Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The histochemical profile of individual human skeletal muscle fibres was analysed by correlating mitochondrial oxidative enzyme activity and that of myofibrillar ATPase at pH 9.5 and after pre-incubation at pH 4.3 and pH 4.6. In normal control muscle, only a small percentage of fibres did not conform to one or other of the normal variants of Type I and Type II fibres. In biopsies from early cases of Werdnig-Hoffmann disease, the denervated fibre populations contained many abnormal Type I and Type II fibres, including "IIc" fibres, but the basic distinction between Type I and Type II was preserved. However, in infantile spinal muscular atrophy patients aged two years and over, this distinction was progressively lost, leading to the total dedifferentiation of the atrophied fibres. In the Kugelberg-Welander form of spinal muscular atrophy, many of the constituent fibres of re-innervated groups displayed normal or near-normal histochemical profiles, but chronically denervated fibres became totally dedifferentiated. In Duchenne dystrophy, the spectrum of histochemical types appeared to be more continuous due to the emergence of fibres with properties intermediate between those of the normal variants, but the basic distinction between Type I and Type II fibres was preserved in the majority of cases. The percentage of severely abnormal fibres was higher in Type II than Type I and probably contributed to the observed decrease in the overall proportion of Type II fibres. Although very small atrophied fibres were observed in biopsies from cases of Becker and Duchenne dystrophy, these did not show the total dedifferentiation seen in the chronically denervated fibres in cases of spinal muscular atrophy.
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PMID:Patterns of abnormal histochemical fibre type differentitation in human muscle biopsies. 15 Apr 55

A cDNA encoding a Ca-ATPase homologue, designated SMA3, was isolated from an adult cDNA library of Schistosoma mansoni. The full-length cloned DNA contains a 3105-bp open reading frame that potentially encodes a 1035-amino-acid protein with a M(r) of 113,729 and a pl of 6.48. Homology searches for SMA3 reveal high sequence identity with a variety of Ca-ATPases from evolutionarily diverse organisms. SMA3 is predicted to contain 10 transmembrane regions typical of this protein family as well as other conserved domains, such as the phosphorylation site and FITC binding domain. The greatest sequence identity (40-50%) is found to those Ca-ATPases belonging to the secretory pathway subclass. Identification of the 5' end of the SMA3 cDNA by RACE analysis reveals the presence of a 36-base spliced leader RNA, suggesting that the SMA3 pre-mRNA is processed by trans-splicing. Northern analysis reveals a single dominant transcript of 5 kb in adult RNA preparations. Antibodies raised against an amino terminal peptide detect the protein in the adult tegument, suggesting that SMA3 functions to help control Ca homeostasis within the tegument and may play a role in signal transduction at the host parasite interface.
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PMID:Schistosoma mansoni: molecular characterization of a tegumental Ca-ATPase (SMA3). 1156 Apr 14