메뉴 건너뛰기




Volumn 66, Issue 4, 1996, Pages 1599-1609

Polyamine modification increases the permeability of proteins at the blood-nerve and blood-brain barriers

Author keywords

Albumin; Blood brain barrier; Blood nerve barrier; IgG; Insulin; Polyamine; Superoxide dismutase

Indexed keywords

ALBUMIN; BRAIN PROTEIN; IMMUNOGLOBULIN G; POLYAMINE; PUTRESCINE; SPERMIDINE; SPERMINE; SUPEROXIDE DISMUTASE;

EID: 0029976387     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.66041599.x     Document Type: Article
Times cited : (82)

References (71)
  • 1
    • 0019907789 scopus 로고
    • Post-translational modification of neuronal proteins: Evidence for transglutaminase activity in R2, the giant cholinergic neuron of Aplysia
    • Ambron R. T. and Kremzner L. T. (1982) Post-translational modification of neuronal proteins: evidence for transglutaminase activity in R2, the giant cholinergic neuron of Aplysia. Proc. Natl. Acad. Sci. USA 79, 3442-3446.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3442-3446
    • Ambron, R.T.1    Kremzner, L.T.2
  • 3
    • 0021681204 scopus 로고
    • A brain-to-blood carrier-mediated transport system for small, n-tyrosinated peptides
    • Banks W. A. and Kastin A. J. (1984) A brain-to-blood carrier-mediated transport system for small, n-tyrosinated peptides. Pharmacol. Biochem. Behav. 21, 943-946.
    • (1984) Pharmacol. Biochem. Behav. , vol.21 , pp. 943-946
    • Banks, W.A.1    Kastin, A.J.2
  • 4
    • 0025362892 scopus 로고
    • Peptide transport systems for opiates across the blood-brain barrier
    • Banks W. A and Kastin E. J (1990) Peptide transport systems for opiates across the blood-brain barrier. Am. J. Physiol. 259, E1-E10.
    • (1990) Am. J. Physiol. , vol.259
    • Banks, W.A.1    Kastin, E.J.2
  • 5
    • 0023578366 scopus 로고
    • Carrier-mediated transport of vasopressin across the blood-brain barrier of the mouse
    • Banks W. A., Kastin A. J., Horvath A., and Michals E. A. (1987) Carrier-mediated transport of vasopressin across the blood-brain barrier of the mouse. J. Neurosci. Res. 18, 326-332.
    • (1987) J. Neurosci. Res. , vol.18 , pp. 326-332
    • Banks, W.A.1    Kastin, A.J.2    Horvath, A.3    Michals, E.A.4
  • 6
    • 0024849292 scopus 로고
    • Bidirectional transport of interleukin-1 alpha across the blood-brain barrier
    • Banks W. A., Kastin A. J., and Durham D. A. (1989) Bidirectional transport of interleukin-1 alpha across the blood-brain barrier. Brain Res. Bull. 23, 433-437.
    • (1989) Brain Res. Bull. , vol.23 , pp. 433-437
    • Banks, W.A.1    Kastin, A.J.2    Durham, D.A.3
  • 7
    • 0025955822 scopus 로고
    • Delivering peptides to the central nervous system: Dilemmas and strategies
    • Banks W. A., Kastin A. J., and Barrera C. M. (1991) Delivering peptides to the central nervous system: dilemmas and strategies. Pharm. Res. 8, 1345-1350.
    • (1991) Pharm. Res. , vol.8 , pp. 1345-1350
    • Banks, W.A.1    Kastin, A.J.2    Barrera, C.M.3
  • 8
    • 0027055922 scopus 로고
    • Permeability of the blood-brain barrier to peptides: An approach to the development of therapeutically useful analogs
    • Banks W A., Audus K. L., and Davis T. P. (1992) Permeability of the blood-brain barrier to peptides: an approach to the development of therapeutically useful analogs. Peptides 13, 1289-1294.
    • (1992) Peptides , vol.13 , pp. 1289-1294
    • Banks, W.A.1    Audus, K.L.2    Davis, T.P.3
  • 9
    • 0027184484 scopus 로고
    • Endogenous peptide tyr-pro-trp-gly-NH2 (tyr-w-MIF-1) is transported from the brain to the blood by peptide transport system-1
    • Banks W. A., Kastin A. J., and Ehrensing C. A. (1993) Endogenous peptide tyr-pro-trp-gly-NH2 (tyr-w-MIF-1) is transported from the brain to the blood by peptide transport system-1. J. Neurosci. Res. 35, 690-695.
    • (1993) J. Neurosci. Res. , vol.35 , pp. 690-695
    • Banks, W.A.1    Kastin, A.J.2    Ehrensing, C.A.3
  • 10
    • 0023522549 scopus 로고
    • 1]-Peptide T-amide is transported from blood to brain by a saturable system
    • 1]-Peptide T-amide is transported from blood to brain by a saturable system. Brain Res. Bull. 19, 629-633.
    • (1987) Brain Res. Bull. , vol.19 , pp. 629-633
    • Barrera, C.M.1    Kastin, A.J.2    Banks, W.A.3
  • 12
    • 0024283029 scopus 로고
    • Covalent incorporation of polyamines as gamma-glutamyl derivatives into CHO cell protein
    • Beninati S., Piacentini M., Cocuzzi E. R., Autuori F., and Folk J. E. (1988) Covalent incorporation of polyamines as gamma-glutamyl derivatives into CHO cell protein. Biochim. Biophys. Acta 952, 325-333.
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 325-333
    • Beninati, S.1    Piacentini, M.2    Cocuzzi, E.R.3    Autuori, F.4    Folk, J.E.5
  • 13
    • 0023153692 scopus 로고
    • Posttranslational protein modification by polyamines in intact and regenerating nerves
    • Chakraborty G., Leach T., Zanakis M. F., Sturman J. A., and Ingoglia N A. (1987) Posttranslational protein modification by polyamines in intact and regenerating nerves. J. Neurochem. 48, 669-675.
    • (1987) J. Neurochem. , vol.48 , pp. 669-675
    • Chakraborty, G.1    Leach, T.2    Zanakis, M.F.3    Sturman, J.A.4    Ingoglia, N.A.5
  • 14
    • 0020492513 scopus 로고
    • Carbamoylation of Cu,Zn-superoxide dismutase by cyanate. Role of lysines in the enzyme action
    • Cocco D., Rossi L., Barra D., Bossa F., and Rotilio G. (1982) Carbamoylation of Cu,Zn-superoxide dismutase by cyanate. Role of lysines in the enzyme action. FEBS Lett. 150, 303-306.
    • (1982) FEBS Lett. , vol.150 , pp. 303-306
    • Cocco, D.1    Rossi, L.2    Barra, D.3    Bossa, F.4    Rotilio, G.5
  • 15
    • 0020162215 scopus 로고
    • Posttranslational formation of hypusine in a single major protein occurs generally in growing cells and is associated with activation of lymphocyte growth
    • Cooper H. L., Park M. H., and Folk J. E. (1982) Posttranslational formation of hypusine in a single major protein occurs generally in growing cells and is associated with activation of lymphocyte growth. Cell 29, 791-797.
    • (1982) Cell , vol.29 , pp. 791-797
    • Cooper, H.L.1    Park, M.H.2    Folk, J.E.3
  • 17
    • 0020357311 scopus 로고
    • Electrostatic interactions in the reaction mechanism of bovine erythrocyte superoxide dismutase
    • Cudd A. and Fridovich I. (1982) Electrostatic interactions in the reaction mechanism of bovine erythrocyte superoxide dismutase. J. Biol. Chem. 257, 11443-11447.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11443-11447
    • Cudd, A.1    Fridovich, I.2
  • 19
    • 0018816617 scopus 로고
    • Transglutaminases
    • Folk J. E. (1980) Transglutaminases. Annu. Rev Biochem. 49, 517-531.
    • (1980) Annu. Rev Biochem. , vol.49 , pp. 517-531
    • Folk, J.E.1
  • 20
    • 0020698882 scopus 로고
    • Mechanism and basis for specificity of transglutaminase-catalyzed epsilon-(gamma-glutamyl) lysine bond formation
    • (Meister A., ed). Wiley and Sons, New York
    • Folk J. E. (1983) Mechanism and basis for specificity of transglutaminase-catalyzed epsilon-(gamma-glutamyl) lysine bond formation, in Advances in Enzymology and Related Areas in Molecular Biology (Meister A., ed). Wiley and Sons, New York.
    • (1983) Advances in Enzymology and Related Areas in Molecular Biology
    • Folk, J.E.1
  • 22
    • 13344266833 scopus 로고
    • The blood-brain barrier in infectious diseases. Its permeability to toxins in relation to their electrical charges
    • Friedemann V. and Elkeles A. (1934) The blood-brain barrier in infectious diseases. Its permeability to toxins in relation to their electrical charges. Lancet 226, 719-724.
    • (1934) Lancet , vol.226 , pp. 719-724
    • Friedemann, V.1    Elkeles, A.2
  • 23
    • 0022372211 scopus 로고
    • MIF-1 antagonizes warm-, but not cold-water stress-induced analgesia: Dissociation from immobility
    • Galina Z. H. and Kastin A. J. (1985) MIF-1 antagonizes warm-, but not cold-water stress-induced analgesia: dissociation from immobility. Peptides 6, 1109-1112.
    • (1985) Peptides , vol.6 , pp. 1109-1112
    • Galina, Z.H.1    Kastin, A.J.2
  • 24
    • 0028179387 scopus 로고
    • The di- and tripeptide transport protein of Lactococcus lactis - a new type of bacterial peptide transporter
    • Hagting A., Kunji E. R. S., Leenhouts K. J., Poolman B., and Konings W. N. (1994) The di- and tripeptide transport protein of Lactococcus lactis - a new type of bacterial peptide transporter. J. Biol. Chem. 269, 11391-11399.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11391-11399
    • Hagting, A.1    Kunji, E.R.S.2    Leenhouts, K.J.3    Poolman, B.4    Konings, W.N.5
  • 25
    • 0022365637 scopus 로고
    • Endothelial negative surface charge areas and blood-brain barrier function
    • Hardebo J. E. and Kåhrström J. (1985) Endothelial negative surface charge areas and blood-brain barrier function. Acta Physiol. Scand. 125, 495-499.
    • (1985) Acta Physiol. Scand. , vol.125 , pp. 495-499
    • Hardebo, J.E.1    Kåhrström, J.2
  • 26
    • 0023130270 scopus 로고
    • Differential opening of the brain endothelial barrier following neutralization of the endothelial luminal anionic charge in vitro
    • Hart M. N., Van Dyk L. F., Moore S. A., Shasby D. M., and Cancilla P. A. (1987) Differential opening of the brain endothelial barrier following neutralization of the endothelial luminal anionic charge in vitro. J. Neuropathol Exp. Neurol. 46, 141-153.
    • (1987) J. Neuropathol Exp. Neurol. , vol.46 , pp. 141-153
    • Hart, M.N.1    Van Dyk, L.F.2    Moore, S.A.3    Shasby, D.M.4    Cancilla, P.A.5
  • 27
    • 0014216749 scopus 로고
    • A method for the quantitative modification and estimation of carboxylic acid groups in proteins
    • Hoare D. G. and Koshland D. E. Jr. (1967) A method for the quantitative modification and estimation of carboxylic acid groups in proteins. J. Biol. Chem. 242, 2447-2453.
    • (1967) J. Biol. Chem. , vol.242 , pp. 2447-2453
    • Hoare, D.G.1    Koshland Jr., D.E.2
  • 28
    • 0025687503 scopus 로고
    • Isolation of polyamine transport-deficient mutants of Escherichia coli and cloning of the genes for polyamine transport proteins
    • Kashiwagi K., Hosokawa N., Furuchi T., Kobayashi H., Sasakawa C., Yoshikawa M., and Igarashi K. (1990) Isolation of polyamine transport-deficient mutants of Escherichia coli and cloning of the genes for polyamine transport proteins. J. Biol. Chem. 265, 20893-20897.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20893-20897
    • Kashiwagi, K.1    Hosokawa, N.2    Furuchi, T.3    Kobayashi, H.4    Sasakawa, C.5    Yoshikawa, M.6    Igarashi, K.7
  • 29
    • 0026583203 scopus 로고
    • Excretion of putrescine by the putrescine-ornithine antiporter encoded by the potE gene of Escherichia coli
    • Kashiwagi K., Miyamoto S., Suzuki F , Kobayashi H., and Igarashi K. (1992) Excretion of putrescine by the putrescine-ornithine antiporter encoded by the potE gene of Escherichia coli. Proc. Natl. Acad. Sci. USA 89, 4529-4533.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4529-4533
    • Kashiwagi, K.1    Miyamoto, S.2    Suzuki, F.3    Kobayashi, H.4    Igarashi, K.5
  • 30
    • 0023200855 scopus 로고
    • Absorptive-mediated endocytosis of cationized albumin and a β-endorphin-cationized albumin chimeric peptide by isolated brain capillaries
    • Kumagai A. K., Eisenberg J. B., and Pardridge W. M. (1987) Absorptive-mediated endocytosis of cationized albumin and a β-endorphin-cationized albumin chimeric peptide by isolated brain capillaries. J. Biol. Chem. 262, 15214-15219.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15214-15219
    • Kumagai, A.K.1    Eisenberg, J.B.2    Pardridge, W.M.3
  • 31
    • 0022575415 scopus 로고
    • Transglutaminase and neuronal differentiation
    • Maccioni R. B. and Seeds N. W. (1986) Transglutaminase and neuronal differentiation. Mol. Cell. Biochem. 69, 161-168.
    • (1986) Mol. Cell. Biochem. , vol.69 , pp. 161-168
    • Maccioni, R.B.1    Seeds, N.W.2
  • 32
    • 0020477470 scopus 로고
    • Succinylated copper, zinc superoxide dismutase. A novel approach to the problem of active subunits
    • Marmocchi F., Mavelli I., Rigo A., Stevanato R., Bossa F., and Rotilio G. (1982) Succinylated copper, zinc superoxide dismutase. A novel approach to the problem of active subunits. Biochemistry 21, 2853-2856.
    • (1982) Biochemistry , vol.21 , pp. 2853-2856
    • Marmocchi, F.1    Mavelli, I.2    Rigo, A.3    Stevanato, R.4    Bossa, F.5    Rotilio, G.6
  • 34
    • 0026772547 scopus 로고
    • Nucleotide sequence of the Escherichia coli cad operon: A system for neutralization of low extracellular pH
    • Meng S. Y. and Bennett G. N. (1992) Nucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pH. J. Bacteriol. 174, 2659-2669.
    • (1992) J. Bacteriol. , vol.174 , pp. 2659-2669
    • Meng, S.Y.1    Bennett, G.N.2
  • 35
    • 0019401255 scopus 로고
    • Endothelial surface charge: Blood-brain barrier opening to horseradish peroxidase induced by polycation protamine sulfate
    • Nagy Z., Peters H., and Hüttner I. (1981) Endothelial surface charge: blood-brain barrier opening to horseradish peroxidase induced by polycation protamine sulfate. Acta Neuropathol. 7, 7-9.
    • (1981) Acta Neuropathol. , vol.7 , pp. 7-9
    • Nagy, Z.1    Peters, H.2    Hüttner, I.3
  • 36
    • 0021077661 scopus 로고
    • Charge-related alterations of the cerebral endothelium
    • Nagy Z., Peters H., and Hüttner I. (1983) Charge-related alterations of the cerebral endothelium. Lab. Invest. 49, 662-671.
    • (1983) Lab. Invest. , vol.49 , pp. 662-671
    • Nagy, Z.1    Peters, H.2    Hüttner, I.3
  • 37
    • 0023781359 scopus 로고
    • Endothelial functional responses and increased vascular permeability induced by polycations
    • Needham L., Hellewell P. G., Williams T. J., and Gordon J. L. (1988) Endothelial functional responses and increased vascular permeability induced by polycations. Lab. Invest. 59, 538-548.
    • (1988) Lab. Invest. , vol.59 , pp. 538-548
    • Needham, L.1    Hellewell, P.G.2    Williams, T.J.3    Gordon, J.L.4
  • 39
    • 0025223675 scopus 로고
    • Evaluation of cationized rat albumin as a potential blood-brain barrier drug transport vector
    • Pardridge W. M., Triguero D., Buciak J., and Yang J. (1990) Evaluation of cationized rat albumin as a potential blood-brain barrier drug transport vector. J. Pharmacol. Exp. Ther. 255, 893-899.
    • (1990) J. Pharmacol. Exp. Ther. , vol.255 , pp. 893-899
    • Pardridge, W.M.1    Triguero, D.2    Buciak, J.3    Yang, J.4
  • 40
    • 0019570951 scopus 로고
    • Identification of hypusine, an unusual amino acid, in a protein from human lymphocytes and of spermidine as its biosynthetic precursor
    • Park M. H., Cooper H. L., and Folk J. E. (1981) Identification of hypusine, an unusual amino acid, in a protein from human lymphocytes and of spermidine as its biosynthetic precursor. Proc. Natl. Acad. Sci. USA 78, 2869-2873.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 2869-2873
    • Park, M.H.1    Cooper, H.L.2    Folk, J.E.3
  • 41
    • 0020490856 scopus 로고
    • The biosynthesis of protein-bound hypusine (N epsilon- [4-amino-2-hydroxybutyl]lysine). Lysine as the amino acid precursor and the intermediate role of deoxyhypusine (N epsilon-[4-aminobutyl]lysine)
    • Park M. H., Cooper H. L., and Folk J. E. (1982) The biosynthesis of protein-bound hypusine (N epsilon- [4-amino-2-hydroxybutyl]lysine). Lysine as the amino acid precursor and the intermediate role of deoxyhypusine (N epsilon-[4-aminobutyl]lysine). J. Biol. Chem. 257, 7217-7222.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7217-7222
    • Park, M.H.1    Cooper, H.L.2    Folk, J.E.3
  • 43
    • 0022450919 scopus 로고
    • Recent advances in the biochemistry of polyamines in eukaryotes
    • Pegg A. E. (1986) Recent advances in the biochemistry of polyamines in eukaryotes. Biochem. J. 234, 249-262.
    • (1986) Biochem. J. , vol.234 , pp. 249-262
    • Pegg, A.E.1
  • 44
    • 0028115836 scopus 로고
    • Isolation and characterization of a Saccharomyces cerevisiae peptide transport gene
    • Perry J. R., Basrai M. A., Steiner H. Y., Naider F., and Becker J. M. (1994) Isolation and characterization of a Saccharomyces cerevisiae peptide transport gene. Mol. Cell. Biol. 14, 104-115.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 104-115
    • Perry, J.R.1    Basrai, M.A.2    Steiner, H.Y.3    Naider, F.4    Becker, J.M.5
  • 45
    • 0023849375 scopus 로고
    • Gamma-glutamylamine derivatives in isolated rat hepatocyte proteins
    • Piacentini M. and Beninati S. (1988) Gamma-glutamylamine derivatives in isolated rat hepatocyte proteins. Biochem. J. 249, 813-817.
    • (1988) Biochem. J. , vol.249 , pp. 813-817
    • Piacentini, M.1    Beninati, S.2
  • 46
    • 0023838641 scopus 로고
    • Free and protein-conjugated polyamines in mouse epidermal cells
    • Piacentini M., Martinet N., Beninati S., and Folk J. E. (1988) Free and protein-conjugated polyamines in mouse epidermal cells. J. Biol. Chem. 263, 3790-3794.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3790-3794
    • Piacentini, M.1    Martinet, N.2    Beninati, S.3    Folk, J.E.4
  • 47
    • 0019487684 scopus 로고
    • Glycoprotein molecular weight estimation using SDS-pore gradient electrophoresis: Comparison of TRIS-glycine and TRIS-borate-EDTA buffer systems
    • Poduslo J. F. (1981) Glycoprotein molecular weight estimation using SDS-pore gradient electrophoresis: comparison of TRIS-glycine and TRIS-borate-EDTA buffer systems. Anal. Biochem. 114, 131-139.
    • (1981) Anal. Biochem. , vol.114 , pp. 131-139
    • Poduslo, J.F.1
  • 48
    • 0026545543 scopus 로고
    • Increased permeability across the blood-nerve barrier of albumin glycated in vitro and in vivo from patients with diabetic polyneuropathy
    • Poduslo J. F. and Curran G. L. (1992) Increased permeability across the blood-nerve barrier of albumin glycated in vitro and in vivo from patients with diabetic polyneuropathy. Proc. Natl. Acad Sci. USA 89, 2218-2222.
    • (1992) Proc. Natl. Acad Sci. USA , vol.89 , pp. 2218-2222
    • Poduslo, J.F.1    Curran, G.L.2
  • 49
    • 0028273935 scopus 로고
    • Glycation increases the permeability of proteins across the blood-nerve and blood-brain barriers
    • Poduslo J. F. and Curran G. L. (1994) Glycation increases the permeability of proteins across the blood-nerve and blood-brain barriers. Mol. Brain Res. 23, 157-162.
    • (1994) Mol. Brain Res. , vol.23 , pp. 157-162
    • Poduslo, J.F.1    Curran, G.L.2
  • 50
    • 0020379124 scopus 로고
    • Altered blood nerve barrier in experimental lead neuropathy assessed by changes in endoneurial albumin concentration
    • Poduslo J. F., Low P. A., Windebank A. J., Dyck P. J., Berg C. T., and Schmelzer J. D. (1982) Altered blood nerve barrier in experimental lead neuropathy assessed by changes in endoneurial albumin concentration. J. Neurosci. 2, 1507-1514.
    • (1982) J. Neurosci. , vol.2 , pp. 1507-1514
    • Poduslo, J.F.1    Low, P.A.2    Windebank, A.J.3    Dyck, P.J.4    Berg, C.T.5    Schmelzer, J.D.6
  • 51
    • 0024040627 scopus 로고
    • Increase in albumin, IgG, and IgM blood-nerve barrier indices in human diabetic neuropathy
    • Poduslo J. F., Curran G. L., and Dyck P. J. (1988) Increase in albumin, IgG, and IgM blood-nerve barrier indices in human diabetic neuropathy. Proc. Natl. Acad. Sci. USA 85, 4879-4883.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4879-4883
    • Poduslo, J.F.1    Curran, G.L.2    Dyck, P.J.3
  • 52
    • 0028301348 scopus 로고
    • Macromolecular permeability across the blood-nerve and blood-brain barriers
    • Poduslo J. F., Curran G. L., and Berg C. T. (1994) Macromolecular permeability across the blood-nerve and blood-brain barriers. Proc. Natl. Acad. Sci. USA 91, 5705-5709.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5705-5709
    • Poduslo, J.F.1    Curran, G.L.2    Berg, C.T.3
  • 54
    • 0021333744 scopus 로고
    • Characterization of the polyamine transport system in mouse neuroblastoma cells
    • Rinehart C. A. Jr. and Chen K. Y. (1984) Characterization of the polyamine transport system in mouse neuroblastoma cells. J. Biol. Chem. 259, 4750-4756.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4750-4756
    • Rinehart Jr., C.A.1    Chen, K.Y.2
  • 55
    • 0025170587 scopus 로고
    • Permeability of neutral vs. anionic dextrans in cultured brain microvascular endothelium
    • Sahagun G., Moore S. A., and Hart M. N. (1990) Permeability of neutral vs. anionic dextrans in cultured brain microvascular endothelium. Am. J. Physiol. 259, H162-H166.
    • (1990) Am. J. Physiol. , vol.259
    • Sahagun, G.1    Moore, S.A.2    Hart, M.N.3
  • 56
    • 0000831917 scopus 로고
    • Brain transglutaminase: In vitro crosslinking of human neurofilament proteins into insoluble polymers
    • Selkoe D. J., Abraham C., and Ihara Y. (1982) Brain transglutaminase: in vitro crosslinking of human neurofilament proteins into insoluble polymers. Proc. Natl. Acad. Sci. USA 79, 6070-6074
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6070-6074
    • Selkoe, D.J.1    Abraham, C.2    Ihara, Y.3
  • 58
    • 0024674746 scopus 로고
    • Permeability and mechanism of albumin, cationized albumin, and glycosylated albumin transcellular transport across monolayers of cultured bovine brain capillary endothelial cells
    • Smith K R. and Borchardt R. T. (1989) Permeability and mechanism of albumin, cationized albumin, and glycosylated albumin transcellular transport across monolayers of cultured bovine brain capillary endothelial cells. Pharm. Res. 6, 466-473.
    • (1989) Pharm. Res. , vol.6 , pp. 466-473
    • Smith, K.R.1    Borchardt, R.T.2
  • 63
    • 0026686432 scopus 로고
    • Evidence that spermine, spermidine, and putrescine are transported electrophoretically in mitochondria by a specific polyamine uniporter
    • Toninello A., Via L. D., Siliprandi D., and Garlid K. D. (1992) Evidence that spermine, spermidine, and putrescine are transported electrophoretically in mitochondria by a specific polyamine uniporter. J. Biol. Chem. 267, 18393-18397.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18393-18397
    • Toninello, A.1    Via, L.D.2    Siliprandi, D.3    Garlid, K.D.4
  • 64
    • 0001120209 scopus 로고
    • Blood-brain barrier transport of cationized immunoglobulin G: Enhanced delivery compared to native protein
    • Triguero D., Buciak J. B., Yang J., and Pardridge W. M. (1989) Blood-brain barrier transport of cationized immunoglobulin G: enhanced delivery compared to native protein. Proc. Natl. Acad. Sci. USA 86, 4761-4765.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4761-4765
    • Triguero, D.1    Buciak, J.B.2    Yang, J.3    Pardridge, W.M.4
  • 65
    • 0027526320 scopus 로고
    • The herbicide sensitivity gene CHL1 of Arabidopsis encodes a nitrate-indueible nitrate transporter
    • Tsay Y. F., Schroeder J. I., Feldmann K. A., and Crawford N. M. (1993) The herbicide sensitivity gene CHL1 of Arabidopsis encodes a nitrate-indueible nitrate transporter. Cell 72, 705-713.
    • (1993) Cell , vol.72 , pp. 705-713
    • Tsay, Y.F.1    Schroeder, J.I.2    Feldmann, K.A.3    Crawford, N.M.4
  • 68
    • 0026625767 scopus 로고
    • Enhanced permeabilities of cationized-bovine serum albumins at the blood-nerve and blood-brain barriers in awake rats
    • Wadhwani K. C., Shimon-Hophy M., and Rapoport S. I. (1992) Enhanced permeabilities of cationized-bovine serum albumins at the blood-nerve and blood-brain barriers in awake rats. J. Neurosci. Res. 32, 407-414.
    • (1992) J. Neurosci. Res. , vol.32 , pp. 407-414
    • Wadhwani, K.C.1    Shimon-Hophy, M.2    Rapoport, S.I.3
  • 70
    • 0019271329 scopus 로고
    • Transglutaminase-mediated covalent attachment of polyamines to proteins: Mechanisms and potential physiological significance
    • Williams-Ashman H. G. and Canellakis Z. N. (1980) Transglutaminase-mediated covalent attachment of polyamines to proteins: mechanisms and potential physiological significance. Physiol. Chem. Phys. Med. NMR 12, 457-472.
    • (1980) Physiol. Chem. Phys. Med. NMR , vol.12 , pp. 457-472
    • Williams-Ashman, H.G.1    Canellakis, Z.N.2
  • 71
    • 0025213058 scopus 로고
    • A saturable mechanism for transport of immunoglobulin G across the blood-brain barrier of the guinea pig
    • Zlokovic B. V., Skundric D. S., Segal M. B., Lipovac M. N., Mackic J. B., and Davson H. (1990) A saturable mechanism for transport of immunoglobulin G across the blood-brain barrier of the guinea pig. Exp. Neurol. 107, 263-270.
    • (1990) Exp. Neurol. , vol.107 , pp. 263-270
    • Zlokovic, B.V.1    Skundric, D.S.2    Segal, M.B.3    Lipovac, M.N.4    Mackic, J.B.5    Davson, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.