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Results for “Cytoplasmic Structures”

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At least 919 records · Page 51Linked to original sources
PubMed1995

Ultrastructural studies of neutral lipid localisation in Streptomyces.

Triacylglycerol is accumulated by Streptomyces spp. when grown in submerged culture. Ultrastructural studies using transmission electron microscopy (TEM), staining and freeze-fracture/freeze-etch procedures, and light microscopy confirmed the accumulation of neutral lipid by S. lividans and S. coelicolor during the stationary phase and its storage within membrane-bound globular structures within the cytoplasm. These structures were of various sizes and occupied up to approximately 80% of the total cell volume at that time. There was no evidence of such material within cells examined during the early exponential phase of growth. The globules visualised by TEM were electron-transparent since they comprised lipids containing saturated fatty acids that did not react with osmium tetroxide. The globules appeared to be bounded by a single membrane.

Freeze Etching↗
PubMed2005

RNA decapping inside and outside of processing bodies.

Decapping is a central step in eukaryotic mRNA turnover. Recent studies have identified several factors involved in catalysis and regulation of decapping. These include the following: an mRNA decapping complex containing the proteins Dcp1 and Dcp2; a nucleolar decapping enzyme, X29, involved in the degradation of U8 snoRNA and perhaps of other capped nuclear RNAs; and a decapping 'scavenger' enzyme, DcpS, that hydrolyzes the cap structure resulting from complete 3'-to-5' degradation of mRNAs by the exosome. Several proteins that stimulate mRNA decapping by the Dcp1:Dcp2 complex co-localize with Dcp1 and Dcp2, together with Xrn1, a 5'-to-3' exonuclease, to structures in the cytoplasm called processing bodies. Recent evidence suggests that the processing bodies may constitute specialized cellular compartments of mRNA turnover, which suggests that mRNA and protein localization may be integral to mRNA decay.

Animals↗
PubMed2002

An approach for high sensitivity detection of breast cancer by analysis of changes in structure of the cytoplasmic matrix of lymphocytes specifically induced by a specific breast tumour antigen (MUC-l/SEC).

An alternative procedure for detection breast cancer was examined based on the observation that lymphocytes re-exposed in vitro to antigenic stimulation will change their intracellular structuredness as measured by polarization of fluorescent light emitted by fluorescein labeled cells (SCM test). The specific antigen MUC-l/SEC was used to elicit such response in lymphocytes of patients with and without breast cancer. Eighty-five samples with breast cancer were tested, of which 72 were correctly diagnosed. Of the 41 controls, 35 were correctly identified as healthy subjects. The sensitivity of the test was 85% and the specificity was 81%. These results suggest a possible valuable method for screening and early detection of breast cancer. The clinical importance of this procedure lies in the ability to screen high-risk populations with higher specificity and sensitivity than any combinations of currently available procedures for breast cancer detection.

Journal Article↗
PubMed1980

Hepatitis B virus (HBV)-specific structures found in cytoplasmic extracts of cells producing HBV surface antigen (HBsAg) in vitro.

Two kinds of hepatitis B virus-specific particles are present in cytoplasmic extracts of hepatoma cells synthesizing hepatitis B virus (HBV) surface antigen. One class of particle contains the surface antigen of the virus, is 20S in size and has a buoyant density (in CsCl) of 1.2 g/ml. The second class of particle is a deoxyribonucleoprotein (CNP) with 1.3 g/ml buoyant density (in CsCl) and is 30S in size, the DNA of which contains HBV sequences thus proving virus specificity.

Cytoplasm↗