Specific localization and quantification of biotin transport components in yeast by use of a biotin-conjugated, impermeant, electron-dense label

1978 ◽  
Vol 19 (1) ◽  
Author(s):  
EdwardA. Bayer ◽  
Ehud Skutelsky ◽  
T. Viswanatha ◽  
Meir Wilchek
Keyword(s):  
Specific Localization ◽  
Dense Label

Immunocytochemistry. A Review of Methodology for Electron Microscopic Applicaiton

1974 ◽  
Vol 32 ◽  
pp. 328-329
Author(s):  
Joseph E. Mazurkiewicz
Keyword(s):  
Electron Microscopy ◽  
Light Microscopy ◽  
Ultrastructural Level ◽  
Electron Microscopic ◽  
Biological Interest ◽  
Investigative Approach ◽  
Immunologic Activity ◽  
Dense Label

Immunocytochemistry is a powerful investigative approach in which one of the most exacting examples of specificity, that of the reaction of an antibody with its antigen, isused to localize tissue and cell specific molecules in situ. Following the introduction of fluorescent labeled antibodies in T950, a large number of molecules of biological interest had been studied with light microscopy, especially antigens involved in the pathogenesis of some diseases. However, with advances in electron microscopy, newer methods were needed which could reveal these reactions at the ultrastructural level. An electron dense label that could be coupled to an antibody without the loss of immunologic activity was desired.

Specific Localization of an Auto-inhibition Mechanism at Presynaptic Terminals of Identified Serotonergic Neurons

Neuroscience ◽  
2020 ◽  
Author(s):  
Miriam García-Ávila ◽  
Ximena Torres ◽  
Montserrat G. Cercós ◽  
Citlali Trueta
Keyword(s):  
Inhibition Mechanism ◽  
Serotonergic Neurons ◽  
Presynaptic Terminals ◽  
Specific Localization

scholarly journals Distinct p63 and p73 Protein Interactions Predict Specific Functions in mRNA Splicing and Polyploidy Control in Epithelia

Cells ◽  
2020 ◽  
Vol 10 (1) ◽  
pp. 25
Author(s):  
Julian M. Rozenberg ◽  
Olga S. Rogovaya ◽  
Gerry Melino ◽  
Nickolai A. Barlev ◽  
Alexander Kagansky
Keyword(s):  
Protein Interactions ◽  
Transcriptional Repression ◽  
Genome Stability ◽  
Spindle Assembly Checkpoint ◽  
Genotoxic Stress ◽  
Protein Protein Interactions ◽  
Proliferating Cells ◽  
P53 Family ◽  
Differentiated Cells ◽  
Specific Localization

Epithelial organs are the first barrier against microorganisms and genotoxic stress, in which the p53 family members p63 and p73 have both overlapping and distinct functions. Intriguingly, p73 displays a very specific localization to basal epithelial cells in human tissues, while p63 is expressed in both basal and differentiated cells. Here, we analyse systematically the literature describing p63 and p73 protein–protein interactions to reveal distinct functions underlying the aforementioned distribution. We have found that p73 and p63 cooperate in the genome stability surveillance in proliferating cells; p73 specific interactors contribute to the transcriptional repression, anaphase promoting complex and spindle assembly checkpoint, whereas p63 specific interactors play roles in the regulation of mRNA processing and splicing in both proliferating and differentiated cells. Our analysis reveals the diversification of the RNA and DNA specific functions within the p53 family.

scholarly journals Synapsin I (protein I), a nerve terminal-specific phosphoprotein. I. Its general distribution in synapses of the central and peripheral nervous system demonstrated by immunofluorescence in frozen and plastic sections.

1983 ◽  
Vol 96 (5) ◽  
pp. 1337-1354 ◽  
Author(s):  
P De Camilli ◽  
R Cameron ◽  
P Greengard
Keyword(s):  
Nervous System ◽  
Detailed Examination ◽  
Specific Protein ◽  
Nerve Cells ◽  
General Distribution ◽  
Synapsin I ◽  
Nervous Systems ◽  
Synaptic Region ◽  
Specific Localization ◽  
Peripheral Nervous Systems

Synapsin I (formerly referred to as protein I) is the collective name for two almost identical phosphoproteins, synapsin Ia and synapsin Ib (protein Ia and protein Ib), present in the nervous system. Synapsin I has previously been shown by immunoperoxidase studies (De Camilli, P., T. Ueda, F. E. Bloom, E. Battenberg, and P. Greengard, 1979, Proc. Natl. Acad. Sci. USA, 76:5977-5981; Bloom, F. E., T. Ueda, E. Battenberg, and P. Greengard, 1979, Proc. Natl. Acad. Sci. USA 76:5982-5986) to be a neuron-specific protein, present in both the central and peripheral nervous systems and concentrated in the synaptic region of nerve cells. In those preliminary studies, the occurrence of synapsin I could be demonstrated in only a portion of synapses. We have now carried out a detailed examination of the distribution of synapsin I immunoreactivity in the central and peripheral nervous systems. In this study we have attempted to maximize the level of resolution of immunohistochemical light microscopy images in order to estimate the proportion of immunoreactive synapses and to establish their precise distribution. Optimal results were obtained by the use of immunofluorescence in semithin sections (approximately 1 micron) prepared from Epon-embedded nonosmicated tissues after the Epon had been removed. Our results confirm the previous observations on the specific localization of synapsin I in nerve cells and synapses. In addition, the results strongly suggest that, with a few possible exceptions involving highly specialized neurons, all synapses contain synapsin I. Finally, immunocytochemical experiments indicate that synapsin I appearance in the various regions of the developing nervous system correlates topographically and temporally with the appearance of synapses. In two accompanying papers (De Camilli, P., S. M. Harris, Jr., W. B. Huttner, and P. Greengard, and Huttner, W. B., W. Schiebler, P. Greengard, and P. De Camilli, 1983, J. Cell Biol. 96:1355-1373 and 1374-1388, respectively), evidence is presented that synapsin I is specifically associated with synaptic vesicles in nerve endings.

scholarly journals Identification and Specific Localization of Tyrosine-Phosphorylated Proteins in Trypanosoma brucei

2009 ◽  
Vol 8 (4) ◽  
pp. 617-626 ◽  
Author(s):  
Isabelle R. E. Nett ◽  
Lindsay Davidson ◽  
Douglas Lamont ◽  
Michael A. J. Ferguson
Keyword(s):  
Trypanosoma Brucei ◽  
Tyrosine Kinases ◽  
Immunofluorescence Microscopy ◽  
Significant Proportion ◽  
Tyrosine Residues ◽  
Phosphorylated Proteins ◽  
Cell Extracts ◽  
Proteomics Approach ◽  
Specific Localization ◽  
Multicellular Organisms

ABSTRACT Phosphorylation on tyrosine residues is a key signal transduction mechanism known to regulate intercellular and intracellular communication in multicellular organisms. Despite the lack of conventional tyrosine kinases in the genome of the single cell organism Trypanosoma brucei, phosphorylation on trypanosomal protein tyrosine residues has been reported for this parasite. However, the identities of most of the tyrosine-phosphorylated proteins and their precise site(s) of phosphorylation were unknown. Here, we have applied a phosphotyrosine-specific proteomics approach to identify 34 phosphotyrosine-containing proteins from whole-cell extracts of procyclic form T. brucei. A significant proportion of the phosphotyrosine-containing proteins identified in this study were protein kinases of the CMGC kinase group as well as some proteins of unknown function and proteins involved in energy metabolism, protein synthesis, and RNA metabolism. Interestingly, immunofluorescence microscopy using anti-phosphotyrosine antibodies suggests that there is a concentration of tyrosine-phosphorylated proteins associated with cytoskeletal structures (basal body and flagellum) and in the nucleolus of the parasite. This localization of tyrosine-phosphorylated proteins supports the idea that the function of signaling molecules is controlled by their precise location in T. brucei, a principle well known from higher eukaryotes.

Tissue-specific localization of mitochondrial imidazoline-guanidinium receptive sites

1992 ◽  
Vol 219 (2) ◽  
pp. 335-338 ◽  
Author(s):  
Frédérique Tesson ◽  
Isabelle Limon ◽  
Angelo Parini
Keyword(s):  
Tissue Specific ◽  
Specific Localization

scholarly journals Metabolic compartmentalization in the human cortex and hippocampus: evidence for a cell- and region-specific localization of lactate dehydrogenase 5 and pyruvate dehydrogenase

2007 ◽  
Vol 8 (1) ◽  
Author(s):  
Jocelyn D Laughton ◽  
Philippe Bittar ◽  
Yves Charnay ◽  
Luc Pellerin ◽  
Enikö Kovari ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Pyruvate Dehydrogenase ◽  
Human Cortex ◽  
Specific Localization ◽  
A Cell
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