Cystic fibrosis: acidification indication

Article Abstract:

Patients with cystic fibrosis have defects in a number of metabolic functions and experience various clinical symptoms resulting from abnormal secretions of the sweat glands, intestines, pancreas and lungs. Cystic fibrosis has been shown to occur when a particular gene, known as the cystic fibrosis transmembrane conductance regulator (CFTR), is genetically altered, or mutated. The CFTR functions as a channel, transporting chloride ions across cell membranes. It is not certain how this altered protein causes all the metabolic defects that are associated with the disease. Research by J. Barasch and colleagues, published in the July 4, 1991 issue of Nature, shows that the loss of this chloride channel causes certain components inside the cell to be basic instead of acidic. The altered environment seems to result in the defective modification of proteins, such as the abnormal addition of different types of sugar molecules to proteins. This may result in functional defects in several proteins, including enzymes (which act as catalysts for biological functions). Further study is needed to explore whether this is the mechanism involved in the development and progression of cystic fibrosis and to develop therapies that overcome this defect so that cystic fibrosis can be treated. (Consumer Summary produced by Reliance Medical Information, Inc.)

Physiological aspects, Development and progression

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Stimulation of CFTR activity by its phosphorylated R domain

Article Abstract:

Researchers investigated the action of phosphorylation in controlling the activity of the chloride channel in the cystic fibrosis transmembrane conductance regulator (CFTR). They found that adding a regulatory (R) domain peptide to a CFTR variant, which had much of the R-domain removed, did not inhibit activity, whereas a phosphorylated R-domain peptide stimulated activity. Investigation of this surprising dual effect of the R-domain revealed that phosphorylation of the R-domain increases ATP sensitivity and thereby increases the rate of channel opening. Phosphorylation of one domain stimulates ATP interaction with another domain.

Protein kinases, Phosphorylation

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Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive

Article Abstract:

Cystic fibrosis (CF) is caused by mutations to a plasma membrane chloride channel regulator, cystic fibrosis transmembrane conductance regulator (CFTR). The most frequent mutation involves removal of phenylalanine at residue 508 (CFTR-delta-F508). However, the processing of CFTR-delta-F508 resumes a wild-type mutation as the temperature of incubation goes down. This indicates that the most prevalent CF mutation is affected by temperature.

Causes of, Cell membranes, Plasma membranes

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