Bacteriophage-host depth distribution patterns in soil are maintained after nutrient stimulation in vitro

2021 ◽  
Vol 787 ◽  
pp. 147589
Author(s):  
Xiaolong Liang ◽  
Yusong Wang ◽  
Ying Zhang ◽  
Bingxue Li ◽  
Mark Radosevich
Keyword(s):  
Depth Distribution ◽  
Distribution Patterns

scholarly journals Dihydropyridine receptor alpha subunits in normal and dysgenic muscle in vitro: expression of alpha 1 is required for proper targeting and distribution of alpha 2.

1991 ◽  
Vol 115 (5) ◽  
pp. 1345-1356 ◽  
Author(s):  
B E Flucher ◽  
J L Phillips ◽  
J A Powell
Keyword(s):  
Muscle Cells ◽  
Distribution Patterns ◽  
Receptor Alpha ◽  
Alpha Subunits ◽  
Nuclear Domain ◽  
T Tubules ◽  
Immunofluorescence Labeling ◽  
T System ◽  
Triad Junctions

We have studied the subcellular distribution of the alpha 1 and alpha 2 subunits of the skeletal muscle dihydropyridine (DHP) receptor with immunofluorescence labeling of normal and dysgenic (mdg) muscle in culture. In normal myotubes both alpha subunits were localized in clusters associated with the T-tubule membranes of longitudinally as well as transversely oriented T-tubules. The DHP receptor-rich domains may represent the sites where triad junctions with the sarcoplasmic reticulum are being formed. In cultures from dysgenic muscle the alpha 1 subunit was undetectable and the distribution patterns of the alpha 2 subunit were abnormal. The alpha subunit did not form clusters nor was it discretely localized in the T-tubule system. Instead, alpha 2 was found diffusely distributed in parts of the T-system, in structures in the perinuclear region and in the plasma membrane. These results suggest that an interaction between the two alpha subunits is required for the normal distribution of the alpha 2 subunit in the T-tubule membranes. Spontaneous fusion of normal non-muscle cells with dysgenic myotubes resulted in a regional expression of the alpha 1 polypeptide near the foreign nuclei, thus defining the nuclear domain of a T-tubule membrane protein in multi-nucleated muscle cells. Furthermore, the normal intracellular distribution of the alpha 2 polypeptide was restored in domains containing a foreign "rescue" nucleus; this supports the idea that direct interactions between the DHP receptor alpha 1 and alpha 2 subunits are involved in the organization of the junctional T-tubule membranes.

Gap junctions in human umbilical cord endothelial cells contain multiple connexins

1997 ◽  
Vol 272 (1) ◽  
pp. C117-C130 ◽  
Author(s):  
H. Van Rijen ◽  
M. J. van Kempen ◽  
L. J. Analbers ◽  
M. B. Rook ◽  
A. C. van Ginneken ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Lucifer Yellow ◽  
Umbilical Vein ◽  
Electrical Conductance ◽  
Distribution Patterns ◽  
Human Umbilical Cord ◽  
Dye Coupling ◽  
Gap Junctional

We investigated the expression pattern of gap junctional proteins (connexins, Cx) in situ and in vitro and their functional characteristics in cultured human umbilical vein endothelial cells (HUVEC) and cultured human umbilical artery endothelial cells (HUAEC). In both arteries and veins, Cx37, Cx40, and Cx43 could be detected in situ and in vitro (passages 2-4). Distribution patterns of Cx40 and Cx43 were homogeneous in situ but more heterogeneous in vitro. Cx37 is heterogeneously expressed both in situ and in vitro. Among most cells, no Cx37 staining could be detected; when present, it was found as bright spots between some clusters of cells. Cx40 was more abundant in cultured arterial endothelium than in cultured venous endothelium. Dye-coupling experiments with Lucifer yellow CH revealed extensive dye spread in HUVEC (15.2 +/- 0.4, mean +/- SE, n = 110) but was significantly restricted in HUAEC (9.8 +/- 0.3, n = 110). Electrophysiological gap junctional characteristics were determined in cultured HUVEC and HUAEC pairs by use of the dual voltage-clamp technique. In contrast to the dye-coupling experiments, mean macroscopic electrical conductance was significantly larger for HUAEC pairs (31.4 +/- 6.0 nS, n = 12) than for HUVEC pairs (16.6 +/- 2.8, n = 18). In HUVEC, we measured multiple single gap junctional channel conductances in the range of 19-75 pS. Interestingly, additional conductances of 80-200 pS were measured in HUAEC, possibly partially reflecting activity of channels formed of Cx40, which are more abundant in the cultured arterial endothelial cells.

scholarly journals Distribution of the Human Intracellular Serpin Protease Inhibitor 8 in Human Tissues

2002 ◽  
Vol 50 (11) ◽  
pp. 1443-1453 ◽  
Author(s):  
Merel C. Strik ◽  
Bellinda A. Bladergroen ◽  
Dorine Wouters ◽  
Walter Kisiel ◽  
Jan Hendrik Hooijberg ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Distribution Pattern ◽  
Nuclear Localization ◽  
Physiological Role ◽  
Distribution Patterns ◽  
Neuroendocrine Cells ◽  
Human Tissues ◽  
Cytoplasmic Staining

Ovalbumin-like serine protease inhibitors are mainly localized intracellularly and their in vivo functions are largely unknown. To elucidate their physiological role(s), we studied the expression of one of these inhibitors, protease inhibitor 8 (PI-8), in normal human tissues by immunohistochemistry using a PI-8-specific monoclonal antibody. PI-8 was strongly expressed in the nuclei of squamous epithelium of mouth, pharynx, esophagus, and epidermis, and by the epithelial layer of skin appendages, particularly by more differentiated epithelial cells. PI-8 was also expressed by monocytes and by neuroendocrine cells in the pituitary gland, pancreas, and digestive tract. Monocytes showed nuclear and cytoplasmic localization of PI-8, whereas neuroendocrine cells showed only cytoplasmic staining. In vitro nuclear localization of PI-8 was confirmed by confocal analysis using serpin-transfected HeLa cells. Furthermore, mutation of the P1 residue did not affect the subcellular distribution pattern of PI-8, indicating that its nuclear localization is independent of the interaction with its target protease. We conclude that PI-8 has a unique distribution pattern in human tissues compared to the distribution patterns of other intracellular serpins. Additional studies must be performed to elucidate its physiological role.

scholarly journals Nontuberculous Mycobacteria in Guadeloupe, Martinique, and French Guiana from 1994 to 2012

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Elisabeth Streit ◽  
Julie Millet ◽  
Nalin Rastogi
Keyword(s):  
French Guiana ◽  
Nontuberculous Mycobacteria ◽  
Clinical Specimen ◽  
Distribution Patterns ◽  
Drug Susceptibility ◽  
Geographical Variations ◽  
Common Group ◽  
Human Infections ◽  
Changes Over Time

Nontuberculous mycobacteria (NTM) are ubiquitous environmental organisms able to cause severe opportunistic human infections. Their distribution patterns are subject to geographical variations. This study describes their isolation frequencies from clinical specimen in the three French overseas departments of the Americas, namely, Guadeloupe, Martinique, and French Guiana during 1994–2012. A total of 651 strains from as many patients (one isolate per species per patient) were analysed regarding regional isolation patterns and potential pattern changes over time. TheMycobacterium aviumcomplex was the most common group of NTM in Guadeloupe and French Guiana. In Martinique it was the second most common after the rapidly growing mycobacteria.M. fortuitumwas the most commonly isolated species in all three departments. Some species (M. kansasii,M. xenopi, andM. terraecomplex) displayed a clear regional preference. Furthermore a change in isolation frequency was observed forM. intracellulare(increase) andM. kansasii(decrease) in Guadeloupe. In conclusion, marked regional differences in isolation frequencies of NTM species were observed in the study area. Results are discussed in context of variables such as study populations, risk factors, methodology employed, isolation from pulmonary versus sterile isolation sites (blood, urine, and CSF), and in vitro drug-susceptibility patterns.

scholarly journals Rad51 and Dmc1 Form Mixed Complexes Associated with Mouse Meiotic Chromosome Cores and Synaptonemal Complexes

1999 ◽  
Vol 147 (2) ◽  
pp. 207-220 ◽  
Author(s):  
Madalena Tarsounas ◽  
Takashi Morita ◽  
Ronald E. Pearlman ◽  
Peter B. Moens
Keyword(s):  
Protein Interactions ◽  
Meiotic Chromosome ◽  
Amino Acid Level ◽  
Distribution Patterns ◽  
Early Prophase ◽  
Protein Protein Interactions ◽  
Prophase I ◽  
Meiotic Chromosomes ◽  
Yeast Meiosis

The eukaryotic RecA homologues RAD51 and DMC1 function in homology recognition and formation of joint-molecule recombination intermediates during yeast meiosis. The precise immunolocalization of these two proteins on the meiotic chromosomes of plants and animals has been complicated by their high degree of identity at the amino acid level. With antibodies that have been immunodepleted of cross-reactive epitopes, we demonstrate that RAD51 and DMC1 have identical distribution patterns in extracts of mouse spermatocytes in successive prophase I stages, suggesting coordinate functionality. Immunofluorescence and immunoelectron microscopy with these antibodies demonstrate colocalization of the two proteins on the meiotic chromosome cores at early prophase I. We also show that mouse RAD51 and DMC1 establish protein–protein interactions with each other and with the chromosome core component COR1(SCP3) in a two-hybrid system and in vitro binding analyses. These results suggest that the formation of a multiprotein recombination complex associated with the meiotic chromosome cores is essential for the development and fulfillment of the meiotic recombination process.

scholarly journals The Neurotransmitter Receptor Architecture of the Mouse Olfactory System

2021 ◽  
Vol 15 ◽  
Author(s):  
Kimberley Lothmann ◽  
Katrin Amunts ◽  
Christina Herold
Keyword(s):  
Olfactory System ◽  
Piriform Cortex ◽  
Hierarchical Cluster ◽  
Distribution Patterns ◽  
Olfactory Cortex ◽  
Cluster Solution ◽  
Olfactory Tubercle ◽  
Neurotransmitter Receptor ◽  
Heterogeneous Expression

The uptake, transmission and processing of sensory olfactory information is modulated by inhibitory and excitatory receptors in the olfactory system. Previous studies have focused on the function of individual receptors in distinct brain areas, but the receptor architecture of the whole system remains unclear. Here, we analyzed the receptor profiles of the whole olfactory system of adult male mice. We examined the distribution patterns of glutamatergic (AMPA, kainate, mGlu2/3, and NMDA), GABAergic (GABAA, GABAA(BZ), and GABAB), dopaminergic (D1/5) and noradrenergic (α1 and α2) neurotransmitter receptors by quantitative in vitro receptor autoradiography combined with an analysis of the cyto- and myelo-architecture. We observed that each subarea of the olfactory system is characterized by individual densities of distinct neurotransmitter receptor types, leading to a region- and layer-specific receptor profile. Thereby, the investigated receptors in the respective areas and strata showed a heterogeneous expression. Generally, we detected high densities of mGlu2/3Rs, GABAA(BZ)Rs and GABABRs. Noradrenergic receptors revealed a highly heterogenic distribution, while the dopaminergic receptor D1/5 displayed low concentrations, except in the olfactory tubercle and the dorsal endopiriform nucleus. The similarities and dissimilarities of the area-specific multireceptor profiles were analyzed by a hierarchical cluster analysis. A three-cluster solution was found that divided the areas into the (1) olfactory relay stations (main and accessory olfactory bulb), (2) the olfactory cortex (anterior olfactory cortex, dorsal peduncular cortex, taenia tecta, piriform cortex, endopiriform nucleus, entorhinal cortex, orbitofrontal cortex) and the (3) olfactory tubercle, constituting its own cluster. The multimodal receptor-architectonic analysis of each component of the olfactory system provides new insights into its neurochemical organization and future possibilities for pharmaceutic targeting.

scholarly journals Spexin and a novel cichlid-specific spexin paralog both inhibit FSH and LH through a specific galanin receptor (Galr2b) in tilapia

2019 ◽  
Author(s):  
Yaron Cohen ◽  
Krist Hausken ◽  
Yoav Bonfil ◽  
Michael Gutnick ◽  
Berta Levavi-Sivan
Keyword(s):  
Mammalian Species ◽  
Cichlid Fish ◽  
Peptide Hormone ◽  
Distribution Patterns ◽  
Cichlid Species ◽  
Amino Acid Peptide ◽  
Lh Cells ◽  
Pleiotropic Functions

AbstractSpexin (SPX) is a 14 amino acid peptide hormone that has pleiotropic functions across vertebrates, one of which is involvement in the brain-pituitary-gonad axis of fish. SPX(1) has been identified in each class of vertebrates, and a second SPX (named SPX2) has been found in some non-mammalian species. We have cloned two spexin paralogs, designated as Spx1a and Spx1b, from Nile tilapia (Oreochromis niloticus) that have varying tissue distribution patterns. Spx1b is a novel peptide only identified in cichlid fish, and is more closely related to Spx1 than Spx2 homologs as supported by phylogenetic, synteny, and functional analyses. Kisspeptin, Spx, and galanin (Gal) peptides and their corresponding kiss receptors and Gal receptors (Galrs), respectively, are evolutionarily related. Cloning of six tilapia Galrs (Galr1a, Galr1b, Galr2a, Galr2b, Galr type 1, and Galr type 2) and subsequent in vitro second-messenger reporter assays for Gαs, Gαq, and Gαi suggests that Gal and Spx activate Galr1a/Galr2a and Galr2b, respectively. A decrease in plasma follicle stimulating hormone and luteinizing hormone concentrations was observed with injections of Spx1a or Spx1b in vivo. Additionally, application of Spx1a to pituitary slices decreased the firing rate of LH cells, suggesting direct inhibition at the pituitary level. These data collectively suggest an inhibitory mechanism of action against the secretion of gonadotropins for a traditional and a novel spexin paralog in cichlid species.

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