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THE SUBCELLULAR DISTRIBUTION OF CEREBRAL PHOSPHOPROTEINS.

ABSTRACT: 1. The subcellular distribution of the phosphoprotein fraction of grey matter from guinea-pig brain has been determined. Phosphoproteins occurred in all fractions of the tissue, the mitochondrial fraction containing 29%, supernatant 26%, microsomal fraction 23% and nuclear fraction 15%. The quantity of phosphoproteins per unit quantity of protein was highest in the microsomal fraction and lowest (by a factor of nearly 50%) in the mitochondrial fraction. 2. Observations are reported on the nature of the nuclear subfraction believed from earlier work to contain a phosphoprotein sensitive to the effects of electrical pulses applied to cerebral slices in vitro. With respect to its content of phosphoprotein, cholesterol, ribonucleic acid and succinate-dehydrogenase activity, the subfraction resembles the nerve-ending fraction of the mitochondrial fraction, from which it appears to be derived by cross-contamination. Electron microscopy tended to confirm this impression. Reasons are adduced for discounting the earlier claim that the sensitive phosphoprotein is contained in a new subcellular structure distinct from nuclei, mitochondria or microsomes.

SUBMITTER: TREVOR AJ

PROVIDER: S-EPMC1206820 | biostudies-other | 1965 Jun

REPOSITORIES: biostudies-other

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Project description:BackgroundCLIC1 is a chloride channel whose cellular role remains uncertain. The distribution of CLIC1 in normal tissues is largely unknown and conflicting data have been reported regarding the cellular membrane fraction in which CLIC1 resides.ResultsNew antisera to CLIC1 were generated and were found to be sensitive and specific for detecting this protein. These antisera were used to investigate the distribution of CLIC1 in mouse tissue sections and three cultured cell lines. We find CLIC1 is expressed in the apical domains of several simple columnar epithelia including glandular stomach, small intestine, colon, bile ducts, pancreatic ducts, airway, and the tail of the epididymis, in addition to the previously reported renal proximal tubule. CLIC1 is expressed in a non-polarized distribution in the basal epithelial cell layer of the stratified squamous epithelium of the upper gastrointesitinal tract and the basal cells of the epididymis, and is present diffusely in skeletal muscle. Distribution of CLIC1 was examined in Panc1 cells, a relatively undifferentiated, non-polarized human cell line derived from pancreatic cancer, and T84 cells, a human colon cancer cell line which can form a polarized epithelium that is capable of regulated chloride transport. Digitonin extraction was used to distinguish membrane-inserted CLIC1 from the soluble cytoplasmic form of the protein. We find that digitonin-resistant CLIC1 is primarily present in the plasma membrane of Panc1 cells. In T84 cells, we find digitonin-resistant CLIC1 is present in an intracellular compartment which is concentrated immediately below the apical plasma membrane and the extent of apical polarization is enhanced with forskolin, which activates transepithelial chloride transport and apical membrane traffic in these cells. The sub-apical CLIC1 compartment was further characterized in a well-differentiated mouse renal proximal tubule cell line. The distribution of CLIC1 was found to overlap that of megalin and the sodium-phosphate cotransporter, NaPi-II, which are markers of the apical endocytic/recycling compartment in proximal tubule.ConclusionThe cell and tissue specific patterns of CLIC1 expression suggest it may play distinct roles in different cell types. In certain polarized columnar epithelia, it may play a role in apical membrane recycling.

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THE SUBCELLULAR DISTRIBUTION OF CEREBRAL PHOSPHOPROTEINS.

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