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Volumn 10, Issue 5, 2010, Pages 467-470

Cathepsin D: Regulation in mammary gland remodeling, misregulation in breast cancer

Author keywords

Aspartic cathepsins; Breast cancer; Postlactational involution; Proteases; Protein trafficking; Secretion

Indexed keywords

CATHEPSIN D;

EID: 77957146781     PISSN: 15384047     EISSN: 15558576     Source Type: Journal    
DOI: 10.4161/cbt.10.5.12855     Document Type: Note
Times cited : (8)

References (29)
  • 1
    • 57649155302 scopus 로고    scopus 로고
    • Proteases: Multifunctional enzymes in life and disease
    • Lopez-Otin C, Bond JS. Proteases: multifunctional enzymes in life and disease. J BiolChem 2008; 283:30433-7.
    • (2008) J BiolChem , vol.283 , pp. 30433-30437
    • Lopez-Otin, C.1    Bond, J.S.2
  • 2
    • 34948884579 scopus 로고    scopus 로고
    • Stromal induction of breast cancer: Inflammation and invasion
    • Radisky ES, Radisky DC. Stromal induction of breast cancer: inflammation and invasion. Rev Endocr Metab Disord 2007; 8:279-87.
    • (2007) Rev Endocr Metab Disord , vol.8 , pp. 279-287
    • Radisky, E.S.1    Radisky, D.C.2
  • 3
    • 0037052448 scopus 로고    scopus 로고
    • Stromal effects on mammary gland development and breast cancer
    • Wiseman BS, Werb Z. Stromal effects on mammary gland development and breast cancer. Science 2002; 296:1046-9.
    • (2002) Science , vol.296 , pp. 1046-1049
    • Wiseman, B.S.1    Werb, Z.2
  • 7
    • 50649106648 scopus 로고    scopus 로고
    • Cathepsin D - Many functions of one aspartic protease
    • Benes P, Vetvicka V, Fusek M. Cathepsin D - many functions of one aspartic protease. Crit Rev Oncol Hematol 2008; 68:12-28.
    • (2008) Crit Rev Oncol Hematol , vol.68 , pp. 12-28
    • Benes, P.1    Vetvicka, V.2    Fusek, M.3
  • 9
    • 0024321224 scopus 로고
    • Increased secretion, altered processing, and glycosylation of pro-cathepsin D in human mammary cancer cells
    • Capony F, Rougeot C, Montcourrier P, Cavailles V, Salazar G, Rochefort H. Increased secretion, altered processing and glycosylation of pro-cathepsin D in human mammary cancer cells. Cancer Res 1989; 49:3904-9. (Pubitemid 19197419)
    • (1989) Cancer Research , vol.49 , Issue.14 , pp. 3904-3909
    • Capony, F.1    Rougeot, C.2    Montcourrier, P.3    Cavailles, V.4    Salazar, G.5    Rochefort, H.6
  • 10
    • 0028130332 scopus 로고
    • Specific mannose-6-phosphate receptor-independent sorting of pro-cathepsin D in breast cancer cells
    • Capony F, Braulke T, Rougeot C, Roux S, Montcourrier P, Rochefort H. Specific mannose-6-phosphate receptor-independent sorting of pro-cathepsin D in breast cancer cells. Exp Cell Res 1994; 215:154-63.
    • (1994) Exp Cell Res , vol.215 , pp. 154-163
    • Capony, F.1    Braulke, T.2    Rougeot, C.3    Roux, S.4    Montcourrier, P.5    Rochefort, H.6
  • 11
    • 4544262273 scopus 로고    scopus 로고
    • Defective acidification of intracellular organelles results in aberrant secretion of cathepsin D in cancer cells
    • Kokkonen N, Rivinoja A, Kauppila A, Suokas M, Kellokumpu I, Kellokumpu S. Defective acidification of intracellular organelles results in aberrant secretion of cathepsin D in cancer cells. J Biol Chem 2004; 279:39982-8.
    • (2004) J Biol Chem , vol.279 , pp. 39982-39988
    • Kokkonen, N.1    Rivinoja, A.2    Kauppila, A.3    Suokas, M.4    Kellokumpu, I.5    Kellokumpu, S.6
  • 12
    • 0027287596 scopus 로고
    • Immunoradiometric assay of pro-cathepsin D in breast cancer cytosol: Relative prognostic value versus total cathepsin D
    • Brouillet JP, Spyratos F, Hacene K, Fauque J, Freiss G, Dupont F, et al. Immunoradiometric assay of pro-cathepsin D in breast cancer cytosol: relative prognostic value versus total cathepsin D. Eur J Cancer 1993; 29:1248-51.
    • (1993) Eur J Cancer , vol.29 , pp. 1248-1251
    • Brouillet, J.P.1    Spyratos, F.2    Hacene, K.3    Fauque, J.4    Freiss, G.5    Dupont, F.6
  • 13
    • 0031709904 scopus 로고    scopus 로고
    • Endocytosis of pro-cathepsin D into breast cancer cells is mostly independent of mannose-6-phosphate receptors
    • Laurent-Matha V, Farnoud MR, Lucas A, Rougeot C, Garcia M, Rochefort H. Endocytosis of pro-cathepsin D into breast cancer cells is mostly independent of mannose-6-phosphate receptors. J Cell Sci 1998; 111:2539-49. (Pubitemid 28474957)
    • (1998) Journal of Cell Science , vol.111 , Issue.17 , pp. 2539-2549
    • Laurent-Matha, V.1    Farnoud, M.R.2    Lucas, A.3    Rougeot, C.4    Garcia, M.5    Rochefort, H.6
  • 14
    • 33646367913 scopus 로고    scopus 로고
    • Processing of human cathepsin D is independent of its catalytic function and auto-activation: Involvement of cathepsins L and B
    • Laurent-Matha V, Derocq D, Prebois C, Katunuma N, Liaudet-Coopman E. Processing of human cathepsin D is independent of its catalytic function and auto-activation: involvement of cathepsins L and B. J Biochem 2006; 139:363-71.
    • (2006) J Biochem , vol.139 , pp. 363-371
    • Laurent-Matha, V.1    Derocq, D.2    Prebois, C.3    Katunuma, N.4    Liaudet-Coopman, E.5
  • 15
    • 0037194598 scopus 로고    scopus 로고
    • Cathepsin-D affects multiple tumor progression steps in vivo: Proliferation, angiogenesis and apoptosis
    • Berchem G, Glondu M, Gleizes M, Brouillet JP, Vignon F, Garcia M, et al. Cathepsin-D affects multiple tumor progression steps in vivo: proliferation, angiogenesis and apoptosis. Oncogene 2002; 21:5951-5.
    • (2002) Oncogene , vol.21 , pp. 5951-5955
    • Berchem, G.1    Glondu, M.2    Gleizes, M.3    Brouillet, J.P.4    Vignon, F.5    Garcia, M.6
  • 16
    • 0035909530 scopus 로고    scopus 로고
    • A mutated cathepsin-D devoid of its catalytic activity stimulates the growth of cancer cells
    • DOI 10.1038/sj.onc.1204843
    • Glondu M, Coopman P, Laurent-Matha V, Garcia M, Rochefort H, Liaudet-Coopman E. A mutated cathepsin-D devoid of its catalytic activity stimulates the growth of cancer cells. Oncogene 2001; 20:6920-9. (Pubitemid 33052181)
    • (2001) Oncogene , vol.20 , Issue.47 , pp. 6920-6929
    • Glondu, M.1    Coopman, P.2    Laurent-Matha, V.3    Garcia, M.4    Rochefort, H.5    Liaudet-Coopman, E.6
  • 17
    • 67649220699 scopus 로고    scopus 로고
    • Mammary involution and breast cancer risk: Transgenic models and clinical studies
    • Radisky DC, Hartmann LC. Mammary involution and breast cancer risk: transgenic models and clinical studies. J Mammary Gland Biol Neoplasia 2009; 14:181-91.
    • (2009) J Mammary Gland Biol Neoplasia , vol.14 , pp. 181-191
    • Radisky, D.C.1    Hartmann, L.C.2
  • 18
    • 4944265617 scopus 로고    scopus 로고
    • Epithelial-stromal interactions in the mouse and human mammary gland in vivo
    • Parmar H, Cunha GR. Epithelial-stromal interactions in the mouse and human mammary gland in vivo. Endocr Relat Cancer 2004; 11:437-58.
    • (2004) Endocr Relat Cancer , vol.11 , pp. 437-458
    • Parmar, H.1    Cunha, G.R.2
  • 19
    • 26244464309 scopus 로고    scopus 로고
    • ECM degrading proteases and tissue remodelling in the mammary gland
    • Green KA, Lund LR. ECM degrading proteases and tissue remodelling in the mammary gland. Bioessays 2005; 27:894-903.
    • (2005) Bioessays , vol.27 , pp. 894-903
    • Green, K.A.1    Lund, L.R.2
  • 20
  • 21
    • 8744233052 scopus 로고    scopus 로고
    • Cathepsin D released by lactating rat mammary epithelial cells is involved in prolactin cleavage under physiological conditions
    • Lkhider M, Castino R, Bouguyon E, Isidoro C, Ollivier-Bousquet M. Cathepsin D released by lactating rat mammary epithelial cells is involved in prolactin cleavage under physiological conditions. J Cell Sci 2004; 117:5155-64.
    • (2004) J Cell Sci , vol.117 , pp. 5155-5164
    • Lkhider, M.1    Castino, R.2    Bouguyon, E.3    Isidoro, C.4    Ollivier-Bousquet, M.5
  • 22
    • 33846815521 scopus 로고    scopus 로고
    • A cathepsin D-cleaved 16 kDa form of prolactin mediates postpartum cardiomyopathy
    • Hilfiker-Kleiner D, Kaminski K, Podewski E, Bonda T, Schaefer A, Sliwa K, et al. A cathepsin D-cleaved 16 kDa form of prolactin mediates postpartum cardiomyopathy. Cell 2007; 128:589-600.
    • (2007) Cell , vol.128 , pp. 589-600
    • Hilfiker-Kleiner, D.1    Kaminski, K.2    Podewski, E.3    Bonda, T.4    Schaefer, A.5    Sliwa, K.6
  • 23
    • 0029782494 scopus 로고    scopus 로고
    • Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNFalpha
    • Deiss LP, Galinka H, Berissi H, Cohen O, Kimchi A. Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNFalpha. EMBO J 1996; 15:3861-70.
    • (1996) EMBO J , vol.15 , pp. 3861-3870
    • Deiss, L.P.1    Galinka, H.2    Berissi, H.3    Cohen, O.4    Kimchi, A.5
  • 24
    • 4344699813 scopus 로고    scopus 로고
    • Cathepsin L is involved in cathepsin D processing and regulation of apoptosis in A549 human lung epithelial cells
    • Wille A, Gerber A, Heimburg A, Reisenauer A, Peters C, Saftig P, et al. Cathepsin L is involved in cathepsin D processing and regulation of apoptosis in A549 human lung epithelial cells. Biol Chem 2004; 385:665-70.
    • (2004) Biol Chem , vol.385 , pp. 665-670
    • Wille, A.1    Gerber, A.2    Heimburg, A.3    Reisenauer, A.4    Peters, C.5    Saftig, P.6
  • 25
    • 64249088369 scopus 로고    scopus 로고
    • Nitration of cathepsin D enhances its proteolytic activity during mammary gland remodelling after lactation
    • Zaragoza R, Torres L, Garcia C, Eroles P, Corrales F, Bosch A, et al. Nitration of cathepsin D enhances its proteolytic activity during mammary gland remodelling after lactation. Biochem J 2009; 419:279-88.
    • (2009) Biochem J , vol.419 , pp. 279-288
    • Zaragoza, R.1    Torres, L.2    Garcia, C.3    Eroles, P.4    Corrales, F.5    Bosch, A.6
  • 26
    • 0029953972 scopus 로고    scopus 로고
    • Self-activation of recombinant human lysosomal procathepsin D at a newly engineered cleavage junction, "short" pseudocathepsin D
    • Beyer BM, Dunn BM. Self-activation of recombinant human lysosomal procathepsin D at a newly engineered cleavage junction, "short" pseudocathepsin D. J Biol Chem 1996; 271:15590-6.
    • (1996) J Biol Chem , vol.271 , pp. 15590-15596
    • Beyer, B.M.1    Dunn, B.M.2
  • 27
    • 0019877648 scopus 로고
    • Biosynthesis of a lysosomal enzyme. Partial structure of two transient and functionally distinct NH2-terminal sequences in cathepsin D
    • Erickson AH, Conner GE, Blobel G. Biosynthesis of a lysosomal enzyme. Partial structure of two transient and functionally distinct NH2-terminal sequences in cathepsin D. J Biol Chem 1981; 256:11224-31.
    • (1981) J Biol Chem , vol.256 , pp. 11224-11231
    • Erickson, A.H.1    Conner, G.E.2    Blobel, G.3
  • 28
    • 0029070829 scopus 로고
    • Role of glycosylation in the expression of human procathepsin D
    • Fortenberry SC, Schorey JS, Chirgwin JM. Role of glycosylation in the expression of human procathepsin D. J Cell Sci 1995; 108:2001-6.
    • (1995) J Cell Sci , vol.108 , pp. 2001-2006
    • Fortenberry, S.C.1    Schorey, J.S.2    Chirgwin, J.M.3
  • 29
    • 33645322443 scopus 로고    scopus 로고
    • Pregnancy-associated breast cancer and metastasis
    • Schedin P. Pregnancy-associated breast cancer and metastasis. Nat Rev Cancer 2006; 6:281-91.
    • (2006) Nat Rev Cancer , vol.6 , pp. 281-291
    • Schedin, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.