메뉴 건너뛰기




Volumn 292, Issue 2, 2007, Pages

Altered levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma

Author keywords

Angiotensin II; Intracrine peptide signaling; Peptide hormones; Peptide metabolism; Renal tumor cell biology

Indexed keywords

5 OXOPROLYL PEPTIDASE; AMINOPEPTIDASE; AMINOPEPTIDASE B; ASPARTYL AMINOPEPTIDASE; GLUTAMYL AMINOPEPTIDASE; MICROSOMAL AMINOPEPTIDASE; PEPTIDASE; PUROMYCIN;

EID: 33846864246     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.00148.2006     Document Type: Article
Times cited : (47)

References (45)
  • 1
    • 0025321792 scopus 로고
    • Role of aminopeptidase activity in the regulation of the pressor activity of circulating angiotensins
    • Ahmad S, Ward PE. Role of aminopeptidase activity in the regulation of the pressor activity of circulating angiotensins. J Pharmacol Exp Ther 252: 643-650, 1990.
    • (1990) J Pharmacol Exp Ther , vol.252 , pp. 643-650
    • Ahmad, S.1    Ward, P.E.2
  • 4
    • 0037372507 scopus 로고    scopus 로고
    • The angiogenic regulator CD13/APN is a transcriptional target of Ras signalling pathways in endothelial morphogenesis
    • Bhagwat SV, Petrovic N, Okamoto Y, Shapiro LH. The angiogenic regulator CD13/APN is a transcriptional target of Ras signalling pathways in endothelial morphogenesis. Blood 101: 1818-1826, 2003.
    • (2003) Blood , vol.101 , pp. 1818-1826
    • Bhagwat, S.V.1    Petrovic, N.2    Okamoto, Y.3    Shapiro, L.H.4
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254, 1976.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0036563250 scopus 로고    scopus 로고
    • Biological properties of the angiotensin peptides other than angiotensin II: Implications for hypertension and cardiovascular diseases
    • Cesari M, Rossi GP, Pessina AC. Biological properties of the angiotensin peptides other than angiotensin II: implications for hypertension and cardiovascular diseases. J Hypertens 20: 793-799, 2002.
    • (2002) J Hypertens , vol.20 , pp. 793-799
    • Cesari, M.1    Rossi, G.P.2    Pessina, A.C.3
  • 8
    • 0028843821 scopus 로고
    • Puromycin-sensitive aminopeptidase: Sequence analysis, expression and functional characterization
    • Constam DB, Tobler AR, Rensing-Ehl A, Kemler I, Hersh LB, Fontana A. Puromycin-sensitive aminopeptidase: sequence analysis, expression and functional characterization. J Biol Chem 270: 26931-26939, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 26931-26939
    • Constam, D.B.1    Tobler, A.R.2    Rensing-Ehl, A.3    Kemler, I.4    Hersh, L.B.5    Fontana, A.6
  • 9
    • 0002565473 scopus 로고
    • Characteristics of angiotensin II receptors and their role in cell and organ physiology
    • edited by Laragh JH and BM Brenner. New York: Raven
    • De Gasparo M, Bottari S, Levens NR. Characteristics of angiotensin II receptors and their role in cell and organ physiology. In: Hypertension; Pathophysiology, Diagnosis and Management, edited by Laragh JH and BM Brenner. New York: Raven, 1995, p. 1695-1710.
    • (1995) Hypertension; Pathophysiology, Diagnosis and Management , pp. 1695-1710
    • De Gasparo, M.1    Bottari, S.2    Levens, N.R.3
  • 10
    • 0020376310 scopus 로고
    • Prognostic significance of morphologic parameters in renal cell carcinoma
    • Furhman SA, Lasky LC, Limas C. Prognostic significance of morphologic parameters in renal cell carcinoma. Am J Surg Pathol 6: 655-663, 1982.
    • (1982) Am J Surg Pathol , vol.6 , pp. 655-663
    • Furhman, S.A.1    Lasky, L.C.2    Limas, C.3
  • 12
    • 0037190118 scopus 로고    scopus 로고
    • Aminopeptidase inhibitors bestatin and actinonin inhibit cell proliferation of myeloma cells predominantly by intracellular interactions
    • Grujic M, Renko M. Aminopeptidase inhibitors bestatin and actinonin inhibit cell proliferation of myeloma cells predominantly by intracellular interactions. Cancer Lett 182: 113-119, 2002.
    • (2002) Cancer Lett , vol.182 , pp. 113-119
    • Grujic, M.1    Renko, M.2
  • 13
    • 33750698034 scopus 로고    scopus 로고
    • Neuropeptide processing
    • edited by Lendeckel U and Hooper NM. New York: Springer Science Business Media
    • Hallberg M, Le Grevès P, Nyberg F. Neuropeptide processing. In: Proteases in the Brain, edited by Lendeckel U and Hooper NM. New York: Springer Science Business Media, 2005, p. 203-234.
    • (2005) Proteases in the Brain , pp. 203-234
    • Hallberg, M.1    Le Grevès, P.2    Nyberg, F.3
  • 15
    • 0027160183 scopus 로고
    • Multiple autocrine growth factors modulate vascular smooth muscle cell growth response to angiotensin II
    • Itoh H, Mukoyama M, Pratt RE, Gibbons GH, Dzau VJ. Multiple autocrine growth factors modulate vascular smooth muscle cell growth response to angiotensin II. J Clin Invest 91: 2268-2274, 1993.
    • (1993) J Clin Invest , vol.91 , pp. 2268-2274
    • Itoh, H.1    Mukoyama, M.2    Pratt, R.E.3    Gibbons, G.H.4    Dzau, V.J.5
  • 17
    • 0030845329 scopus 로고    scopus 로고
    • Antiapoptotic action of angiotensin fragments to neuronal cells from angiotensinogen knockout mice
    • Kakinuma Y, Hama H, Sugiyama F, Goto K, Murakami K, Fukamizu A. Antiapoptotic action of angiotensin fragments to neuronal cells from angiotensinogen knockout mice. Neurosci Lett 232: 167-170, 1997.
    • (1997) Neurosci Lett , vol.232 , pp. 167-170
    • Kakinuma, Y.1    Hama, H.2    Sugiyama, F.3    Goto, K.4    Murakami, K.5    Fukamizu, A.6
  • 18
    • 0031885821 scopus 로고    scopus 로고
    • Regulation of the expression of aminopeptidase A, aminopeptidase N/CD13 and dipeptidylpeptidase IV/CD26 in renal carcinoma cells and renal tubular epithelial cells by cytokines and cAMP-increasing mediators
    • Kehlen A, Göhring B, Langner J, Riemann D. Regulation of the expression of aminopeptidase A, aminopeptidase N/CD13 and dipeptidylpeptidase IV/CD26 in renal carcinoma cells and renal tubular epithelial cells by cytokines and cAMP-increasing mediators. Clin Exp Immunol 111: 435-441, 1998.
    • (1998) Clin Exp Immunol , vol.111 , pp. 435-441
    • Kehlen, A.1    Göhring, B.2    Langner, J.3    Riemann, D.4
  • 19
    • 20344389482 scopus 로고    scopus 로고
    • Subcellular distribution of membrane-bound aminopeptidases in the human and rat brain
    • Larrinaga G, Callado LF, Agirregoitia N, Varona A, Gil J. Subcellular distribution of membrane-bound aminopeptidases in the human and rat brain. Neurosci Lett 383: 136-140, 2005.
    • (2005) Neurosci Lett , vol.383 , pp. 136-140
    • Larrinaga, G.1    Callado, L.F.2    Agirregoitia, N.3    Varona, A.4    Gil, J.5
  • 20
    • 0025008623 scopus 로고
    • Characterization of aminopeptidases in human kidney soluble fraction
    • Mantle D, Lauffart B, McDermott J, Gibson A. Characterization of aminopeptidases in human kidney soluble fraction. Clin Chim Acta 187: 105-113, 1990.
    • (1990) Clin Chim Acta , vol.187 , pp. 105-113
    • Mantle, D.1    Lauffart, B.2    McDermott, J.3    Gibson, A.4
  • 21
    • 0026504969 scopus 로고
    • Comparison of soluble aminopeptidases in human cerebral cortex, skeletal muscle and kidney tissues
    • Mantle D. Comparison of soluble aminopeptidases in human cerebral cortex, skeletal muscle and kidney tissues. Clin Chim Acta 207: 107-118, 1992.
    • (1992) Clin Chim Acta , vol.207 , pp. 107-118
    • Mantle, D.1
  • 24
    • 0029948534 scopus 로고    scopus 로고
    • Proteases involved in the metabolism of angiotensin II, bradykinin, calcitonin gene-related peptide (CGRP), and neuropeptide Y by vascular smooth muscle cells
    • Mentlein R, Roos T. Proteases involved in the metabolism of angiotensin II, bradykinin, calcitonin gene-related peptide (CGRP), and neuropeptide Y by vascular smooth muscle cells. Peptides 17: 709-720, 1996.
    • (1996) Peptides , vol.17 , pp. 709-720
    • Mentlein, R.1    Roos, T.2
  • 25
    • 33750344202 scopus 로고    scopus 로고
    • Tumors of the kidney, bladder, and related urinary structures
    • Washington, DC: American Registry of Pathology
    • Murphy WM, Grignon DJ, Perlman EJ. Tumors of the kidney, bladder, and related urinary structures. In: AFIP Atlas of Tumor Pathology 4th Series, Fascicle 1. Washington, DC: American Registry of Pathology, 2004, p. 101-240.
    • (2004) AFIP Atlas of Tumor Pathology 4th Series, Fascicle , vol.1 , pp. 101-240
    • Murphy, W.M.1    Grignon, D.J.2    Perlman, E.J.3
  • 28
    • 18044393842 scopus 로고    scopus 로고
    • Olivo R do A, Teixeira C de F, Silveira PF. Representative aminopeptidases and prolyl endopeptidase from murine macrophages: comparative activity levels in resident and elicited cells. Biochem Pharmacol 69: 1441-1450, 2005.
    • Olivo R do A, Teixeira C de F, Silveira PF. Representative aminopeptidases and prolyl endopeptidase from murine macrophages: comparative activity levels in resident and elicited cells. Biochem Pharmacol 69: 1441-1450, 2005.
  • 30
    • 1342324063 scopus 로고    scopus 로고
    • Arginine-aminopeptidase in rat cardiac fibroblastic cells participates in angiotensin peptide turnover
    • Petrov VV, Fagard RH, Lijnen PJ. Arginine-aminopeptidase in rat cardiac fibroblastic cells participates in angiotensin peptide turnover. Cardiovasc Res 61: 724-735, 2004.
    • (2004) Cardiovasc Res , vol.61 , pp. 724-735
    • Petrov, V.V.1    Fagard, R.H.2    Lijnen, P.J.3
  • 31
    • 33846878195 scopus 로고    scopus 로고
    • CD13/aminopeptidase N in tumor growth and angiogenesis
    • edited by Hooper NM and Lendeckel U. New York: Kluwer Academic/Plenum
    • Petrovic N, Schacke W, Shapiro LH. CD13/aminopeptidase N in tumor growth and angiogenesis. In: Aminopeptidases in Biology and Disease, edited by Hooper NM and Lendeckel U. New York: Kluwer Academic/Plenum, 2004, p. 179-200.
    • (2004) Aminopeptidases in Biology and Disease , pp. 179-200
    • Petrovic, N.1    Schacke, W.2    Shapiro, L.H.3
  • 32
    • 0037370644 scopus 로고    scopus 로고
    • Implications of intracrine hormone action for physiology and medicine
    • Re RN. Implications of intracrine hormone action for physiology and medicine. Am J Physiol Heart Circ Physiol 284: H751-H757, 2003.
    • (2003) Am J Physiol Heart Circ Physiol , vol.284
    • Re, R.N.1
  • 33
    • 0034650948 scopus 로고    scopus 로고
    • CD13/N-aminopeptidase is involved in the development of dendritic cells and macrophages from cord blood CD34(+) cells
    • Rosenzwajg M, Tailleux L, Gluckman JC. CD13/N-aminopeptidase is involved in the development of dendritic cells and macrophages from cord blood CD34(+) cells. Blood 95: 453-460, 2000.
    • (2000) Blood , vol.95 , pp. 453-460
    • Rosenzwajg, M.1    Tailleux, L.2    Gluckman, J.C.3
  • 34
    • 0027195127 scopus 로고    scopus 로고
    • Saiki I, Fujii H, Yoneda J, Abe F, Nakajima M, Tsuruo T, Azuma I. Role of aminopeptidase N (CD13) in tumor-cell invasion and extracellular matrix degradation. Int J Cancer 54: 137-143, 1993.
    • Saiki I, Fujii H, Yoneda J, Abe F, Nakajima M, Tsuruo T, Azuma I. Role of aminopeptidase N (CD13) in tumor-cell invasion and extracellular matrix degradation. Int J Cancer 54: 137-143, 1993.
  • 36
    • 33846886027 scopus 로고    scopus 로고
    • Effects on mammals of the aminopeptidase inhibitor bestatine
    • edited by Hooper NM and Lendeckel U. New York: Kluwer Academic/Plenum
    • Scornik OA, Botbol V. Effects on mammals of the aminopeptidase inhibitor bestatine. In: Aminopeptidases in Biology and Disease, edited by Hooper NM and Lendeckel U. New York: Kluwer Academic/Plenum, 2004, p. 127-143.
    • (2004) Aminopeptidases in Biology and Disease , pp. 127-143
    • Scornik, O.A.1    Botbol, V.2
  • 37
    • 0035889652 scopus 로고    scopus 로고
    • Augmentation of dead ligandinduced apoptosis by aminopeptidase inhibitors in human solid tumor cell lines
    • Sekine K, Fujii H, Abe F, Nishikawa K. Augmentation of dead ligandinduced apoptosis by aminopeptidase inhibitors in human solid tumor cell lines. Int J Cancer 94: 485-491, 2001.
    • (2001) Int J Cancer , vol.94 , pp. 485-491
    • Sekine, K.1    Fujii, H.2    Abe, F.3    Nishikawa, K.4
  • 38
    • 0033046028 scopus 로고    scopus 로고
    • Induction of apoptosis by bestatin (ubenimex) in human leukemic cell lines
    • Sekine K, Fujii H, Abe F. Induction of apoptosis by bestatin (ubenimex) in human leukemic cell lines. Leukemia 13: 729-734, 1999.
    • (1999) Leukemia , vol.13 , pp. 729-734
    • Sekine, K.1    Fujii, H.2    Abe, F.3
  • 39
    • 0027935132 scopus 로고
    • 1] angiotensin I by a novel aminopeptidase in the rat hypothalamus
    • 1] angiotensin I by a novel aminopeptidase in the rat hypothalamus. Biochem Pharmacol 48: 1043-1046, 1994.
    • (1994) Biochem Pharmacol , vol.48 , pp. 1043-1046
    • Sim, M.K.1    Choo, M.H.2    Qiu, X.S.3
  • 41
    • 13944269123 scopus 로고    scopus 로고
    • Mitotic infidelity and centrosome duplication errors in cells overexpressing tripeptidyl-peptidase II
    • Stavropoulou V, Xie J, Henriksson M, Tomkinson B, Imreh S, Masucci MG. Mitotic infidelity and centrosome duplication errors in cells overexpressing tripeptidyl-peptidase II. Cancer Res 65: 1361-1368, 2005.
    • (2005) Cancer Res , vol.65 , pp. 1361-1368
    • Stavropoulou, V.1    Xie, J.2    Henriksson, M.3    Tomkinson, B.4    Imreh, S.5    Masucci, M.G.6
  • 42
    • 0042357061 scopus 로고    scopus 로고
    • Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases
    • Tanioka T, Hattori A, Masuda S, Nomura Y, Nakayama H, Mizutani S, Tsujimoto M. Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases. J Biol Chem 278: 32275-32283, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 32275-32283
    • Tanioka, T.1    Hattori, A.2    Masuda, S.3    Nomura, Y.4    Nakayama, H.5    Mizutani, S.6    Tsujimoto, M.7
  • 43
    • 33846887537 scopus 로고    scopus 로고
    • The puromycin-sensitive aminopeptidase. Role in neurological, reproductive, inmunological and proliferative disorders
    • edited by Hooper NM and Lendeckel U. New York: Kluwer Academic/Plenum
    • Thompson MW, Hersh LB. The puromycin-sensitive aminopeptidase. Role in neurological, reproductive, inmunological and proliferative disorders. In: Aminopeptidases in Biology and Disease, edited by Hooper NM and Lendeckel U. New York: Kluwer Academic/Plenum 2004, p. 1-15.
    • (2004) Aminopeptidases in Biology and Disease , pp. 1-15
    • Thompson, M.W.1    Hersh, L.B.2
  • 44
    • 33846868984 scopus 로고    scopus 로고
    • Methionine-aminopeptidase: Emerging role in angiogenesis
    • edited by Hooper NM and Lendeckel U. New York: Kluwer Academic/Plenum
    • Vetro JA, Dummitt B, Chang YH. Methionine-aminopeptidase: emerging role in angiogenesis. In: Aminopeptidases in Biology and Disease, edited by Hooper NM and Lendeckel U. New York: Kluwer Academic/Plenum, 2004, p. 17-44.
    • (2004) Aminopeptidases in Biology and Disease , pp. 17-44
    • Vetro, J.A.1    Dummitt, B.2    Chang, Y.H.3
  • 45
    • 0032569016 scopus 로고    scopus 로고
    • Purification, characterization and cloning of a cytosolic aspartyl aminopeptidase
    • Wilk S, Wilk E, Magnusson RP. Purification, characterization and cloning of a cytosolic aspartyl aminopeptidase. J Biol Chem 273: 15961-15970, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 15961-15970
    • Wilk, S.1    Wilk, E.2    Magnusson, R.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.