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Bibliografía
[1.]
E. Beutler, G.A. Grabowski.
Gaucher disease.
The metabolic and molecular basis of inherited disease, 7.a, pp. 2641-2670
[2.]
G.A. Grabowski.
Gaucher disease. Enzymology, genetics, and treatment.
Adv Hum Genet, 21 (1993), pp. 377-441
[3.]
B. Shafit-Zagardo, E.A. Devine, M. Smith, G.A.F. Arredondo, R.J. Desnick.
Assignment of the gene for acid betaglucosidase to human chromosome 1.
Am J Hum Genet, 33 (1981), pp. 564
[4.]
G.A. Grabowski, M. Horowitz.
Gaucher disease: molecular, genetics and enzymological aspects.
Baillière’s Clin Haematology, 10 (1997), pp. 635-656
[5.]
L. Lacerda, O. Amaral, R. Pintó, P. Oliveira, J. Aerts, M.C. Sa Miranda.
Gaucher disease: N370S glucocerebrosidase gene frequency in the Portuguese population.
Clin Genet, 45 (1994), pp. 298-300
[6.]
O. Nilsson, J.E. Mansson, G. Hakansson, L. Svennerholm.
The occurrence of psychosine and other glycolypids in spleen and liver from three subtypes of Gaucher’s disease.
Biochim Biophys Acta, 712 (1982), pp. 453-463
[7.]
P.M. Strasberg, I. Warren, M.A. Skomorowski, J.A. Lowden.
HPLC analysis of neutral glycolipids: an aid in the diagnosis of lysosomal storage disease.
Clin Chim Acta, 132 (1983), pp. 29-41
[8.]
A. Erickson, K. Johanson, J.E. Mansson, L. Svenenerholm.
Enzyme replacement therapy of infantile Gaucher disease.
Neuropediatrics, 24 (1993), pp. 237-238
[9.]
N.W. Barton, R.O. Brady, J.M. Dambrosia, A.M. Di Bisceglie, S.H. Doppelt, S.C. Hill.
Replacement therapy for inherited enzyme deficiency-macrophage targeted glucocerebrosidase for Gaucher’s disease.
N Engl J Med, 324 (1991), pp. 1464-1470
[10.]
A. Erikson, M. Astrom, J.E. Mansson.
Enzyme infusion therapy of Norrbottnian type (type 3) Gaucher disease.
Neuropediatrics, 26 (1995), pp. 203-207
[11.]
C. Scheibenbogen, R. Andreesen.
Developmental regulation of the cytokine repertoire in human macrophages: IL-1, IL-6, TNF-a and M-CSF.
J Leukoc Biol, 50 (1991), pp. 35-42
[12.]
S. O’Laughlin, M. Braverman, M. Smith-Jefferies, P. Buckley.
Macrophages (histocytes) in various reactive and inflammatory conditions express different antigenic phenotypes.
Hum Pathol, 23 (1992), pp. 1410-1418
[13.]
Y. Liel, A. Rudich, O. Nagauker-Shriker, T. Yermiyahu, R. Levy.
Monocyte dysfunction in patients with Gaucher disease: evidence for interference of glucocerebrosidase with superoxide generation.
Blood, 83 (1994), pp. 2646-2653
[14.]
H. Ginsberg, G.A. Grabowski, J.C. Gibson, R. Fagerstrom, J. Goldblatt, H.S. Gilbert.
Reduced plasma concentrations of total, low density lipoprotein and high density lipoprotein cholesterol in patients with Gaucher type I disease.
Clin Genet, 26 (1984), pp. 109-116
[15.]
N.A. Le, J.C. Gibson, A. Rubinstein, G.A. Grabowski, H.N. Ginsberg.
Abnormalities in lipoprotein metabolism in Gaucher type 1 disease.
Metabolism, 37 (1988), pp. 240-245
[16.]
M. Pocoví, A. Cenarro, F. Civeira, M.A. Torralba, J.I. Pérez-Calvo, P. Mozas.
Beta-glucocerebrosidase gene locus as a link for Gaucher’s disease and familial hypo-a-lipoproteinaemia.
Lancet, 351 (1998), pp. 1919-1923
[17.]
G. Franceschini, C.R. Sirtori, A. Capurso, K.H. Weisgraber, R.W. Maley.
A-I Milano apoprotein: decreased high density lipoprotein cholesterol levels with significant lipoprotein modifications and without clinical atherosclerosis in an Italian family.
J Clin Invest, 66 (1980), pp. 892-900
[18.]
D. Recalde, A. Cenarro, F. Civeira, M. Pocoví.
Apo A-IZaragoza: A novel mutation in the apolipoprotein A-I gene associated with familial hypoalphalipoproteinemia.
Hum Mutat, 11 (1998), pp. 416
[19.]
S.K. Basu, Y. Ho, M.S. Brown, D.W. Bilheimer, R.G. Anderson, J.L. Goldstein.
Biochemical and genetic studies of the apo E secreted by mouse macrophages and human monocytes.
J Biol Chem, 257 (1982), pp. 9788-9795
[20.]
A. Von Eckardstein.
Cholesterol efflux from macrophages and other cells.
Curr Opin Lipidol, 7 (1996), pp. 308-319
[21.]
M.F. Linton, J.B. Atkinson, S. Fazio.
Prevention of atherosclerosis in apolipoprotein E deficient mice by bone marrow transplantation.
Science, 267 (1995), pp. 1034-1037
[22.]
G. Assmann, A. Von Eckardstein, Y. Huang, S. Wu.
A lipoprotein containing only apo E is present in normal and HDL-deficient plasmas and releases cholesterol from cells. International Symposium on Atherosclerosis. Montreal.
Atherosclerosis X, pp. 662-665
[23.]
A. Abrahamov, D. Elstein, V. Gross-Tsur, B. Farber, Y. Glaser, I. Hadas-Halpern.
Gaucher’s disease variant characterized by progressive calcification of heart valves and unique genotype.
Lancet, 346 (1995), pp. 1000-1003
[24.]
A.J. Chabas, B. Cormand, D. Ginberg, J.M. Burguera, S. Balcells, J.L. Merino.
Unusual expression of Gaucher’s disease: cardiovascular calcifications in three sibs homozygous for the D409H mutation.
J Med Genet, 32 (1995), pp. 740-742
[25.]
I. Gery, S. Zigler, R.O. Brady, J.A. Barranger.
Selective effects of glucocerebroside (Gaucher’s storage material) on macrophage cultures.
J Clin Invest, 68 (1981), pp. 1182-1189
[26.]
M.J. Allen, B.J. Myer, A.M. Khokher, N. Rushton, T.M. Cox.
Proinflammatory cytokines and the pathogenesis of Gaucher’s disease: increased release of interleukin-6 and interleukin-10.
Q J Med, 90 (1997), pp. 19-25
[27.]
C.E.M. Hollak, L. Evers, J.M.F.G. Aerts, M.H.J. Van Oers.
Elevated level of M-CSF, CD14 and IL8 in type I Gaucher patients.
Blood Cells Mol Dis, 23 (1997), pp. 201-212
[28.]
A. Zimran, A. Kay, T. Gelbart, P. Garver, D. Thurston, A. Saven.
Gaucher’s disease: clinical, laboratory, radiologic and genetic features of 53 patients.
Medicine (Baltimore, 71 (1992), pp. 337-353
[29.]
P.W. Pratt, S. Estren, S. Kochwa.
Immunoglobulin abnormalities in Gaucher’s disease.
Blood, 31 (1968), pp. 635-640
[30.]
J.T. Salonen, S. Ylá-Herttuala, R. Yamamoto, S. Butler, H. Korpela, R. Salonen, et al.
Autoantibody against oxidized LDL and progression of carotid atherosclerosis.
Lancet, 339 (1992), pp. 883-887
[31.]
J.L. Beaumont, F. Doucet, P. Vivier, M. Antonucci.
Immunoglobulin bound lipoproteins (Ig-Lp) as marker of familial hypercholesterolemia, xanthomatosis and atherosclerosis.
Atherosclerosis, 74 (1988), pp. 191-201
[32.]
R.I. Griffith, G.T. Virella, H.C. Stevenson, M.F. Lopes-Virella.
Low density lipoprotein metabolism by human macrophages activated with low density lipoprotein immunocomplexes.
J Exp Med, 168 (1988), pp. 1041-1059
[33.]
M.W. Fanger, L. Shen, R.F. Graziano, P.M. Guyre.
Citotoxicity mediated by human Fc receptor of IgG.
Immunol Today, 10 (1989), pp. 92-99
[34.]
T. Levade, S. Gatt, A. Maret, R. Salvayre.
Different pathways of uptake and degradation of sphingomyelin by limphoblastoid cells and the potential participation of the neutral sphingomyelinase.
J Biol Chem, 266 (1991), pp. 13519-13529
[35.]
P.M. Morganelli, P.M. Guyre.
Macrophage function and Gaucher disease. Gaucher Clin Perspectives.
Mol Med Therapeutics, 3 (1995), pp. 1-5
[36.]
J. Flach, P. Plet, P. Jolles.
What’s new in chitinase research?.
Experientia, 48 (1992), pp. 701-716
[37.]
M. Huberd, E. Cabib, L.H. Miller.
Malaria parasite chitinase and penetration of the mosquito peritrophic membrane.
Proc Natl Acad Sci USA, 88 (1991), pp. 2807-2810
[38.]
N. Raghavan, D.O. Freedman, P.C. Fitzgerald, T.R. Unnasch, E.A. Ottesen, T.B. Nutman.
Cloning and characterization of potential protective chitinase-like recombinant antigen from Wucheria bancrofti.
Infect Immun, 62 (1994), pp. 1901-1908
[39.]
C.E.M. Hollack, S. Van Weely, M.H.J. Van Oers, J.M.F.G. Aerts.
Marked elevation of plasma chitotriosidase activity. A novel hallmark of Gaucher disease.
J Clin Invest, 93 (1994), pp. 1288-1292
[40.]
E.B. Arias, H.G. Verhage, R.C. Jaffe.
Complementary deoxyribonucleic acid cloning and molecular characterization of an estrogendependent human oviductal glycoprotein.
Biol Reprod, 51 (1994), pp. 685-694
[41.]
B. Hu, K. Trinh, W.F. Figueira, P.A. Price.
Isolation and sequence of a novel human chondrocyte protein related to mammalian members of a chitinase protein family.
J Biol Chem, 271 (1996), pp. 19415-19420
[42.]
Y. Guo, W. He, A.M. Boer, R.A. Wevers, A.M. De Bruijn, J.E. Groener.
Elevated plasma chitotriosidase activity in various lysosomal storage disease.
J Inher Metab Dis, 18 (1995), pp. 717-722
[43.]
A. Cenarro, M. Pocoví, P. Giraldo, A.L. García-Otín, J.M. Ordovás.
Plasma lipoprotein responses to enzyme-replacement in Gaucher’s disease.
Lancet, 353 (1999), pp. 642-643
[44.]
E. Young, C. Chatterton, A. Vellodi, B. Winchester.
Plasma chitotriosidase activity in Gaucher disease patients who have been treated either by bone marrow transplantation or by enzyme replacement therapy with alglucerase.
J Inher Metab Dis, 20 (1997), pp. 595-602
[45.]
J.M.F.G. Aerts, C.E.M. Hollack.
Plasma and metabolic abnormalities in Gaucher’s disease.
Baillière’s Clin Haematol, 10 (1997), pp. 691-709
[46.]
R. Boot, H. Renkema, A. Strijiand, A.J. Van Zonneveld, J.M.F.G. Aerts.
Cloning of cDNA encoding chitotriosidase, a human chitinase produced by macrophages.
J Biol Chem, 270 (1995), pp. 26252-26256
[47.]
R. Boot, H. Renkema, M. Verhoek, A. Strijland, J. Bliek, T.M. De Meulemeester.
The human chitotriosidase gene. Nature of inherited enzyme deficiency.
J Biol Chem, 273 (1998), pp. 25680-25685
[48.]
B.E. Hakala, C. White, A.D. Recklies.
Human cartilague gp39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of chitinase protein family.
J Biol Chem, 268 (1983), pp. 25803-25810
[49.]
R.B. Kirkpatrick, J.G. Emery, J.R. Connor, R. Doods, P.G. Lysko, M. Rosenberg.
Induction and expression of human cartilague glycoprotein 39 in rheumatoid inflammatory and peripheral blood monocyte-derived macrophages.
Exp Cell Res, 237 (1997), pp. 46-54
[50.]
S.W. Krause, M. Rehli, E. Kreutz, L. Schwarzfischer, J.D. Paulauskis, R. Andreesen.
Differential screening identifies markers of monocyte to macrophage maturation.
J Leukoc Biol, 60 (1996), pp. 540-545
[51.]
G.F. Verheijden, A.W. Rijnders, E. Bos, C.J. Coenen-de Roo, C.J. Van Staveren, A.M. Miltenburg.
Human cartilague glycoprotein 39 as a candidate autoantigen in rheumatoid arthritis.
Arthritis Rheum, 40 (1997), pp. 1115-1125
[52.]
J.S. Johansen, S. Moller, P.A. Price, F. Bendtsen, J. Junge, C. Garbarsch.
Plasma YKL-40: a new potential marker of fibrosis in patients with alcoholic cirrhosis.
Scand J Gastroenterol, 32 (1997), pp. 582-590
[53.]
R.T.G. Boot, T.A. Van Achterberg, B.E. Van Aken, G.H. Renkema, M.J. Jacobs, J.M. Aerts.
Strong induction of member of chitinase family of proteins in atherosclerosis: chitotriosidase and human cartilague gp39 expressed in lesion macrophages.
Arterioscler Thromb Vasc Biol, 19 (1999), pp. 687-694
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