Defect in 3'-phosphoadenosine 5'-phosphosulfate synthesis in brachymorphic mice. II. Tissue distribution of the defect |
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Authors: | K Sugahara N B Schwartz |
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Affiliation: | Departments of Pediatrics and Biochemistry, The Joseph P. Kennedy, Jr. Mental Retardation Research Center, Pritzker School of Medicine, University of Chicago, Chicago, Illinois 60637 USA |
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Abstract: | The tissue distribution of the defective PAPS synthetic pathway in homozygous brachymorphic mice () has been investigated using four different criteria: (i) incorporation of 35SO42? into adenosine 5′-phosphosulfate (APS), 3′-phosphoadenosine 5′-phosphosulfate (PAPS), and endogenous macromolecular acceptors, (ii) APS kinase (adenylylsulfate kinase; ATP:adenylylsulfate 3′-phosphotransferase, EC 2.7.1.25) activity, (iii) ATP sulfurylase (sulfate adenylyltransferase; ATP:sulfate adenylyltransferase, EC 2.7.7.4) activity, (iv) thermostability of ATP sulfurylase. With respect to the first three criteria, the results indicate that liver is affected as profoundly as cartilage (K. Sugahara and N. B. Schwartz, Arch. Biochem. Biophys. (1982) 214, 589–601). In contrast, skin and brain show no differences between normal and mutant. Kidney is significantly, but only moderately, affected. The results from thermostability studies demonstrate that ATP sulfurylase activity is more labile in cartilage, liver, and kidney, but not in skin or brain, supporting the above-observed distribution of the defect. Therefore, the present results indicate a multiple, but not universal, tissue distribution of the defective PAPS synthetic pathway in mice. Furthermore, these findings support the suggestion that ATP sulfurylase as well as APS kinase is defective in brachymorphic mice. |
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Keywords: | Recipient of Career Development Award K04-AM00603. Author to whom all correspondence should be addressed. |
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