메뉴 건너뛰기




Volumn 10, Issue 6, 2004, Pages

Acetylsalicylic acid-dependent inhibition of collagen biosynthesis and β1-integrin signaling in cultured fibroblasts

Author keywords

Acetylsalicylic acid; Collagen; Fibroblast; Intracellular signaling; Prolidase

Indexed keywords

ACETYLSALICYLIC ACID; BETA1 INTEGRIN; COLLAGEN; FOCAL ADHESION KINASE; INTEGRIN RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; NONSTEROID ANTIINFLAMMATORY AGENT; PROLINE; PROLINE DIPEPTIDASE; PROTEIN GRAB2; SOS PROTEIN; THREONINE; UNCLASSIFIED DRUG;

EID: 3042816317     PISSN: 12341010     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (21)

References (31)
  • 1
    • 0028399309 scopus 로고
    • Role of inducible cyclooxygenase (COX-2) in inflammation
    • Seibert K, Masferrer JL: Role of inducible cyclooxygenase (COX-2) in inflammation. Receptor, 1994; 4: 17-23
    • (1994) Receptor , vol.4 , pp. 17-23
    • Seibert, K.1    Masferrer, J.L.2
  • 2
    • 0024528916 scopus 로고
    • The mechanisms of action of non-steroidal antiinflammatory drugs
    • Abramson SB, Weissman G: The mechanisms of action of non-steroidal antiinflammatory drugs. Arthritis Rheum, 1989; 32: 1-9
    • (1989) Arthritis Rheum , vol.32 , pp. 1-9
    • Abramson, S.B.1    Weissman, G.2
  • 3
    • 0035671557 scopus 로고    scopus 로고
    • Cyclooxygenase-1 and cyclooxygenase-2 selectivity of non-steroidal anti-inflammatory drugs: Investigation using human peripheral monocytes
    • Kato M, Nishida S, Kitasato H et al: Cyclooxygenase-1 and cyclooxygenase-2 selectivity of non-steroidal anti-inflammatory drugs: investigation using human peripheral monocytes. J Pharm Pharmacol, 2001; 53: 1679-85
    • (2001) J Pharm Pharmacol , vol.53 , pp. 1679-1685
    • Kato, M.1    Nishida, S.2    Kitasato, H.3
  • 4
    • 0030423854 scopus 로고    scopus 로고
    • Inhibition of prolidase activity by non-steroid antiinflammatory drugs in cultured human skin fibroblasts
    • Miltyk W, Karna E, Pałka J: Inhibition of prolidase activity by non-steroid antiinflammatory drugs in cultured human skin fibroblasts. Pol J Pharmacol, 1996; 48: 609-13
    • (1996) Pol J Pharmacol , vol.48 , pp. 609-613
    • Miltyk, W.1    Karna, E.2    Pałka, J.3
  • 5
    • 17644446471 scopus 로고    scopus 로고
    • The mechanism of daunorubicin-induced inhibition of prolidase activity in human skin fibroblasts and its implication to impaired collagen biosynthesis
    • Muszynska A, Pałka J, Gorodkiewicz E: The mechanism of daunorubicin-induced inhibition of prolidase activity in human skin fibroblasts and its implication to impaired collagen biosynthesis. Exp Toxicol Pathol, 2000; 52: 149-55
    • (2000) Exp Toxicol Pathol , vol.52 , pp. 149-155
    • Muszynska, A.1    Pałka, J.2    Gorodkiewicz, E.3
  • 6
    • 0030323134 scopus 로고    scopus 로고
    • Modulation of prolidase activity during in vitro aging of human skin fibroblasts the role of extracellular matrix collagen
    • Pałka J, Miltyk W, Karna E, Wołczyński S: Modulation of prolidase activity during in vitro aging of human skin fibroblasts the role of extracellular matrix collagen. Tokai J Exp Clin Med, 1996; 21: 207-213
    • (1996) Tokai J Exp Clin Med , vol.21 , pp. 207-213
    • Pałka, J.1    Miltyk, W.2    Karna, E.3    Wołczyński, S.4
  • 7
    • 0034019794 scopus 로고    scopus 로고
    • Potential role of pyrroline 5-carboxylate in regulation of collagen biosynthesis in cultured human skin fibroblasts
    • Miltyk W, Pałka JA: Potential role of pyrroline 5-carboxylate in regulation of collagen biosynthesis in cultured human skin fibroblasts. Comp Biochem Physiol A Mol Integr Physiol, 2000; 125: 265-271
    • (2000) Comp Biochem Physiol A Mol Integr Physiol , vol.125 , pp. 265-271
    • Miltyk, W.1    Pałka, J.A.2
  • 8
  • 9
    • 0025243440 scopus 로고
    • Specificity and pH dependence for acylproline cleavage by prolidase
    • Mock WL, Green PC, Boyer KD: Specificity and pH dependence for acylproline cleavage by prolidase. J Biol Chem, 1990; 265: 19600-605
    • (1990) J Biol Chem , vol.265 , pp. 19600-19605
    • Mock, W.L.1    Green, P.C.2    Boyer, K.D.3
  • 10
    • 0024413070 scopus 로고
    • Collagen biosynthetic anomalies in prolidase deficiency: Effect of glycyl-L-proline on the degradation of newly synthesized collagen
    • Chamson A, Voigtlander V, Myara I, Frey J: Collagen biosynthetic anomalies in prolidase deficiency: effect of glycyl-L-proline on the degradation of newly synthesized collagen. Clin Physiol Bioch, 1989; 7: 128-136
    • (1989) Clin Physiol Bioch , vol.7 , pp. 128-136
    • Chamson, A.1    Voigtlander, V.2    Myara, I.3    Frey, J.4
  • 11
    • 0027439867 scopus 로고
    • Proline-dependent structural and biological properties of peptides and proteins
    • Yaron A, Naider F: Proline-dependent structural and biological properties of peptides and proteins. Crit Rev Biochem Mol Biol, 1993; 28: 31-81
    • (1993) Crit Rev Biochem Mol Biol , vol.28 , pp. 31-81
    • Yaron, A.1    Naider, F.2
  • 12
    • 0027276281 scopus 로고
    • Hydrolysis of proline dipeptides completely fulfills the proline requirement in a proline - Auxotropic Chinese Hamster Ovary cell line
    • Emmerson KS, Phang JM: Hydrolysis of proline dipeptides completely fulfills the proline requirement in a proline - auxotropic Chinese Hamster Ovary cell line. J Nutr, 1993; 123: 909-14
    • (1993) J Nutr , vol.123 , pp. 909-914
    • Emmerson, K.S.1    Phang, J.M.2
  • 13
    • 0016591014 scopus 로고
    • Iminopeptiduria: A genetic defect in recycling of collagen; a method for determining prolidase in erythrocytes
    • Jackson SH, Dennis AW, Greenberg M: Iminopeptiduria: a genetic defect in recycling of collagen; a method for determining prolidase in erythrocytes. CMA Journal, 1975; 113: 759-63
    • (1975) CMA Journal , vol.113 , pp. 759-763
    • Jackson, S.H.1    Dennis, A.W.2    Greenberg, M.3
  • 14
    • 0030930783 scopus 로고    scopus 로고
    • Prolidase activity in fibroblasts is regulated by interaction of extracellular matrix with cell surface integrin receptors
    • Pałka JA, Phang JM: Prolidase activity in fibroblasts is regulated by interaction of extracellular matrix with cell surface integrin receptors. J Cell Biochem, 1997; 67: 166-175
    • (1997) J Cell Biochem , vol.67 , pp. 166-175
    • Pałka, J.A.1    Phang, J.M.2
  • 15
    • 0033137070 scopus 로고    scopus 로고
    • Extracellular matrix and integrin signalling: The shape of things to come
    • Boudreau NJ, Jones PL: Extracellular matrix and integrin signalling: the shape of things to come. Biochem J, 1999; 339: 481-88
    • (1999) Biochem J , vol.339 , pp. 481-488
    • Boudreau, N.J.1    Jones, P.L.2
  • 16
    • 0034994101 scopus 로고    scopus 로고
    • Phosphorylation of prolidase increases the enzyme activity
    • Surażyński A, Pałka J, Wolczynski S: Phosphorylation of prolidase increases the enzyme activity. Mol Cell Biochem, 2001; 220: 95-101
    • (2001) Mol Cell Biochem , vol.220 , pp. 95-101
    • Surazyński, A.1    Pałka, J.2    Wolczynski, S.3
  • 17
    • 0019904296 scopus 로고
    • Optimal conditions for prolidase assay by proline colorimetric determination: Application to imidodipeptiduria
    • Myara I, Charpentier C, Lemonnier A: Optimal conditions for prolidase assay by proline colorimetric determination: application to imidodipeptiduria. Clin Chim Acta, 1982; 125: 193-205
    • (1982) Clin Chim Acta , vol.125 , pp. 193-205
    • Myara, I.1    Charpentier, C.2    Lemonnier, A.3
  • 18
    • 33749787148 scopus 로고
    • Photometric estimation of proline and ornithine
    • Chinard FP: Photometric estimation of proline and ornithine. J Biol Chem, 1952; 199: 91-95
    • (1952) J Biol Chem , vol.199 , pp. 91-95
    • Chinard, F.P.1
  • 20
    • 0025060724 scopus 로고
    • Scorbutic and fasted guinea pig sera contain an insulin-like growth factor I reversible inhibitor of proteoglycan and collagen synthesis in chick embryo chondrocytes and adult human skin fibroblasts
    • Oyamada I, Pałka J, Schalk EM et al: Scorbutic and fasted guinea pig sera contain an insulin-like growth factor I reversible inhibitor of proteoglycan and collagen synthesis in chick embryo chondrocytes and adult human skin fibroblasts. Arch Biochem Biophy, 1990; 276: 85-93
    • (1990) Arch Biochem Biophy , vol.276 , pp. 85-93
    • Oyamada, I.1    Pałka, J.2    Schalk, E.M.3
  • 21
    • 84955191506 scopus 로고
    • Determination of collagen synthesis in tissue and cell culture system
    • Furthmay M, ed. Boca Raton FL: CRC Press
    • Peterkofsky B, Chojkier M, Bateman J: Determination of collagen synthesis in tissue and cell culture system. In: Furthmay M, ed. Immunochemistry of the Extracellular Matrix. Boca Raton FL: CRC Press, 1982:19-47
    • (1982) Immunochemistry of the Extracellular Matrix , pp. 19-47
    • Peterkofsky, B.1    Chojkier, M.2    Bateman, J.3
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of baceriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of baceriophage T4. Nature (London), 1970; 227: 680-85
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0025156158 scopus 로고
    • The effect of some antiinflammatory drugs on collagen of rat skin
    • Pałka J, Galewska Z: The effect of some antiinflammatory drugs on collagen of rat skin. Pol J Pharmacol Pharm, 1990; 42: 39-42
    • (1990) Pol J Pharmacol Pharm , vol.42 , pp. 39-42
    • Pałka, J.1    Galewska, Z.2
  • 24
    • 0031732469 scopus 로고    scopus 로고
    • Insulin-like growth factor I - Dependent regulation of prolidase activity in cultured human skin fibroblasts
    • Miltyk W, Karna E, Wołczyński S, Pałka JA: Insulin-like growth factor I - dependent regulation of prolidase activity in cultured human skin fibroblasts. Mol Cell Biochem, 1998; 189: 177-84
    • (1998) Mol Cell Biochem , vol.189 , pp. 177-184
    • Miltyk, W.1    Karna, E.2    Wołczyński, S.3    Pałka, J.A.4
  • 25
    • 0025205276 scopus 로고
    • Integrins and other cell adhesion molecules
    • Albelda SM, Buck CA: Integrins and other cell adhesion molecules. FASEB J, 1990; 4: 2868-80
    • (1990) FASEB J , vol.4 , pp. 2868-2880
    • Albelda, S.M.1    Buck, C.A.2
  • 26
    • 0020456385 scopus 로고
    • How does extracellular matrix direct gene expression?
    • Bissel M: How does extracellular matrix direct gene expression? J Theor Biol, 1981; 99: 31-68
    • (1981) J Theor Biol , vol.99 , pp. 31-68
    • Bissel, M.1
  • 27
    • 0028799028 scopus 로고
    • Expression of c-ets-1, collagenase 1, and urokinase - Type plasminogen activator genes in lung carcinomas
    • Bolon I, Gouyer V, Devouassoux M et al: Expression of c-ets-1, collagenase 1, and urokinase - type plasminogen activator genes in lung carcinomas. Am J Pathol, 1995; 147: 1298-310
    • (1995) Am J Pathol , vol.147 , pp. 1298-1310
    • Bolon, I.1    Gouyer, V.2    Devouassoux, M.3
  • 29
    • 0025978352 scopus 로고
    • Control of growth and differentiation of vascular cells by extracellular matrix
    • Carey DJ: Control of growth and differentiation of vascular cells by extracellular matrix. Ann Rev Physiol, 1991; 53: 161-77
    • (1991) Ann Rev Physiol , vol.53 , pp. 161-177
    • Carey, D.J.1
  • 30
    • 0026903388 scopus 로고
    • Control of cell motility and tumor invasion by extracellular matrix interaction
    • Ruoslahti E: Control of cell motility and tumor invasion by extracellular matrix interaction. Br J Cancer, 1992; 66: 239-42
    • (1992) Br J Cancer , vol.66 , pp. 239-242
    • Ruoslahti, E.1
  • 31
    • 0024583005 scopus 로고
    • Primary structure and gene localization of human prolidase
    • Endo F, Tanoue A, Nakai H et al: Primary structure and gene localization of human prolidase. J Biol Chem, 1989; 264: 4476-81
    • (1989) J Biol Chem , vol.264 , pp. 4476-4481
    • Endo, F.1    Tanoue, A.2    Nakai, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.