31 research outputs found
Acylphosphatase stimulates Ca2+-transport and Ca2+-dependent ATPase activity in cardiac sarcoplasmic reticulum
Seladin-1/dhcr24 protects neuroblastoma cells against aβ toxicity by increasing membrane cholesterol content
RELATIONSHIP BETWEEN SOLUBLE ACYLPHOSPHATASE AND ACYLPHOSPHATASE ACTIVITY FROM SARCOPLASMIC RETICULUM
Studies on synthesis and degradation rates and some molecular properties of guinea-pig muscle acylphosphatase
Regional assignment of the loci for adenilate kinase to 9q32 and for a-acid glycoprotein to 9q31-q32. A locus for Goltz syndrome in region 9q32-qter?
Normal levels of adenylate kinase (AK-1) and of agr1-acid glycoprotein (ORM1) were found in a girl with a deletion 9q32-qter secondary to a maternal translocation (4q35; 9q32), thus excluding these loci from the deleted region. These results, and comparison with other informative data, map the locus for AK-1 to 9q32 and that for ORM1 to region 9q31-q32. The girl has several signs of the Goltz syndrome (focal dermal hypoplasia), which is listed in the McKusick catalog (no. 30560) as an X-linked dominant condition. Our finding indicates that the locus for Golz syndrome is autosomal and in region 9q32-qter or that there are two such conditions, one autosomal and one X-linked
Drosophila melanogaster acylphosphatase: a common ancestor for acylphosphatase isoenzymes of vertebrate species
An open reading flame encoding a putative acylphosphatase
was found in Drosophila melanogaster. The corresponding
gene product shows 40% identity and 22 additional amino
acid residues at the C-terminus as compared to muscle- and
common-type human acylphosphatases. Moreover, all the
residues involved in the catalytic mechanism of vertebrate
enzymes are conserved in the D. melanogaster acylphosphatase.
The D. melanogaster protein and a deletion mutant, similar in
length to vertebrate acylphosphatases, were produced by cloning
the corresponding cDNA in Escherichia coli. The wild-type
enzyme is a protein with a well-established three-dimensional fold
and a markedly reduced conformational stability as compared to
vertebrate isoenzymes. The specific activity of the enzyme is
significantly lower than that found in vertebrate enzymes though
the substrate binding capability is basically unaltered. The
deletion of 22 residues does not cause a significant change in k~t,
while affecting the apparent binding parameters. This work
suggests that the genes encoding the vertebrate enzymes originate
from an ancestor gene by duplication and subsequent evolution
Regional assignment of the loci for adenylate kinase to 9q32 and for alfa1 acid glycoprotein to 9q31-q32
Modification of plasma glycosaminoglycans in long distance runners
Background: It is well documented that exercise reduces the risk of thromboembolic disease, possibly by increasing the plasma concentration of anticoagulant-antithrombotic compounds. Objectives: As plasma glycosaminoglycans (GAGs) play a role in the anticoagulant-antithrombotic potential of plasma, to examine the concentration and profile of these compounds in well trained, long distance runners and sedentary subjects. Methods: Plasma GAGs were measured in 10 male, long distance runners and 10 sedentary counterparts before and after ergometric tests. GAGs were extracted, purified, and identified by electrophoretic and enzymatic methods, and measured as hexosamine. Results: Plasma GAGs found in sedentary subjects were slow migrating heparan sulphates I and II, keratan sulphate I, and chondroitin 4–6-sulphate. Those found in trained athletes were slow migrating heparan sulphate I, chondroitin 4–6-sulphate (or keratan sulphate I), and fast migrating heparan sulphate. Total plasma concentrations of GAGs were higher in athletes than in sedentary subjects at rest. In sedentary subjects, plasma GAGs did not change after cycle ergometric exercise at 80% of their anaerobic threshold. However, the appearance of a novel band of heparan sulphate migrating faster than fast migrating heparan sulphate was observed in athletes after exercise. Conclusions: Exercise changes the amount and profile of plasma GAGs; these changes may play a role in protecting subjects who practise aerobic sports against developing cardiovascular disease