden PD, Lefkowitz GK, Ficazzola M, Gitlin J, Lepor H. Identification of genes associated with stromal hyperplasia and glandular atrophy of the prostate by mRNA differential display. Exp Cell Res 1998;245(1):19-26.
    • (1998) Exp Cell Res , vol.245 , Issue.1 , pp. 19-26
    • Walden, P.D.1    Lefkowitz, G.K.2    Ficazzola, M.3    Gitlin, J.4    Lepor, H.5
  • 44
    • 0030900414 scopus 로고    scopus 로고
    • Gene expression and autoradiographic localization of endothelin-1 and its receptors A and B in the different zones of the normal human prostate
    • Prayer-Galetti T, Rossi GP, Belloni AS, Albertin G, Battanello W, Piovan V, Gardiman M, Pagano F. Gene expression and autoradiographic localization of endothelin-1 and its receptors A and B in the different zones of the normal human prostate. J Urol 1997;157(6):2334-2339.
    • (1997) J Urol , vol.157 , Issue.6 , pp. 2334-2339
    • Prayer-Galetti, T.1    Rossi, G.P.2    Belloni, A.S.3    Albertin, G.4    Battanello, W.5    Piovan, V.6    Gardiman, M.7    Pagano, F.8
  • 45
    • 0034541255 scopus 로고    scopus 로고
    • Neutral endopeptidase promotes phorbol ester-induced apoptosis in prostate cancer cells by inhibiting neuropeptide-induced protein kinase C delta degradation
    • Sumitomo M, Shen R, Goldberg JS, Dai J, Navarro D, Nanus DM. Neutral endopeptidase promotes phorbol ester-induced apoptosis in prostate cancer cells by inhibiting neuropeptide-induced protein kinase C delta degradation. Cancer Res 2000;60(23): 6590-6596.
    • (2000) Cancer Res , vol.60 , Issue.23 , pp. 6590-6596
    • Sumitomo, M.1    Shen, R.2    Goldberg, J.S.3    Dai, J.4    Navarro, D.5    Nanus, D.M.6
  • 47
    • 0027227317 scopus 로고
    • Transforming growth factor-beta 1 inhibits enkephalinase (EC 3.4.24.11) gene expression in human endometrial stromal cells and sex skin fibroblasts in culture
    • Casey ML, Smith JW, Nagai K, MacDonald PC. Transforming growth factor-beta 1 inhibits enkephalinase (EC 3.4.24.11) gene expression in human endometrial stromal cells and sex skin fibroblasts in culture. J Clin Endocrinol Metab 1993;77(1): 144-150.
    • (1993) J Clin Endocrinol Metab , vol.77 , Issue.1 , pp. 144-150
    • Casey, M.L.1    Smith, J.W.2    Nagai, K.3    MacDonald, P.C.4
  • 48
    • 0032893856 scopus 로고    scopus 로고
    • Membrane-bound cell surface peptidases in reproductive organs
    • Fujiwara H, Imai K, Inoue T, Maeda M, Fujii S. Membrane-bound cell surface peptidases in reproductive organs. Endocr J 1999;46(1):11-25.
    • (1999) Endocr J , vol.46 , Issue.1 , pp. 11-25
    • Fujiwara, H.1    Imai, K.2    Inoue, T.3    Maeda, M.4    Fujii, S.5
  • 49
    • 0034962346 scopus 로고    scopus 로고
    • Neutral endopeptidase is expressed on the follicular granulosa cells of rabbit ovaries
    • Zappulla JP, DesGroseillers L. Neutral endopeptidase is expressed on the follicular granulosa cells of rabbit ovaries. Comp Biochem Physiol B Biochem Mol Biol 2001;129(4): 863-870.
    • (2001) Comp Biochem Physiol B Biochem Mol Biol , vol.129 , Issue.4 , pp. 863-870
    • Zappulla, J.P.1    DesGroseillers, L.2
  • 50
    • 0034743144 scopus 로고    scopus 로고
    • Upregulation of neutral endopeptidase expression and enzymatic activity during the differentiation of human choriocarcinoma cells
    • Uehara C, Ino K, Suzuki T, Kajiyama H, Kikkawa F, Nagasaka T, Mizutani S. Upregulation of neutral endopeptidase expression and enzymatic activity during the differentiation of human choriocarcinoma cells. Placenta 2001;22(6):540-549.
    • (2001) Placenta , vol.22 , Issue.6 , pp. 540-549
    • Uehara, C.1    Ino, K.2    Suzuki, T.3    Kajiyama, H.4    Kikkawa, F.5    Nagasaka, T.6    Mizutani, S.7
  • 51
    • 0029997485 scopus 로고    scopus 로고
    • Phenotypic expression of marrow cells when grown on various substrata
    • Fried A, Shamay A, Wientroub S, Benayahu D. Phenotypic expression of marrow cells when grown on various substrata. J Cell Biochem 1996;61(2):246-254.
    • (1996) J Cell Biochem , vol.61 , Issue.2 , pp. 246-254
    • Fried, A.1    Shamay, A.2    Wientroub, S.3    Benayahu, D.4
  • 53
    • 0035253674 scopus 로고    scopus 로고
    • Semiquantitative morphology of human prostatic development and regional distribution of prostatic neuroendocrine cells
    • Aumuller G, Leonhardt M, Renneberg H, von Rahden B, Bjartell A, Abrahamsson PA. Semiquantitative morphology of human prostatic development and regional distribution of prostatic neuroendocrine cells. Prostate 2001;46(2):108-115.
    • (2001) Prostate , vol.46 , Issue.2 , pp. 108-115
    • Aumuller, G.1    Leonhardt, M.2    Renneberg, H.3    Von Rahden, B.4    Bjartell, A.5    Abrahamsson, P.A.6
  • 55
    • 0029039010 scopus 로고
    • Neuroendocrine peptides in the prostate
    • Gkonos PJ, Krongrad A, Roos BA. Neuroendocrine peptides in the prostate. Urol Res 1995;23(2):81-87.
    • (1995) Urol Res , vol.23 , Issue.2 , pp. 81-87
    • Gkonos, P.J.1    Krongrad, A.2    Roos, B.A.3
  • 56
    • 0027491367 scopus 로고
    • Relationship of neuroendocrine cells of prostate and serotonin to benign prostatic hyperplasia
    • Cockett AT, di Sant'Agnese PA, Gopinath P, Schoen SR, Abrahamsson PA. Relationship of neuroendocrine cells of prostate and serotonin to benign prostatic hyperplasia. Urology 1993;42(5):512-519.
    • (1993) Urology , vol.42 , Issue.5 , pp. 512-519
    • Cockett, A.T.1    Di Sant'Agnese, P.A.2    Gopinath, P.3    Schoen, S.R.4    Abrahamsson, P.A.5
  • 57
    • 0034891773 scopus 로고    scopus 로고
    • The expression of neuropeptides in hyperplastic and malignant prostate tissue and its possible clinical implications
    • Yu DS, Hsieh DS, Chen HI, Chang SY. The expression of neuropeptides in hyperplastic and malignant prostate tissue and its possible clinical implications. J Urol 2001;166(3): 871-875.
    • (2001) J Urol , vol.166 , Issue.3 , pp. 871-875
    • Yu, D.S.1    Hsieh, D.S.2    Chen, H.I.3    Chang, S.Y.4
  • 58
    • 0026668312 scopus 로고
    • Neutral endopeptidase modulates endothelin-l-induced airway smooth muscle contraction in guinea-pig trachea
    • Di Maria GU, Katayama M, Borson DB, Nadel JA. Neutral endopeptidase modulates endothelin-l-induced airway smooth muscle contraction in guinea-pig trachea. Regul Pept 1992;39(2-3):137-145.
    • (1992) Regul Pept , vol.39 , Issue.2-3 , pp. 137-145
    • Di Maria, G.U.1    Katayama, M.2    Borson, D.B.3    Nadel, J.A.4
  • 59
    • 0027360943 scopus 로고
    • Stimulation of the chemotactic migration of human fibroblasts by substance P
    • Kahler CM, Sitte BA, Reinisch N, Wiedermann CJ. Stimulation of the chemotactic migration of human fibroblasts by substance P. Eur J Pharmacol 1993;249(3):281-286.
    • (1993) Eur J Pharmacol , vol.249 , Issue.3 , pp. 281-286
    • Kahler, C.M.1    Sitte, B.A.2    Reinisch, N.3    Wiedermann, C.J.4
  • 60
    • 0030822201 scopus 로고    scopus 로고
    • Substance P augments fibrogenic cytokine-induced fibroblast proliferation: Possible involvement of neuropeptide in tissue fibrosis
    • Katayama I, Nishioka K. Substance P augments fibrogenic cytokine-induced fibroblast proliferation: Possible involvement of neuropeptide in tissue fibrosis. J Dermatol Sci 1997;15(3): 201-206.
    • (1997) J Dermatol Sci , vol.15 , Issue.3 , pp. 201-206
    • Katayama, I.1    Nishioka, K.2
  • 61
    • 0022252979 scopus 로고
    • Receptor-mediated mitogenic effects of substance P on cultured smooth muscle cells
    • Payan DG. Receptor-mediated mitogenic effects of substance P on cultured smooth muscle cells. Biochem Biophys Res Commun 1985;130(1):104-109.
    • (1985) Biochem Biophys Res Commun , vol.130 , Issue.1 , pp. 104-109
    • Payan, D.G.1
  • 62
    • 0027301880 scopus 로고
    • In-situ polymerase chain reaction. An overview of methods, applications and limitations of a new molecular technique
    • Komminoth P, Long AA. In-situ polymerase chain reaction. An overview of methods, applications and limitations of a new molecular technique. Virchows Arch B Cell Pathol Incl Mol Pathol 1993;64(2):67-73.
    • (1993) Virchows Arch B Cell Pathol Incl Mol Pathol , vol.64 , Issue.2 , pp. 67-73
    • Komminoth, P.1    Long, A.A.2
  • 63
    • 0026579363 scopus 로고
    • Intracellular amplification of proviral DNA in tissue sections using the polymerase chain reaction
    • Chiu KP, Cohen SH, Morris DW, Jordan GW. Intracellular amplification of proviral DNA in tissue sections using the polymerase chain reaction. J Histochem Cytochem 1992;40(3): 333-341.
    • (1992) J Histochem Cytochem , vol.40 , Issue.3 , pp. 333-341
    • Chiu, K.P.1    Cohen, S.H.2    Morris, D.W.3    Jordan, G.W.4
  • 65
    • 0030707803 scopus 로고    scopus 로고
    • Multiple sorting signals determine apical localization of a nonglycosylated integral membrane protein
    • Alonso MA, Fan L, Alarcon B. Multiple sorting signals determine apical localization of a nonglycosylated integral membrane protein. J Biol Chem 1997;272(49):30748-30752.
    • (1997) J Biol Chem , vol.272 , Issue.49 , pp. 30748-30752
    • Alonso, M.A.1    Fan, L.2    Alarcon, B.3
  • 66
    • 0028810337 scopus 로고
    • N-glycans as apical sorting signals in epithelial cells
    • Scheiffele P, Peranen J, Simons K. N-glycans as apical sorting signals in epithelial cells. Nature 1995;378(6552):96-98.
    • (1995) Nature , vol.378 , Issue.6552 , pp. 96-98
    • Scheiffele, P.1    Peranen, J.2    Simons, K.3
  • 67
    • 0028147134 scopus 로고
    • Role of glycosylation in transport and enzymic activity of neutral endopeptidase-24.11
    • Lafrance MH, Vezina C, Wang Q, Boileau G, Crine P, Lemay G. Role of glycosylation in transport and enzymic activity of neutral endopeptidase-24.11. Biochem J 1994;302(Pt 2): 451-454.
    • (1994) Biochem J , vol.302 , Issue.PART 2 , pp. 451-454
    • Lafrance, M.H.1    Vezina, C.2    Wang, Q.3    Boileau, G.4    Crine, P.5    Lemay, G.6
  • 68
    • 0026795062 scopus 로고
    • Expression and polarized apical secretion in Madin-Darby canine kidney cells of a recombinant soluble form of neutral endopeptidase lacking the cytosolic and transmembrane domains
    • Corbeil D, Boileau G, Lemay G, Crine P. Expression and polarized apical secretion in Madin-Darby canine kidney cells of a recombinant soluble form of neutral endopeptidase lacking the cytosolic and transmembrane domains. J Biol Chem 1992;267(4):2798-2801.
    • (1992) J Biol Chem , vol.267 , Issue.4 , pp. 2798-2801
    • Corbeil, D.1    Boileau, G.2    Lemay, G.3    Crine, P.4


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