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Multiple sulfatase deficiency (Mucosulfatidosis): Impaired degradation of labeled sulfated compounds in cultured skin fibroblasts in vivo (1980)

Eto, Y. ; Numaguchi, S. ; Tahara, T. ; [et al.]

Springer

European journal of pediatrics 135 (1980), S. 85-89

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ISSN: 1432-1076

Keywords: Multiple sulfatase deficiencies ; Cultured skin fibroblasts ; 35S-sulfatide ; 35S-mucopolysaccharide ; 14C-cholesterol sulfate degradation

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Abstract Skin fibroblasts from a Japanese patient with multiple sulfatase deficiency (MSD) (Mucosulfatidosis) were studied with regard to metabolism of various sulfated compounds in vivo. Several sulfatase activities (arylsulfatases A,B and C, cholesterol sulfatase, heparin N-sulfatase) were deficient in skin fibroblasts grown in F-10 CO2 medium. The accumulation and degradation of 35S-sulfatide, 35S-mucopolysaccharides, 14C-cholesterol sulfate by MSD cells were also studied, comparing them to control, Hunter and metachromatic leukodystrophy cells. MSD fibroblasts accumulated and failed to degrade these compounds in vivo. Cholesterol sulfate was also incorporated into the control and pathological cells, and MSD cells were unable to hydrolyze cholesterol sulfate, though cholesterol sulfate is known to be hydrolyzed in the non-lysosomal subfraction. From these data it is clear that multiple enzyme deficiencies in MSD fibroblasts can be demonstrated in vivo.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00445900

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Discovery of a human erythroid differentiation factor (EDF) and its large-scale production (1988)

Tsuji, T. ; Eto, Y. ; Takano, S. ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Biotechnology and Bioengineering 31 (1988), S. 675-681

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ISSN: 0006-3592

Keywords: Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology

Notes: A novel human protein exhibiting erythroid differentiation activity was discovered in the culture fluids of phorbol ester-stimulated human cells. The differentiation assay system involving Friend virus-derived mouse leukemia cells was used. THP-1 cells of myelomonocytic origin were typical producers. 4β-Phorbol 12-myristate 13-acetate (PMA) was essential for inducible excretion of the erythroid differentiation factor (EDF). The factor was stable toward heat and pH (acidic or alkaline) but lost its activity on pronase treatment, which suggested its proteinous nature. After an optimization of the condition, production of EDF was performed on a 200-L scale for purification of the protein.

Additional Material: 4 Ill.