메뉴 건너뛰기




Volumn 168, Issue 1-2, 1997, Pages 177-183

Fibroblast chemotaxis and prolidase activity modulation by insulin-like growth factor II and mannose 6-phosphate

Author keywords

Chemotaxis; Fibroblasts; Mannose 6 phosphate; Prolidase

Indexed keywords

ALPHA MANNOSIDASE; CATHEPSIN D; CYTOKINE; LYSOSOME ENZYME; MANNOSE 6 PHOSPHATE; PEPSTATIN; PROLINE DIPEPTIDASE; SOMATOMEDIN B; SOMATOMEDIN B RECEPTOR;

EID: 0031040948     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006842315499     Document Type: Article
Times cited : (47)

References (34)
  • 1
    • 0024419880 scopus 로고
    • Involvement of protein kinase C in signal transduction during fibroblast chemotaxis to platelet-derived growth factor and a fragment of fibronectin
    • Adelmann-Grill BC, Wach F, Behr J, Krieg T et al: Involvement of protein kinase C in signal transduction during fibroblast chemotaxis to platelet-derived growth factor and a fragment of fibronectin. Eur J Cell Biol 50: 128-131, 1989
    • (1989) Eur J Cell Biol , vol.50 , pp. 128-131
    • Adelmann-Grill, B.C.1    Wach, F.2    Behr, J.3    Krieg, T.4
  • 2
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner JF Jr: Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J 5: 2145-2154, 1991
    • (1991) FASEB J , vol.5 , pp. 2145-2154
    • Woessner Jr., J.F.1
  • 3
    • 0008592479 scopus 로고
    • Intracellular proteolysis
    • A Neuberger and K Brocklehurst (eds).
    • Bohley P: Intracellular proteolysis. In: A Neuberger and K Brocklehurst (eds). Hydrolytic Enzymes. Elsevier Sci Publ, 1987, pp 307-331
    • (1987) Hydrolytic Enzymes. Elsevier Sci Publ , pp. 307-331
    • Bohley, P.1
  • 4
    • 0017169539 scopus 로고
    • The structure activity relations of synthetic peptides as chemotactic factors and inducers of lysosomal enzyme secretion for neutrophils
    • Showell HJ, Freer RJ, Zigmond SH, Schiffmann E, Aswanikumar S, Corcoran B, Becker EL: The structure activity relations of synthetic peptides as chemotactic factors and inducers of lysosomal enzyme secretion for neutrophils. J Exp Med 143: 1154-1169, 1976
    • (1976) J Exp Med , vol.143 , pp. 1154-1169
    • Showell, H.J.1    Freer, R.J.2    Zigmond, S.H.3    Schiffmann, E.4    Aswanikumar, S.5    Corcoran, B.6    Becker, E.L.7
  • 5
    • 8044261219 scopus 로고
    • Relation of protease action on the cell surface to growth control and adhesion
    • E Reich, DB Rifkin, E Shawl (eds). Cold Spring Harbor
    • Blumberg PM, Robbins PW: Relation of protease action on the cell surface to growth control and adhesion. In: E Reich, DB Rifkin, E Shawl (eds). Proteases and Biological Control. Cold Spring Harbor, 1975, pp 945-956
    • (1975) Proteases and Biological Control , pp. 945-956
    • Blumberg, P.M.1    Robbins, P.W.2
  • 6
    • 0022348139 scopus 로고
    • Cell-mediated extracellular acidification and bone resorption: Evidence for a low pH in resorbing lacunae and localization of a 100 kD lysosomal membrane protein at the osteoclast ruffled border
    • Baron R, Neff L, Louvard D, Courtoy PJ: Cell-mediated extracellular acidification and bone resorption: evidence for a low pH in resorbing lacunae and localization of a 100 kD lysosomal membrane protein at the osteoclast ruffled border. J Cell Biol 101: 2210-2222, 1985
    • (1985) J Cell Biol , vol.101 , pp. 2210-2222
    • Baron, R.1    Neff, L.2    Louvard, D.3    Courtoy, P.J.4
  • 7
    • 0022555844 scopus 로고
    • Lysosomal enzymes and their receptors
    • Von Figura K, Hasilik A: Lysosomal enzymes and their receptors. Ann Rev Biochem 55: 167-193, 1986
    • (1986) Ann Rev Biochem , vol.55 , pp. 167-193
    • Von Figura, K.1    Hasilik, A.2
  • 8
    • 0022572229 scopus 로고
    • Trafficking of lysosomal enzymes in normal and disease states
    • Kornfeld S: Trafficking of lysosomal enzymes in normal and disease states. J Clin Invest 77: 1-6, 1986
    • (1986) J Clin Invest , vol.77 , pp. 1-6
    • Kornfeld, S.1
  • 9
    • 0021742661 scopus 로고
    • The mannose 6-phosphate receptor: Function, biosynthesis and translocation
    • Sahagian GG: The mannose 6-phosphate receptor: function, biosynthesis and translocation. Biol Cell 51: 207-214, 1984
    • (1984) Biol Cell , vol.51 , pp. 207-214
    • Sahagian, G.G.1
  • 11
    • 0025321110 scopus 로고
    • Beta-galactosidase decreases the binding affinity of the insulin-like growth factor-II/mannose 6-phosphate receptor for the insulin-like growth factor II
    • Kiess W, Thomas CL, Sklar MM, Nissley SP: Beta-galactosidase decreases the binding affinity of the insulin-like growth factor-II/mannose 6-phosphate receptor for the insulin-like growth factor II. Eur J Biochem 190: 71-77, 1990
    • (1990) Eur J Biochem , vol.190 , pp. 71-77
    • Kiess, W.1    Thomas, C.L.2    Sklar, M.M.3    Nissley, S.P.4
  • 12
    • 0024512027 scopus 로고
    • Insulin like growth factor-II (IGF-II) inhibits both the cellular uptake of β-galactosidase and the binding of β- Galactosidase to purified IGF-II/mannose 6-phosphate receptor
    • Kiess W, Thomas CL, Geenstein LA, Lee L, Sklar MM, Rechler MM, Sahagian GG, Nissley SP: Insulin like growth factor-II (IGF-II) inhibits both the cellular uptake of β-galactosidase and the binding of β- galactosidase to purified IGF-II/mannose 6-phosphate receptor. J Biol Chem 264: 4710-4714, 1989
    • (1989) J Biol Chem , vol.264 , pp. 4710-4714
    • Kiess, W.1    Thomas, C.L.2    Geenstein, L.A.3    Lee, L.4    Sklar, M.M.5    Rechler, M.M.6    Sahagian, G.G.7    Nissley, S.P.8
  • 14
    • 0016591014 scopus 로고
    • Iminodipeptiduria: A genetic defect in recycling of collagen; a method for determining prolidase in erythrocytes
    • Jackson SH, Dennis AW, Greenberg M: Iminodipeptiduria: a genetic defect in recycling of collagen; a method for determining prolidase in erythrocytes. CMA Journal 113: 759-763, 1975
    • (1975) CMA Journal , vol.113 , pp. 759-763
    • Jackson, S.H.1    Dennis, A.W.2    Greenberg, M.3
  • 15
    • 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 28: 31- 81, 1993
    • (1993) Crit Rev Biochem Mol Biol , vol.28 , pp. 31-81
    • Yaron, A.1    Naider, F.2
  • 16
    • 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 123: 909-914, 1993
    • (1993) J Nutr , vol.123 , pp. 909-914
    • Emmerson, K.S.1    Phang, J.M.2
  • 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 125: 193-205, 1982
    • (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 199: 91-95, 1952
    • (1952) J Biol Chem , vol.199 , pp. 91-95
    • Chinard, F.P.1
  • 20
    • 0018937957 scopus 로고
    • Destruction of extracellular matrices containing glycoproteins, elastin and collagen by metastatic human tumor cells
    • Jones PA, DeClerck YA: Destruction of extracellular matrices containing glycoproteins, elastin and collagen by metastatic human tumor cells. Cancer Res 40: 3222-3227, 1980
    • (1980) Cancer Res , vol.40 , pp. 3222-3227
    • Jones, P.A.1    DeClerck, Y.A.2
  • 21
    • 4243967697 scopus 로고
    • Solubility and proteolytic susceptibility of native and denatured haemoglobin and casein
    • Worowski K, Roszkowska W: Solubility and proteolytic susceptibility of native and denatured haemoglobin and casein (in Polish) Acta Polon Pharm 36: 721-728, 1979
    • (1979) Acta Polon Pharm , vol.36 , pp. 721-728
    • Worowski, K.1    Roszkowska, W.2
  • 22
    • 0001247393 scopus 로고
    • Tyrosine and tryptophan determination in protein
    • Folin D, Ciocalteau V: Tyrosine and tryptophan determination in protein. J Biol Chem 73: 627-631, 1927
    • (1927) J Biol Chem , vol.73 , pp. 627-631
    • Folin, D.1    Ciocalteau, V.2
  • 23
    • 0022404587 scopus 로고
    • Cell density affects prolidase and prolinase activity and intracellular amino acid levels in cultured human cells
    • Myara I, Charpentier C, Gantier M, Lemonnier A: Cell density affects prolidase and prolinase activity and intracellular amino acid levels in cultured human cells. Clin Chim Acta 150: 1-9, 1985
    • (1985) Clin Chim Acta , vol.150 , pp. 1-9
    • Myara, I.1    Charpentier, C.2    Gantier, M.3    Lemonnier, A.4
  • 24
    • 0027371512 scopus 로고
    • Changes in IGF-binding proteins in rats with experimental diabetes
    • Pałka J, Bańkowski E, Wolańska M: Changes in IGF-binding proteins in rats with experimental diabetes. Ann Biol Clin 50: 701-706, 1993
    • (1993) Ann Biol Clin , vol.50 , pp. 701-706
    • Pałka, J.1    Bańkowski, E.2    Wolańska, M.3
  • 25
    • 0037963468 scopus 로고
    • Proteolytic activity and collagen synthesis in skin wound of rats with experimental diabetes
    • Pałka J, Wolańska M, Galewska Z, Bańkowski E: Proteolytic activity and collagen synthesis in skin wound of rats with experimental diabetes. Medycyna 2000 11: 39-43, 1991
    • (1991) Medycyna 2000 , vol.11 , pp. 39-43
    • Pałka, J.1    Wolańska, M.2    Galewska, Z.3    Bańkowski, E.4
  • 26
    • 0030025908 scopus 로고    scopus 로고
    • Decrease in the glycosaminoglycan content in the skin of diabetic rats. the role of IGF-I, IGF-binding proteins and proteolytic activity
    • Cechowska-Pasko M, Pałka J, Bańkowski E: Decrease in the glycosaminoglycan content in the skin of diabetic rats. The role of IGF-I, IGF-binding proteins and proteolytic activity. Mol Cell Biochem 154: 1-8, 1996
    • (1996) Mol Cell Biochem , vol.154 , pp. 1-8
    • Cechowska-Pasko, M.1    Pałka, J.2    Bańkowski, E.3
  • 27
    • 0024155411 scopus 로고
    • Similar hormonal changes in sera from scorbutic and fasted (Vitamin C-supplemented) guinea pigs, including decreased IGF-I and appearance of an IGF-I reversible mitogenic inhibitor
    • Pałka J, Bird TA, Oyamada I, Peterkofsky B: Similar hormonal changes in sera from scorbutic and fasted (Vitamin C-supplemented) guinea pigs, including decreased IGF-I and appearance of an IGF-I reversible mitogenic inhibitor. Growth Factors I: 147-156, 1989
    • (1989) Growth Factors , vol.1 , pp. 147-156
    • Pałka, J.1    Bird, T.A.2    Oyamada, I.3    Peterkofsky, B.4
  • 28
    • 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, Takeda K, Peterkofsky B: 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 Biophys 276: 86-93, 1990
    • (1990) Arch Biochem Biophys , vol.276 , pp. 86-93
    • Oyamada, I.1    Pałka, J.2    Schalk, E.M.3    Takeda, K.4    Peterkofsky, B.5
  • 29
    • 0024509261 scopus 로고
    • Differential stimulation of collagenase and chemotactic activity in fibroblasts derived from rat wound repair tissue and human skin by growth factors
    • Buckley-SturrockA, Woodward SC, Senior RM, Griffin GL, Klagsbran M, Davidson JM: Differential stimulation of collagenase and chemotactic activity in fibroblasts derived from rat wound repair tissue and human skin by growth factors. J Cell Physiol 138: 70-78, 1989
    • (1989) J Cell Physiol , vol.138 , pp. 70-78
    • Buckley-SturrockA1    Woodward, S.C.2    Senior, R.M.3    Griffin, G.L.4    Klagsbran, M.5    Davidson, J.M.6
  • 30
    • 0019964846 scopus 로고
    • Chemotactic responses of fibroblasts to tropoelastin and elastin-derived peptides
    • Senior RM, Griffin GL, Mecham RP: Chemotactic responses of fibroblasts to tropoelastin and elastin-derived peptides. J Clin Invest 70: 614-618, 1982
    • (1982) J Clin Invest , vol.70 , pp. 614-618
    • Senior, R.M.1    Griffin, G.L.2    Mecham, R.P.3
  • 31
    • 0020574566 scopus 로고
    • A study on fibroblast chemotaxis using fibronectin and conditional medium as chemoattractants
    • Mensing H, Pontz BF, Müller PK, Ganse-Müller V: A study on fibroblast chemotaxis using fibronectin and conditional medium as chemoattractants. Eur J Cell Biol 29: 268-273, 1983
    • (1983) Eur J Cell Biol , vol.29 , pp. 268-273
    • Mensing, H.1    Pontz, B.F.2    Müller, P.K.3    Ganse-Müller, V.4
  • 32
    • 0025781785 scopus 로고
    • Platelet-derived growth factor activates phospholipase D and chemotactic response in vascular smooth muscle cells
    • Welsh CJ, Schmeichel K, McBride K: Platelet-derived growth factor activates phospholipase D and chemotactic response in vascular smooth muscle cells. In vitro Cell Dev Biol 27 A: 425-431, 1991
    • (1991) In Vitro Cell Dev Biol , vol.27 A , pp. 425-431
    • Welsh, C.J.1    Schmeichel, K.2    McBride, K.3
  • 33
    • 0025062521 scopus 로고
    • Involvement of protein kinase C in the mitogenic and chemotaxis effects of basic fibroblast growth factor on bovine cerebral cortex capillary endothelial cells
    • Daviet L, Herbert JM, Maffrand JP: Involvement of protein kinase C in the mitogenic and chemotaxis effects of basic fibroblast growth factor on bovine cerebral cortex capillary endothelial cells. FEBS Lett 259: 315-317, 1990
    • (1990) FEBS Lett , vol.259 , pp. 315-317
    • Daviet, L.1    Herbert, J.M.2    Maffrand, J.P.3
  • 34
    • 0023117172 scopus 로고
    • Proteolytic activation of protein kinase C: A physiological reaction?
    • Murray AW, Fournier A, Hardy SJ: Proteolytic activation of protein kinase C: a physiological reaction? TIBS 12: 55-56, 1987
    • (1987) TIBS , vol.12 , pp. 55-56
    • Murray, A.W.1    Fournier, A.2    Hardy, S.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.