Protective effects of L- and D-carnosine on alpha-crystallin amyloid fibril formation: implications for cataract disease (352 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2009 Jul 14; 48(27): 6522-6531.
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Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.226, 5-year impact factor: 3.253
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-67650045638&partnerID=40&md5=40601e669c1c77b3a327a331eec94f2a
Keywords: Amyloid Fibril, Amyloid Fibril Formation, Carnosine, Chaperone Activity, Crystallin, Denaturing Conditions, Dipeptide, Fibrillar Structures, Heat Stress, In-Vitro, Inhibitory Effect, Lens Proteins, Lens Transparency, Polypeptide Chain, Protective Effects, Scanning Force Microscopy, Self-Assemble, Senile Cataract, Structural Elements, Thioflavin T, Amines, Optical Instruments, Restoration, Scanning Tunneling Microscopy, Sugar (sucrose), Glycoproteins, Alpha Crystallin, Beta Crystallin, Animal Tissue, Article, Controlled Study, Enantiomer, Female, Nonhuman, Organ Culture, Priority Journal, Protein Denaturation, Turbidimetry, Alpha-Crystallins, Calorimetry, Differential Scanning, Cattle, Circular Dichroism, Atomic Force, Molecular Chaperones, Organ Culture Techniques, Sprague-Dawley, Spectrometry, Fluorescence, Spectrophotometry, Ultraviolet, Stereoisomerism, Bovinae, Rattus,
Affiliations:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging (IBB), CNR, 95125 Catania, Italy
Dipartimento di Chimica Fisica F. Accascina, Università di Palermo, 90128 Palermo, Italy
Department of Chemical Sciences, University of Catania, 95125 Catania, Italy
National Institute of Biostructures and Biosystems, 95125 Catania, Italy
References:
Bloemendal, H., (1981) Molecular and Cellular Biology of the Eye Lens, , Wiley, New Yor
Horwitz, J., α-Crystallin can function as a molecular chaperone (1992) Proc. Natl. Acad. Sci. U.S.A, 89, pp. 10449-10453
Harding, J.J., Viewing molecular mechanisms of ageing through a lens (2002) Ageing Res. Rev, 1, pp. 465-479
Derham, B.K., Harding, J.J., Effects of modifications of α-crystallin on its chaperone and other properties (2002) Biochem. J, 364, pp. 711-717
Spector, A., Li, L.K., Augusteyn, R.C., Schneider, A., Freund, T., α-Crystallin. The isolation and characterization of distinct macromolecular fractions (1971) Biochem. J, 124, pp. 337-343
Liang, J.J.-N., Akhtar, N.J., Human lens high-molecular- weight α-crystallin aggregates (2000) Biochem. Biophys. Res. Commun, 275, pp. 354-359
Fujii, N., Awakura, M., Takemoto, L., Inomata, M., Tarata, T., Fujii, N., Saito, T., Characterization of αA-crystallin from high molecular weight aggregates in the normal human lens (2003) Mol. Vision, 9, pp. 315-322
Sunde, M., Blake, C.C., From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation (1998) Q. Rev. Biophys, 31, pp. 1-39
Van Boekel, M.A., Hoogakker, S.E., Harding, J.J., De Jong, W.W., The infuence of some post-translational modifications on the chaperone-like activity of α-crystallin (1996) Ophthalmic Res, 28, pp. 32-38
Pande, A., Pande, J., Asherie, N., Lomakin, A., Ogun, O., King, J.A., Lubsen, N.H., Benedek, G.B., Crystal cataracts: Human genetic cataracts caused by protein crystallization (2000) Proc. Natl. Acad. Sci. U.S.A, 97, pp. 1993-1998
Harding, J.J., Cataract, Alzheimer's disease, and other conformational diseases (1998) Curr. Opin. Ophthalmol, 9, pp. 10-13
Meehan, S., Berry, Y., Luisi, B., Dobson, C.M., Carver, J.A., MacPhee, C.E., Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation (2004) J. Biol. Chem, 279, pp. 3413-3419
Meehan, S., Knowles, T.P.J., Baldwin, A.J., Smith, J.F., Squires, A.M., Clements, P., Treweek, T.M., Carver, J.A., Characterisation of amyloid fibril formation by small heatshock chaperone proteins human αA-, αB- and R120G αB-crystallin (2007) J. Mol. Biol, 372, pp. 470-484
Tanaka, M., Machida, Y., Niu, S., Ikeda, T., Jana, N.R., Doi, H., Kurosawa, M., Nukina, N., Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease (2004) Nat. Med, 10, pp. 148-154
Arora, A., Ha, C., Park, C.B., Inhibition of insulin amyloid formation by small stress molecules (2004) FEBS Lett, 564, pp. 121-125
Akashi, K., Miyake, C., Yokota, A., Citrulline, a novel compatible solute in drought-tolerant wild watermelon leaves, is an efficient hydroxyl radical scavenger (2001) FEBS Lett, 508, pp. 438-442
Yan, H., Harding, J.J., Carnosine inhibits modifications and decreased molecular chaperone activity of lens α-crystallin induced by ribose and fructose 6-phosphate (2006) Mol. Vision, 12, pp. 205-214
Attanasio, F., Cascio, C., Fisichella, S., Nicoletti, V.G., Pignataro, B., Savarino, A., Rizzarelli, E., Trehalose effects on α-crystallin aggregates (2007) Biochem. Biophys. Res. Commun, 354, pp. 899-905
McFarland, G.A., Holliday, R., Retardation of the senescence of cultured human diploid fibroblasts by carnosine (1994) Exp. Cell Res, 212, pp. 167-175
Gariballa, S.E., Sinclair, A.J., Carnosine: Physiological properties and therapeutic potential (2000) Age Ageing, 29, pp. 207-210
Hipkiss, A.R., Michaelis, J., Syrris, P., Non-enzymatic glycosylation of the dipeptide L-carnosine, a potential anti-protein-cross-linking agent (1995) FEBS Lett, 371, pp. 81-85
Brownson, C., Hipkiss, A.R., Carnosine reacts with a glycated protein (2000) Free Radical Biol. Med, 28, pp. 1564-1570
Seidler, N.W., Yeargans, G.S., Morgan, T.G., Carnosine disaggregates glycated α-crystallin: An in vitro study (2004) Arch. Biochem. Biophys, 427, pp. 110-115
Kang, J.H., Kim, K.S., Choi, S.Y., Kwon, H.Y., Won, M.H., Kang, T.C., Protective effects of carnosine, homocarnosine and anserine against peroxyl radical-mediated Cu,Zn-superoxide dismutase modification (2002) Biochim. Biophys. Acta, 1570, pp. 89-96
Hipkiss, A.R., Presto, J.E., Himswoth, D.T., Worthington, V.C., Abbot, N.J., Protective effects of carnosine against malondialdehyde- induced toxicity towards cultured rat brain endothelial cells (1997) Neurosci. Lett, 238, pp. 135-138
Babizhayev, M.A., Guiotto, A., Kasus-Jacobi, A., N-Acetylcarnosine and histidyl-hydrazide are potent agents for multitargeted ophthalmic therapy of senile cataracts and diabetic ocular complications (2009) J. Drug Targeting, 17, pp. 36-63
Babizhayev, M.A., Deyev, A.I., Yermakova, V.N., Remenshchikov, V.V., Bours, J., Revival of lens transparency with N-acetylcarnosine (2006) Curr. Drug Ther, 1, pp. 91-116
Boldyrev, A., Bulygina, E., Leinsoo, T., Tsubone, I.P.S., Abe, H., Protection of neuronal cells against reactive oxygen species by carnosine and related compounds (2000) Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol, 127, pp. 443-446
Aldini, G, Canevotti, R, and Negrisoli, G. Compositions containing D-carnosine. Patent WO 2005/120543Pignataro, B., Chi, L.F., Gao, S., Anczykowski, B., Niemeyer, C.M., Adler, M., Blohm, D., Fuchs, H., Dynamic scanning force microscopy study of self-assembled DNA-protein oligomers (2002) Appl. Phys. A: Mater. Sci. Process, 74, pp. 447-452
Pignataro, B., Sardone, L., Marletta, G., Dynamic scanning force microscopy investigation of nanostructured spiral-like domains in Langmuir-Blodgett monolayers (2003) Nanotechnology, 14, pp. 245-249
García, J., Martinez, L., Briceño-Valero, J.M., Schilling, C.H., Dimensional Metrology of Nanometric Spherical Particles using AFM: I. Model Development (1997) Probe Microsc, 1, pp. 107-116
Vesenka, J., Tang, C.L., Guthold, M., Keller, D., Delaine, E., Bustamante, C., A substrate preparation for imaging biomolecules with the scanning force microscope (1992) Ultramicroscopy, 42-44, pp. 1243-1249
Naiki, H., Higuchi, K., Hosokawa, M., Takeda, T., Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T (1989) Anal. Biochem, 177, pp. 244-249
LeVine, H.III (1999) Quantification of β-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309, 274-284Burgio, M.R., Bennett, P.M., Koretz, J.F., Heat induced quaternary transitions in hetero- and homo-polymers of α-crystallin (2001) Mol. Vision, 7, pp. 228-233
Blackley, H.K., Sanders, G.H., Davies, M.C., Roberts, C.J., Tendler, S.J., Wilkinson, M.J., In-situ atomic force microscopy study of β-amyloid fibrillization (2000) J. Mol. Biol, 298, pp. 833-840
Lee, J.C., Timasheff, S.N., Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride (1974) Biochemistry, 13, pp. 251-265
Makhatadze, G.I., Privalov, P.L., Protein interactions with urea and guanidinium chloride. A calorimetric study (1992) J. Mol. Biol, 226, pp. 491-505
Horwitz, J., Some properties of the low molecular weight α-crystallin from normal human lens: Comparison with bovine lens (1976) Exp. Eye Res, 23, pp. 471-481
Horwitz, J., Strickland, E.H., Billups, C., Analysis of the vibrational structure in the near-ultraviolet circular dichroism and absorption spectra of phenylalanine and its derivatives (1969) J. Am. Chem. Soc, 91, pp. 184-190
Sun, Y., MacRae, T.H., The small heat shock proteins and their role in human disease (2005) FEBS J, 272, pp. 2613-2627
Heath, E., Carver, J.A., The effect of small molecules in modulating the chaperone activity of αB-crystallin against ordered and disordered protein aggregation (2008) FEBS J, 275, pp. 935-947
Fändrich, M., Forge, V., Buder, K., Kittler, M., Dobson, C.M., Diekmann, S., Myoglobin forms amyloid fibrils by association of unfolded polipeptide segments (2005) Proc. Natl. Acad. Sci. U.S.A, 100, pp. 15463-15468
Nicoletti, V.G., Santoro, A.M., Grasso, G., Vagliasindi, L.I., Giuffrida, M.L., Cuppari, C., Purrello, V.S., Rizzarelli, E., Carnosine interaction with nitric oxide and astroglial cell protection (2007) J. Neurosci. Res, 85, pp. 2239-2245
Calabrese, V., Colombrita, C., Guagliano, E., Sapienza, M., Ravagna, A., Cardile, V., Scapagnini, G., Rizzarelli, E., Protective Effect of Carnosine During Nitrosative Stress in Astroglial Cell Cultures (2005) Neurochem. Res, 30, pp. 797-807
Inomata, M., Hayashi, M., Shumiya, S., Kawashima, S., Ito, Y., Involvement of inducible nitric oxide synthase in cataract formation in Shumiya cataract rat (SCR) (2001) Curr. Eye Res, 23, pp. 307-311
Nagai, N., Liu, Y., Fukuhata, T., Ito, Y., Inhibitors of Inducible Nitric Oxide Synthase Prevent Damage to Human Lens Epithelial Cells Induced by Interferon-γ and Lipopolysaccharide (2006) Biol. Pharm. Bull, 29, pp. 2077-2081
Babizhayev, M.A., Yermakova, V.N., Sakina, N.L., Evstigneeva, R.P., Rozhkova, E.A., Zheltukhina, G.A., Nα-Acetylcarnosine is a prodrug of L-carnosine in ophthalmic application as antioxidant (1996) Clin. Chim. Acta, 254, pp. 1-21
Jay, J., Miller, D. J., Morrison, J. D., and O'Dowd, J. J. (1990) Histidyl derivates in rabbit lens and their diminution in human cataract. Meeting Abstracts of the Journal of Physiology of London , Proceedings Supplement, 420, p 155Stuerenburg, H.J., The roles of carnosine in aging of skeletal muscle and in neuromuscular diseases (2000) Biochemistry (Moscow, Russ. Fed.), 65, pp. 862-865
Horwitz, J., a-Crystallin can function as a molecular chaperone (1992) Proc. Natl. Acad. Sci. U.S.A, 89, pp. 10449-10453
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2009 Jul 14; 48(27): 6522-6531.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.226, 5-year impact factor: 3.253
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-67650045638&partnerID=40&md5=40601e669c1c77b3a327a331eec94f2a
Keywords: Amyloid Fibril, Amyloid Fibril Formation, Carnosine, Chaperone Activity, Crystallin, Denaturing Conditions, Dipeptide, Fibrillar Structures, Heat Stress, In-Vitro, Inhibitory Effect, Lens Proteins, Lens Transparency, Polypeptide Chain, Protective Effects, Scanning Force Microscopy, Self-Assemble, Senile Cataract, Structural Elements, Thioflavin T, Amines, Optical Instruments, Restoration, Scanning Tunneling Microscopy, Sugar (sucrose), Glycoproteins, Alpha Crystallin, Beta Crystallin, Animal Tissue, Article, Controlled Study, Enantiomer, Female, Nonhuman, Organ Culture, Priority Journal, Protein Denaturation, Turbidimetry, Alpha-Crystallins, Calorimetry, Differential Scanning, Cattle, Circular Dichroism, Atomic Force, Molecular Chaperones, Organ Culture Techniques, Sprague-Dawley, Spectrometry, Fluorescence, Spectrophotometry, Ultraviolet, Stereoisomerism, Bovinae, Rattus,
Affiliations:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging (IBB), CNR, 95125 Catania, Italy
Dipartimento di Chimica Fisica F. Accascina, Università di Palermo, 90128 Palermo, Italy
Department of Chemical Sciences, University of Catania, 95125 Catania, Italy
National Institute of Biostructures and Biosystems, 95125 Catania, Italy
References:
Bloemendal, H., (1981) Molecular and Cellular Biology of the Eye Lens, , Wiley, New Yor
Horwitz, J., α-Crystallin can function as a molecular chaperone (1992) Proc. Natl. Acad. Sci. U.S.A, 89, pp. 10449-10453
Harding, J.J., Viewing molecular mechanisms of ageing through a lens (2002) Ageing Res. Rev, 1, pp. 465-479
Derham, B.K., Harding, J.J., Effects of modifications of α-crystallin on its chaperone and other properties (2002) Biochem. J, 364, pp. 711-717
Spector, A., Li, L.K., Augusteyn, R.C., Schneider, A., Freund, T., α-Crystallin. The isolation and characterization of distinct macromolecular fractions (1971) Biochem. J, 124, pp. 337-343
Liang, J.J.-N., Akhtar, N.J., Human lens high-molecular- weight α-crystallin aggregates (2000) Biochem. Biophys. Res. Commun, 275, pp. 354-359
Fujii, N., Awakura, M., Takemoto, L., Inomata, M., Tarata, T., Fujii, N., Saito, T., Characterization of αA-crystallin from high molecular weight aggregates in the normal human lens (2003) Mol. Vision, 9, pp. 315-322
Sunde, M., Blake, C.C., From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation (1998) Q. Rev. Biophys, 31, pp. 1-39
Van Boekel, M.A., Hoogakker, S.E., Harding, J.J., De Jong, W.W., The infuence of some post-translational modifications on the chaperone-like activity of α-crystallin (1996) Ophthalmic Res, 28, pp. 32-38
Pande, A., Pande, J., Asherie, N., Lomakin, A., Ogun, O., King, J.A., Lubsen, N.H., Benedek, G.B., Crystal cataracts: Human genetic cataracts caused by protein crystallization (2000) Proc. Natl. Acad. Sci. U.S.A, 97, pp. 1993-1998
Harding, J.J., Cataract, Alzheimer's disease, and other conformational diseases (1998) Curr. Opin. Ophthalmol, 9, pp. 10-13
Meehan, S., Berry, Y., Luisi, B., Dobson, C.M., Carver, J.A., MacPhee, C.E., Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation (2004) J. Biol. Chem, 279, pp. 3413-3419
Meehan, S., Knowles, T.P.J., Baldwin, A.J., Smith, J.F., Squires, A.M., Clements, P., Treweek, T.M., Carver, J.A., Characterisation of amyloid fibril formation by small heatshock chaperone proteins human αA-, αB- and R120G αB-crystallin (2007) J. Mol. Biol, 372, pp. 470-484
Tanaka, M., Machida, Y., Niu, S., Ikeda, T., Jana, N.R., Doi, H., Kurosawa, M., Nukina, N., Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease (2004) Nat. Med, 10, pp. 148-154
Arora, A., Ha, C., Park, C.B., Inhibition of insulin amyloid formation by small stress molecules (2004) FEBS Lett, 564, pp. 121-125
Akashi, K., Miyake, C., Yokota, A., Citrulline, a novel compatible solute in drought-tolerant wild watermelon leaves, is an efficient hydroxyl radical scavenger (2001) FEBS Lett, 508, pp. 438-442
Yan, H., Harding, J.J., Carnosine inhibits modifications and decreased molecular chaperone activity of lens α-crystallin induced by ribose and fructose 6-phosphate (2006) Mol. Vision, 12, pp. 205-214
Attanasio, F., Cascio, C., Fisichella, S., Nicoletti, V.G., Pignataro, B., Savarino, A., Rizzarelli, E., Trehalose effects on α-crystallin aggregates (2007) Biochem. Biophys. Res. Commun, 354, pp. 899-905
McFarland, G.A., Holliday, R., Retardation of the senescence of cultured human diploid fibroblasts by carnosine (1994) Exp. Cell Res, 212, pp. 167-175
Gariballa, S.E., Sinclair, A.J., Carnosine: Physiological properties and therapeutic potential (2000) Age Ageing, 29, pp. 207-210
Hipkiss, A.R., Michaelis, J., Syrris, P., Non-enzymatic glycosylation of the dipeptide L-carnosine, a potential anti-protein-cross-linking agent (1995) FEBS Lett, 371, pp. 81-85
Brownson, C., Hipkiss, A.R., Carnosine reacts with a glycated protein (2000) Free Radical Biol. Med, 28, pp. 1564-1570
Seidler, N.W., Yeargans, G.S., Morgan, T.G., Carnosine disaggregates glycated α-crystallin: An in vitro study (2004) Arch. Biochem. Biophys, 427, pp. 110-115
Kang, J.H., Kim, K.S., Choi, S.Y., Kwon, H.Y., Won, M.H., Kang, T.C., Protective effects of carnosine, homocarnosine and anserine against peroxyl radical-mediated Cu,Zn-superoxide dismutase modification (2002) Biochim. Biophys. Acta, 1570, pp. 89-96
Hipkiss, A.R., Presto, J.E., Himswoth, D.T., Worthington, V.C., Abbot, N.J., Protective effects of carnosine against malondialdehyde- induced toxicity towards cultured rat brain endothelial cells (1997) Neurosci. Lett, 238, pp. 135-138
Babizhayev, M.A., Guiotto, A., Kasus-Jacobi, A., N-Acetylcarnosine and histidyl-hydrazide are potent agents for multitargeted ophthalmic therapy of senile cataracts and diabetic ocular complications (2009) J. Drug Targeting, 17, pp. 36-63
Babizhayev, M.A., Deyev, A.I., Yermakova, V.N., Remenshchikov, V.V., Bours, J., Revival of lens transparency with N-acetylcarnosine (2006) Curr. Drug Ther, 1, pp. 91-116
Boldyrev, A., Bulygina, E., Leinsoo, T., Tsubone, I.P.S., Abe, H., Protection of neuronal cells against reactive oxygen species by carnosine and related compounds (2000) Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol, 127, pp. 443-446
Aldini, G, Canevotti, R, and Negrisoli, G. Compositions containing D-carnosine. Patent WO 2005/120543Pignataro, B., Chi, L.F., Gao, S., Anczykowski, B., Niemeyer, C.M., Adler, M., Blohm, D., Fuchs, H., Dynamic scanning force microscopy study of self-assembled DNA-protein oligomers (2002) Appl. Phys. A: Mater. Sci. Process, 74, pp. 447-452
Pignataro, B., Sardone, L., Marletta, G., Dynamic scanning force microscopy investigation of nanostructured spiral-like domains in Langmuir-Blodgett monolayers (2003) Nanotechnology, 14, pp. 245-249
García, J., Martinez, L., Briceño-Valero, J.M., Schilling, C.H., Dimensional Metrology of Nanometric Spherical Particles using AFM: I. Model Development (1997) Probe Microsc, 1, pp. 107-116
Vesenka, J., Tang, C.L., Guthold, M., Keller, D., Delaine, E., Bustamante, C., A substrate preparation for imaging biomolecules with the scanning force microscope (1992) Ultramicroscopy, 42-44, pp. 1243-1249
Naiki, H., Higuchi, K., Hosokawa, M., Takeda, T., Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T (1989) Anal. Biochem, 177, pp. 244-249
LeVine, H.III (1999) Quantification of β-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309, 274-284Burgio, M.R., Bennett, P.M., Koretz, J.F., Heat induced quaternary transitions in hetero- and homo-polymers of α-crystallin (2001) Mol. Vision, 7, pp. 228-233
Blackley, H.K., Sanders, G.H., Davies, M.C., Roberts, C.J., Tendler, S.J., Wilkinson, M.J., In-situ atomic force microscopy study of β-amyloid fibrillization (2000) J. Mol. Biol, 298, pp. 833-840
Lee, J.C., Timasheff, S.N., Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride (1974) Biochemistry, 13, pp. 251-265
Makhatadze, G.I., Privalov, P.L., Protein interactions with urea and guanidinium chloride. A calorimetric study (1992) J. Mol. Biol, 226, pp. 491-505
Horwitz, J., Some properties of the low molecular weight α-crystallin from normal human lens: Comparison with bovine lens (1976) Exp. Eye Res, 23, pp. 471-481
Horwitz, J., Strickland, E.H., Billups, C., Analysis of the vibrational structure in the near-ultraviolet circular dichroism and absorption spectra of phenylalanine and its derivatives (1969) J. Am. Chem. Soc, 91, pp. 184-190
Sun, Y., MacRae, T.H., The small heat shock proteins and their role in human disease (2005) FEBS J, 272, pp. 2613-2627
Heath, E., Carver, J.A., The effect of small molecules in modulating the chaperone activity of αB-crystallin against ordered and disordered protein aggregation (2008) FEBS J, 275, pp. 935-947
Fändrich, M., Forge, V., Buder, K., Kittler, M., Dobson, C.M., Diekmann, S., Myoglobin forms amyloid fibrils by association of unfolded polipeptide segments (2005) Proc. Natl. Acad. Sci. U.S.A, 100, pp. 15463-15468
Nicoletti, V.G., Santoro, A.M., Grasso, G., Vagliasindi, L.I., Giuffrida, M.L., Cuppari, C., Purrello, V.S., Rizzarelli, E., Carnosine interaction with nitric oxide and astroglial cell protection (2007) J. Neurosci. Res, 85, pp. 2239-2245
Calabrese, V., Colombrita, C., Guagliano, E., Sapienza, M., Ravagna, A., Cardile, V., Scapagnini, G., Rizzarelli, E., Protective Effect of Carnosine During Nitrosative Stress in Astroglial Cell Cultures (2005) Neurochem. Res, 30, pp. 797-807
Inomata, M., Hayashi, M., Shumiya, S., Kawashima, S., Ito, Y., Involvement of inducible nitric oxide synthase in cataract formation in Shumiya cataract rat (SCR) (2001) Curr. Eye Res, 23, pp. 307-311
Nagai, N., Liu, Y., Fukuhata, T., Ito, Y., Inhibitors of Inducible Nitric Oxide Synthase Prevent Damage to Human Lens Epithelial Cells Induced by Interferon-γ and Lipopolysaccharide (2006) Biol. Pharm. Bull, 29, pp. 2077-2081
Babizhayev, M.A., Yermakova, V.N., Sakina, N.L., Evstigneeva, R.P., Rozhkova, E.A., Zheltukhina, G.A., Nα-Acetylcarnosine is a prodrug of L-carnosine in ophthalmic application as antioxidant (1996) Clin. Chim. Acta, 254, pp. 1-21
Jay, J., Miller, D. J., Morrison, J. D., and O'Dowd, J. J. (1990) Histidyl derivates in rabbit lens and their diminution in human cataract. Meeting Abstracts of the Journal of Physiology of London , Proceedings Supplement, 420, p 155Stuerenburg, H.J., The roles of carnosine in aging of skeletal muscle and in neuromuscular diseases (2000) Biochemistry (Moscow, Russ. Fed.), 65, pp. 862-865
Horwitz, J., a-Crystallin can function as a molecular chaperone (1992) Proc. Natl. Acad. Sci. U.S.A, 89, pp. 10449-10453
Protective effects of L- and D-carnosine on alpha-crystallin amyloid fibril formation: implications for cataract disease
Mildly denaturing conditions induce bovine α-crystallin, the major structural lens protein, to self-assemble into fibrillar structures in vitro. The natural dipeptide L-carnosine has been shown to have potential protective and therapeutic significance in many diseases. Carnosine derivatives have been proposed as potent agents for ophthalmic therapies of senile cataracts and diabetic ocular complications. Here we report the inhibitory effect induced by the peptide (L- and D-enantiomeric form) on α-crystallin fibrillation and the almost complete restoration of the chaperone activity lost after denaturant and/or heat stress. Scanning force microscopy (SFM), thioflavin T, and a turbidimetry assay have been used to determine the morphology of α-crystallin aggregates in the presence and absence of carnosine. DSC and a near-UV CD assay evidenced that the structural precursors of amyloid fibrils are polypeptide chain segments that lack stable structural elements. Moreover, we have found a disassembling effect of carnosine on α-crystallin amyloid fibrils. Finally, we show the ability of carnosine to restore most of the lens transparency in organ-cultured rat lenses exposed to similar denaturing conditions that were used for the in vitro experiments. © 2009 American Chemical Society.
Mildly denaturing conditions induce bovine α-crystallin, the major structural lens protein, to self-assemble into fibrillar structures in vitro. The natural dipeptide L-carnosine has been shown to have potential protective and therapeutic significance in many diseases. Carnosine derivatives have been proposed as potent agents for ophthalmic therapies of senile cataracts and diabetic ocular complications. Here we report the inhibitory effect induced by the peptide (L- and D-enantiomeric form) on α-crystallin fibrillation and the almost complete restoration of the chaperone activity lost after denaturant and/or heat stress. Scanning force microscopy (SFM), thioflavin T, and a turbidimetry assay have been used to determine the morphology of α-crystallin aggregates in the presence and absence of carnosine. DSC and a near-UV CD assay evidenced that the structural precursors of amyloid fibrils are polypeptide chain segments that lack stable structural elements. Moreover, we have found a disassembling effect of carnosine on α-crystallin amyloid fibrils. Finally, we show the ability of carnosine to restore most of the lens transparency in organ-cultured rat lenses exposed to similar denaturing conditions that were used for the in vitro experiments. © 2009 American Chemical Society.
Protective effects of L- and D-carnosine on alpha-crystallin amyloid fibril formation: implications for cataract disease
| ▼ Characterization of neurotoxic and neuroprotective factors by using computational methodologies |
Protective effects of L- and D-carnosine on alpha-crystallin amyloid fibril formation: implications for cataract disease
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Zhang P, Moretti M, Allione M, Tian Y, Ordonez-loza J, Altamura D, Giannini C, Torre B, Das G, Li E, Thoroddsen ST, Sarathy SM, Autiero I, Giugni A, Gentile F, Malara N, Marini M, Di Fabrizio E
* A droplet reactor on a super-hydrophobic surface allows control and characterization of amyloid fibril growth (68 views)
Commun Biol (ISSN: 2399-3642linking), 2020 Aug 20; 3(1): 457-457.
Impact Factor: 12.121
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Caporale A, Monti A, Selis F, Sandomenico A, Tonon G, Ruvo M, Doti N
* A comparative analysis of catalytic activity and stability of microbial transglutaminase in controlled denaturing conditions (164 views)
J Biotechnol (ISSN: 0168-1656linking), 2019 Aug 20; 302: 48-57.
Impact Factor: 3.163
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Malgieri G, D'Abrosca G, Pirone L, Toto A, Palmieri M, Russo L, Sciacca MFM, Tate R, Sivo V, Baglivo I, Majewska R, Coletta M, Pedone PV, Isernia C, De Stefano M, Gianni S, Pedone EM, Milardi D, Fattorusso R
* Folding mechanisms steer the amyloid fibril formation propensity of highly homologous proteins (357 views) (PDF 102 views)
Chem Sci (ISSN: 2041-6520linking, 2041-6520print, 2041-6539), 2018 Apr 7; 9(13): 3290-3298.
Impact Factor: 9.063
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Valente G, Depalo N, De Paola I, Iacobazzi RM, Denora N, Laquintana V, Comparelli R, Altamura E, Latronico T, Altomare M, Fanizza E, Striccoli M, Agostiano A, Saviano M, Del Gatto A, Zaccaro L, Curri ML
* Integrin-targeting with peptide-bioconjugated semiconductor-magnetic nanocrystalline heterostructures (387 views)
Nano Res (ISSN: 1998-0124), 2016; 9(3): 644-662.
Impact Factor: 7.354
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Oliveri V, Attanasio F, Puglisi A, Spencer J, Sgarlata C, Vecchio G
* Multifunctional 8-hydroxyquinoline-appended cyclodextrins as new inhibitors of metal-induced protein aggregation (634 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2014 Jul 14; 20(29): 8954-8964.
Impact Factor: 5.731
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Villari V, Attanasio F, Micali N
* Control of the structural stability of α-crystallin under thermal and chemical stress: The role of carnosine (411 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207linking), 2014; 118(47): 13770-13776.
Impact Factor: 3.302
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Vergara A, Grassi M, Sica F, Pizzo E, D’Alessio G, Mazzarella L, Merlino A
* A Novel Interdomain Interface In Crystallins: Structural Characterization Of The Beta Gamma-Crystallin From Geodia Cydonium At 0. 99 Angstrom Resolution (414 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2013 Jun; 69(6): 960-967.
Impact Factor: 7.232
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Visco AM, Campo N, Vagliasindi LI, Tabbì G
* STUDY OF THE RADICAL SPECIES INDUCED BY ELECTRON-BEAM IRRADIATION IN VACUUM ON BIOMEDICAL UHMWPE (268 views)
International Journal Of Polymer Analysis And Characterization (ISSN: 1023-666x), 2010; 15(7): 424-437.
Impact Factor: 0.814
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Vergara A, Castagnolo D, Carotenuto L, Vitagliano L, Berisio R, Sorrentino G, Gonzalez-ramirez L, Garcia-ruiz J, Zagari A
* Phase behavior and crystallogenesis under counter-diffusion conditions of the collagen-model peptide (Pro-Pro-Gly)10 (399 views)
J Cryst Growth (ISSN: 0022-0248), 2009 Jan 1; 311(2): 304-309.
Impact Factor: 1.534
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Grasso G, D'Urso L, Messina E, Cataldo F, Puglisi O, Spoto G, Compagnini G
* A mass spectrometry and surface enhanced Raman spectroscopy study of the interaction between linear carbon chains and noble metals (466 views)
Carbon (ISSN: 0008-6223), 2009; 47(11): 2611-2619.
Impact Factor: 4.504
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Merlino A, Verde C, Di Prisco G, Mazzarella L, Vergara A
* Reduction of ferric hemoglobin from Trematomus bernacchii in a partial bis-histidyl state produces a deoxy coordination even when encapsulated into the crystal phase (382 views)
Spectroscopy An International Journal (ISSN: 0712-4813), 2008; 22(2-3): 143-152.
Impact Factor: 0.82
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Attanasio F, Cascio C, Fisichella S, Nicoletti VG, Pignataro B, Savarino A, Rizzarelli E
* Trehalose effects on alpha-crystallin aggregates (529 views)
Biochem Biophys Res Commun (ISSN: 0006-291x, 0006-291xlinking), 2007 Mar 23; 354(4): 899-905.
Impact Factor: 2.749
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Matassa R, Carbone M, Lauceri R, Purrello R, Caminiti R
* Supramolecular structure of extrinsically chiral porphyrin hetero-assemblies and achiral analogues (319 views)
Adv Mater (ISSN: 0935-9648), 2007; 19(22): 3961-3967.
Impact Factor: 8.191
View Export to BibTeX Export to EndNote
* A droplet reactor on a super-hydrophobic surface allows control and characterization of amyloid fibril growth (68 views)
Commun Biol (ISSN: 2399-3642linking), 2020 Aug 20; 3(1): 457-457.
Impact Factor: 12.121
View Export to BibTeX Export to EndNote
Caporale A, Monti A, Selis F, Sandomenico A, Tonon G, Ruvo M, Doti N
* A comparative analysis of catalytic activity and stability of microbial transglutaminase in controlled denaturing conditions (164 views)
J Biotechnol (ISSN: 0168-1656linking), 2019 Aug 20; 302: 48-57.
Impact Factor: 3.163
View Export to BibTeX Export to EndNote
Malgieri G, D'Abrosca G, Pirone L, Toto A, Palmieri M, Russo L, Sciacca MFM, Tate R, Sivo V, Baglivo I, Majewska R, Coletta M, Pedone PV, Isernia C, De Stefano M, Gianni S, Pedone EM, Milardi D, Fattorusso R
* Folding mechanisms steer the amyloid fibril formation propensity of highly homologous proteins (357 views) (PDF 102 views)
Chem Sci (ISSN: 2041-6520linking, 2041-6520print, 2041-6539), 2018 Apr 7; 9(13): 3290-3298.
Impact Factor: 9.063
View Export to BibTeX Export to EndNote
Valente G, Depalo N, De Paola I, Iacobazzi RM, Denora N, Laquintana V, Comparelli R, Altamura E, Latronico T, Altomare M, Fanizza E, Striccoli M, Agostiano A, Saviano M, Del Gatto A, Zaccaro L, Curri ML
* Integrin-targeting with peptide-bioconjugated semiconductor-magnetic nanocrystalline heterostructures (387 views)
Nano Res (ISSN: 1998-0124), 2016; 9(3): 644-662.
Impact Factor: 7.354
View Export to BibTeX Export to EndNote
Oliveri V, Attanasio F, Puglisi A, Spencer J, Sgarlata C, Vecchio G
* Multifunctional 8-hydroxyquinoline-appended cyclodextrins as new inhibitors of metal-induced protein aggregation (634 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2014 Jul 14; 20(29): 8954-8964.
Impact Factor: 5.731
View Export to BibTeX Export to EndNote
Villari V, Attanasio F, Micali N
* Control of the structural stability of α-crystallin under thermal and chemical stress: The role of carnosine (411 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207linking), 2014; 118(47): 13770-13776.
Impact Factor: 3.302
View Export to BibTeX Export to EndNote
Vergara A, Grassi M, Sica F, Pizzo E, D’Alessio G, Mazzarella L, Merlino A
* A Novel Interdomain Interface In Crystallins: Structural Characterization Of The Beta Gamma-Crystallin From Geodia Cydonium At 0. 99 Angstrom Resolution (414 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2013 Jun; 69(6): 960-967.
Impact Factor: 7.232
View Export to BibTeX Export to EndNote
Visco AM, Campo N, Vagliasindi LI, Tabbì G
* STUDY OF THE RADICAL SPECIES INDUCED BY ELECTRON-BEAM IRRADIATION IN VACUUM ON BIOMEDICAL UHMWPE (268 views)
International Journal Of Polymer Analysis And Characterization (ISSN: 1023-666x), 2010; 15(7): 424-437.
Impact Factor: 0.814
View Export to BibTeX Export to EndNote
Vergara A, Castagnolo D, Carotenuto L, Vitagliano L, Berisio R, Sorrentino G, Gonzalez-ramirez L, Garcia-ruiz J, Zagari A
* Phase behavior and crystallogenesis under counter-diffusion conditions of the collagen-model peptide (Pro-Pro-Gly)10 (399 views)
J Cryst Growth (ISSN: 0022-0248), 2009 Jan 1; 311(2): 304-309.
Impact Factor: 1.534
View Export to BibTeX Export to EndNote
Grasso G, D'Urso L, Messina E, Cataldo F, Puglisi O, Spoto G, Compagnini G
* A mass spectrometry and surface enhanced Raman spectroscopy study of the interaction between linear carbon chains and noble metals (466 views)
Carbon (ISSN: 0008-6223), 2009; 47(11): 2611-2619.
Impact Factor: 4.504
View Export to BibTeX Export to EndNote
Merlino A, Verde C, Di Prisco G, Mazzarella L, Vergara A
* Reduction of ferric hemoglobin from Trematomus bernacchii in a partial bis-histidyl state produces a deoxy coordination even when encapsulated into the crystal phase (382 views)
Spectroscopy An International Journal (ISSN: 0712-4813), 2008; 22(2-3): 143-152.
Impact Factor: 0.82
View Export to BibTeX Export to EndNote
Attanasio F, Cascio C, Fisichella S, Nicoletti VG, Pignataro B, Savarino A, Rizzarelli E
* Trehalose effects on alpha-crystallin aggregates (529 views)
Biochem Biophys Res Commun (ISSN: 0006-291x, 0006-291xlinking), 2007 Mar 23; 354(4): 899-905.
Impact Factor: 2.749
View Export to BibTeX Export to EndNote
Matassa R, Carbone M, Lauceri R, Purrello R, Caminiti R
* Supramolecular structure of extrinsically chiral porphyrin hetero-assemblies and achiral analogues (319 views)
Adv Mater (ISSN: 0935-9648), 2007; 19(22): 3961-3967.
Impact Factor: 8.191
View Export to BibTeX Export to EndNote
13 Records (13 excluding Abstracts).
Total impact factor: 66.578 (66.578 excluding Abstracts).
Total 5 year impact factor: 56.075 (56.075 excluding Abstracts).
Total impact factor: 66.578 (66.578 excluding Abstracts).
Total 5 year impact factor: 56.075 (56.075 excluding Abstracts).
352 views. Last view on Wednesday 01 March 2023, 16:54:46
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