Evaluation of carrier detection of Duchenne muscular dystrophy using carbonic anhydrase III and creatine kinase

Heath, Robert G.; Carter, N D; Jeffery, Stephen; Edwards, Robert J.; Watts, D.C.; Watts, R. L.

doi:10.1002/ajmg.1320210211

Cited by 3 publications

(1 citation statement)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Assay systems were used with single enzyme activities or combinations of various muscle-derived enzymes in patient serum [206-208, 211, 213]. Besides the examining of disease progression in dystrophic children, screening approaches included fetal plasma [219,220] and the blood analysis of newborns [204,205,221], as well as a large number of investigations into the evaluation of carrier status [222][223][224][225][226]. The combined testing of several serum markers has shown the potential of improved screening efficiency, such as the usage of creatine kinase, myoglobin and hemopexin for identifying Duchenne muscular dystrophy carriers [227].…”

Section: Circulating Biomarkers For Monitoring General Muscle Damagementioning

confidence: 99%

Mass Spectrometry-Based Identification of Muscle-Associated and Muscle-Derived Proteomic Biomarkers of Dystrophinopathies

Dowling

Holland

Ohlendieck

2014

Journal of Neuromuscular Diseases

View full text Add to dashboard Cite

The optimization of large-scale screening procedures of pathological specimens by genomic, proteomic and metabolic methods has drastically increased the bioanalytical capability for swiftly identifying novel biomarkers of inherited disorders, such as neuromuscular diseases. X-linked muscular dystrophy represents the most frequently inherited muscle disease and is characterized by primary abnormalities in the membrane cytoskeletal protein dystrophin. Mass spectrometry-based proteomics has been widely employed for the systematic analysis of dystrophin-deficient muscle tissues, using patient samples and animal models of dystrophinopathy. Both, gel-based methods and label-free mass spectrometric techniques have been applied in comparative analyses and established a large number of altered proteins that are associated with muscle contraction, energy metabolism, ion homeostasis, cellular signaling, the cytoskeleton, the extracellular matrix and the cellular stress response. Although these new indicators of muscular dystrophy have increased our general understanding of the molecular pathogenesis of dystrophinopathy, their application as new diagnostic or prognostic biomarkers would require the undesirable usage of invasive methodology. Hence, to reduce the need for diagnostic muscle biopsy procedures, more recent efforts have focused on the proteomic screening of suitable body fluids, such as plasma, serum or urine, for the identification of changed concentration levels of muscle-derived peptides, protein fragments or intact proteins. The occurrence of muscular dystrophy-related protein species in biofluids will be extremely helpful for the future development of cost-effective and non-invasive diagnostic procedures. Novel biomarker signatures of dystrophinopathies will be indispensible for the swift evaluation of innovative therapeutic approaches, such as exon skipping, codon-read-through or stem cell therapy.

show abstract

Section: Circulating Biomarkers For Monitoring General Muscle Damagementioning

confidence: 99%

Mass Spectrometry-Based Identification of Muscle-Associated and Muscle-Derived Proteomic Biomarkers of Dystrophinopathies

Dowling

Holland

Ohlendieck

2014

Journal of Neuromuscular Diseases

View full text Add to dashboard Cite

show abstract

Carbonic anhydrases

Deutsch

1987

International Journal of Biochemistry

View full text Add to dashboard Cite

Some of the current studies of carbonic anhydrases are directed to the genetic mechanisms underlying their synthesis. Determination of the structure of their genes will probably most readily resolve the question of whether the membrane bound forms of the enzyme represent products of additional loci other than those of the three well-known soluble forms. Extensions of our knowledge of the sequences of these isozymes as well as those from lower animals and from plants will make possible a more precise evaluation of the extent of the multigene aspects of these proteins and their evolutionary backgrounds. Studies of the interrelationships of the regulation of the transcriptional and translational processes of the well-known isozymes and in particular the effects of hormones will be of interest. Insights into modifications of the isozymes' synthetic processes occurring in various diseases should also be forth-coming from these studies. In addition to the above the applications of what are perhaps today somewhat classical methods of protein chemistry will be needed to explore the reasons for the changes in activity accompanying the sequence variations of the different isozymes, the decreases or increases in activity accompanying derivatizations of specific residues and the reasons for the differences in the activity of different inhibitors on the various isozymes. The broad specificity of these enzymes for different substrates and the ability of CA-III to hydrolyze various phenyl esters and in some cases to become derivatized also present problems in protein structural chemistry. In terms of the latter reactions, the meaning of the relationships of these activities to those of the protein ubiquitin, which is homologous to CA-III, needs clarification. It would appear that various of the protein structural studies will be aided by crystallographic investigations of not only CA-III but of various of its derivatives which undergo either increases or decreases in activity. The above areas of studies present a wide variety of problems for workers in various disciplines and backgrounds who are interested in the carbonic anhydrases.

show abstract

Refined candidate region for arthrogryposis multiplex congenita (AMC) and inheritance of humpy back, splay leg and AMC-like phenotypes in pigs

Haubitz¹

2012

View full text Add to dashboard Cite

Evaluation of carrier detection of Duchenne muscular dystrophy using carbonic anhydrase III and creatine kinase

Cited by 3 publications

References 12 publications

Mass Spectrometry-Based Identification of Muscle-Associated and Muscle-Derived Proteomic Biomarkers of Dystrophinopathies

Mass Spectrometry-Based Identification of Muscle-Associated and Muscle-Derived Proteomic Biomarkers of Dystrophinopathies

Carbonic anhydrases

Refined candidate region for arthrogryposis multiplex congenita (AMC) and inheritance of humpy back, splay leg and AMC-like phenotypes in pigs

Contact Info

Product

Resources

About