Biochemical and electrophoretic studies of -galactosidase in normal man, in patients with Fabry’s disease, and in Equidae.
Abstract: No abstract available
Publication Date: 1972-05-01 PubMed ID: 5028964PubMed Central: PMC1762264
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- Journal Article
Summary
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This study investigates the enzyme α-galactosidase in healthy individuals, those with Fabry’s disease, and in Equidae species, revealing two varieties of the enzyme in normal cells and one being absent in patients with Fabry’s disease.
Understanding Fabry’s Disease and α-galactosidase
- Fabry’s disease falls under the category of glycolipid storage disorder which is characterized by the accumulation of a lipid known as ceramide trihexoside.
- A distinguishing feature of this disease is the deficiency of an enzyme known as α-galactosidase.
- The manifestation of the disease shows a clear X-linkage, meaning it is associated with the X chromosome.
Hypotheses and Approach
- The researchers hypothesize that this disorder can be due to an issue in the regulation of enzyme production or due to a structural gene mutation.
- If an abnormal α-galactosidase activity is found, it would imply the disorder is due to a structural mutation.
- Conversely, if no abnormal protein could be found, it could be inferred that a regulatory mutation is a plausible cause.
Methodology
- The research investigates and compares the biochemical properties of α-galactosidase in normal leukocytes and fibroblasts and in those derived from patients with Fabry’s disease.
- In addition, electrophoretic techniques were employed to detect α-galactosidase activity on starch gels and to study the linkage of α-galactosidase.
Results
- The studies found that there are at least two isozymes or forms of α-galactosidase present in normal cells.
- Interestingly, one of these isozymes, termed as α-galactosidase A, was found missing in the cells of patients with Fabry’s disease.
- It was challenging to determine the location of the structural gene for α-galactosidase in humans. However, in Equidae species, this enzyme was found to be autosomally linked, that is, it is connected with a non-sex chromosome.
Cite This Article
APA
Beutler E, Kuhl W.
(1972).
Biochemical and electrophoretic studies of -galactosidase in normal man, in patients with Fabry’s disease, and in Equidae.
Am J Hum Genet, 24(3), 237-249.
Publication
Researcher Affiliations
MeSH Terms
- Animals
- Electrophoresis, Starch Gel
- Female
- Fibroblasts / enzymology
- Galactosidases / isolation & purification
- Genes
- Genes, Regulator
- Genetic Linkage
- Glycolipids / metabolism
- Horses
- Hot Temperature
- Humans
- Hybridization, Genetic
- Isoenzymes / isolation & purification
- Kinetics
- Leukocytes / enzymology
- Lipid Metabolism, Inborn Errors / enzymology
- Male
- Neuraminidase
- Perissodactyla
- Sex Chromosomes
- Syndrome
- Time Factors
References
This article includes 15 references
- SMITHIES O. An improved procedure for starch-gel electrophoresis: further variations in the serum proteins of normal individuals.. Biochem J 1959 Mar;71(3):585-7.
- Hakomori SI, Siddiqui B, Li YT, Li SC, Hellerqvist CG. Anomeric structure of globoside and ceramide grihexoside of human erythrocytes and hamster fibroblasts.. J Biol Chem 1971 Apr 10;246(7):2271-7.
- Krivit W, Desnick RJ, Mapes C, Anderson RL, Sweeley CC. Recent advances in Fabry's disease.. Trans Assoc Am Physicians 1970;83:121-32.
- Goldstone A, Konecny P, Koenig H. Lysosomal hydrolases: Conversion of acidic to basic forms by neuraminidase.. FEBS Lett 1971 Feb 12;13(1):68-72.
- Brady RO, Gal AE, Bradley RM, Martensson E, Warshaw AL, Laster L. Enzymatic defect in Fabry's disease. Ceramidetrihexosidase deficiency.. N Engl J Med 1967 May 25;276(21):1163-7.
- Kint JA. Fabry's disease: alpha-galactosidase deficiency.. Science 1970 Feb 27;167(3922):1268-9.
- Hamerton JL, Richardson BJ, Gee PA, Allen WR, Short RV. Non-random X chromosome expression in female mules and hinnies.. Nature 1971 Jul 30;232(5309):312-5.
- Brady RO. Genetics and the sphingolipidoses.. Med Clin North Am 1969 Jul;53(4):827-38.
- Bensaude I, Callahan J, Philippart M. Fabry's disease as an -galactosidosis: evidence for an -configuration in trihexosyl ceramide.. Biochem Biophys Res Commun 1971 May 21;43(4):913-8.
- Dofuku R, Tettenborn U, Ohno S. Testosterone-"regulon" in the mouse kidney.. Nat New Biol 1971 Jul 7;232(27):5-7.
- Ohno S, Dofuku R, Tettenborn U. More about X-linked testicular feminization of the mouse as a noninducible(is)mutation of a regulatory locus: 5-alpha-androstan-3-alpha-17-beta-diol as the true inducer of kidney alcohol dehydrogenase and beta-glucuronidase.. Clin Genet 1971;2(3):128-40.
- LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent.. J Biol Chem 1951 Nov;193(1):265-75.
- Mapes CA, Anderson RL, Sweeley CC, Desnick RJ, Krivit W. Enzyme replacement in Fabry's disease, an inborn error of metabolism.. Science 1970 Sep 4;169(3949):987-9.
- Handa S, Ariga T, Miyatake T, Yamakawa T. Presence of alpha-anomeric glycosidic configuration in the glycolipids accumulated in kidney with Fabry's disease.. J Biochem 1971 Mar;69(3):625-7.
- Romeo G, Migeon BR. Genetic inactivation of the alpha-galactosidase locus in carriers of Fabry's disease.. Science 1970 Oct 9;170(3954):180-1.
Citations
This article has been cited 19 times.- Hsiao JJ, Smits MM, Ng BH, Lee J, Wright ME. Discovery proteomics defines androgen-regulated glycoprotein networks in prostate cancer cells, as well as putative biomarkers of prostatic diseases. Sci Rep 2021 Nov 15;11(1):22208.
- Miyamura N, Araki E, Matsuda K, Yoshimura R, Furukawa N, Tsuruzoe K, Shirotani T, Kishikawa H, Yamaguchi K, Shichiri M. A carboxy-terminal truncation of human alpha-galactosidase A in a heterozygous female with Fabry disease and modification of the enzymatic activity by the carboxy-terminal domain. Increased, reduced, or absent enzyme activity depending on number of amino acid residues deleted. J Clin Invest 1996 Oct 15;98(8):1809-17.
- Mayes JS, Cray EL, Dell VA, Scheerer JB, Sifers RN. Endocytosis of lysosomal alpha-galactosidase A by cultured fibroblasts from patients with Fabry disease. Am J Hum Genet 1982 Jul;34(4):602-10.
- Ho MW, Beutler S, Tennant L, O'Brien JS. Fabry's disease: evidence for a physically altered -galactosidase. Am J Hum Genet 1972 May;24(3):256-66.
- Shaws TB, Lalley PA. Control of lysosomal acid phosphatase expression in man-mouse cell hybrids. Biochem Genet 1974 Feb;11(2):121-39.
- Nei M, Roychoudhury AK. Genic variation within and between the three major races of man, Caucasoids, Negroids, and Mongoloids. Am J Hum Genet 1974 Jul;26(4):421-43.
- Touster O. Some aspects of the cellular biochemistry of lysosomal and related glycosidases. Mol Cell Biochem 1973 Dec 15;2(2):169-77.
- Beutler E, Guinto E, Kuhl W. Variability of -galactosidase A and B in different tissues of man. Am J Hum Genet 1973 Jan;25(1):42-6.
- Tabira T, Goto I, Kuroiwa Y, Kikuchi M. Neuropathological and biochemical studies in Fabry's disease. Acta Neuropathol 1974;30(4):345-54.
- Roth J, Schulze E, Raabe G, Waldmann G. [Analytical study of Fabry's disease (author's transl)]. Virchows Arch A Pathol Anat Histol 1974;363(3):287-301.
- Hamerton JL, Mohandas T, McAlpine J. Localization of human gene loci using spontaneous chromosome rearrangements in human-Chinese hamster somatic cell hybrids. Am J Hum Genet 1975 Sep;27(5):595-608.
- Serov OL, Zakijan SM, Khlebodarova TM, Korochkin LI. Allelic expression in intergeneric fox hybrids (Alopex lagopus x Vulpes vulpes). I. Comparative electrophoretic studies on blood enzymes and proteins in arctic and silver foxes. Biochem Genet 1976 Dec;14(11-12):1091-103.
- Weil D, Van-Cong N, Finaz C, Rebourcet R, Cochet C, de Grouchy J, Frézal J. [Regional localization of the genes for human IDHs, MDHs PGK, alphaGAL, G6PD by interspecific hybridization (author's transl)]. Hum Genet 1977 Apr 15;36(2):205-11.
- Romeo G, D'Urso M, Pisacane A, Blum E, De Falco A, Ruffilli A. Residual activity of alpha-galactosidase A in Fabry's disease. Biochem Genet 1975 Oct;13(9-10):615-28.
- Weil D, Van-Cong N, Rebourcet R, Frézal J. [Regional localization of the genes for human LDHb, TPI, ENO2, PepB, PGK, alphaGALa, HGPRT, G6PD by interspecific hybridization (author's transl)]. Hum Genet 1978 Jun 9;42(2):181-8.
- Spence MW, Goldbloom AL, Burgess JK, D'entremont D, Ripley BA, Weldon KL. Heterozygote detection in angiokeratoma corporis diffusum (Anderson-Fabry disease). Studies on plasma, leucocytes, and hair follicles. J Med Genet 1977 Apr;14(2):91-9.
- Hamers MN, Westerveld A, Khan M, Tager JM. Characterization of alpha-galactosidase isoenzymes in normal and Fabry human-Chinese Hamster somatic cell hybrids. Hum Genet 1977 May 10;36(3):289-97.
- Roth J, Roth H. [Electron microscopic observations in internal organs in morbus Fabry (author's transl)]. Virchows Arch A Pathol Anat Histol 1978 May 5;378(1):75-90.
- Wan Ho M, Norden AG, Alhadeff JA, O'Brien JS. Glycosphingolipid hydrolases: properties and molecular genetics. Mol Cell Biochem 1977 Oct 7;17(3):125-40.
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