Tissue and species-specific effects of small molecular weight nuclear RNA's on transcription in isolated mammalian nuclei

1981 ◽  
Vol 59 (5) ◽  
pp. 343-352 ◽  
Author(s):  
Wing-Cheong Liu ◽  
Roseline Godbout ◽  
Ernest Jay ◽  
Kenneth K.-Y. Yu ◽  
Margarida O. Krause
Keyword(s):  
Molecular Weight ◽  
Human Cells ◽  
Kidney Cells ◽  
Small Molecular Weight ◽  
Isolated Nuclei ◽  
Specific Effects ◽  
Specific Manner ◽  
Normal Human ◽  
Species Specific ◽  
Slab Gels

Small molecular weight nuclear RNA's (SnRNA's) purified from the 0.35 M NaCl extract of chromatin from human and monkey tissues have been found to stimulate transcription of chromatin in isolated nuclei in a tissue- and species-specific manner. While SnRNA from normal human cells (WI38 fibroblasts and placenta) stimulates homologous transcription to some extent, it has a greater activity on transcription of heterologous tissue of the same species and no activity on heterologous tissue of a different species (monkey kidney cells). Likewise SnRNA from monkey cells stimulates transcription of homologous chromatin but has no effect on human cells. Fractionation of the RNA's in polyacrylamide gradient slab gels revealed that in all cases the active RNA was 160–175 nucleotides in length. Our results are compatible with the hypothesis that the active RNA's are involved in the determination and maintenance of tissue differentiation by recognizing promoter or regulator sequences in the DNA and act at the level of the nucleosome to induce tissue-specific genes.

The Hepatic Chalone. I. Assay Method for the Hormone and Purification of the Rabbit Liver Chalone

1971 ◽  
Vol 49 (12) ◽  
pp. 1376-1383 ◽  
Author(s):  
W. G. Verly ◽  
Y. Deschamps ◽  
J. Pushpathadam ◽  
M. Desrosiers
Keyword(s):  
Molecular Weight ◽  
Dna Synthesis ◽  
Rabbit Liver ◽  
Dose Effect ◽  
Assay Method ◽  
Small Molecular Weight ◽  
Tissue Specific ◽  
Effect Relationship ◽  
Receptor Sites ◽  
Species Specific

Chalone from rabbit liver has been purified 450-fold; it is a polypeptide of small molecular weight. Its action on liver DNA synthesis is tissue-specific but not species-specific. The dose–effect relationship is in agreement with the theory of receptor sites in the hepatocytes with a low affinity for this hormone.

scholarly journals Respiratory Syncytial Virus (RSV) Fusion Protein Subunit F2, Not Attachment Protein G, Determines the Specificity of RSV Infection

2003 ◽  
Vol 77 (8) ◽  
pp. 4609-4616 ◽  
Author(s):  
Jörg Schlender ◽  
Gert Zimmer ◽  
Georg Herrler ◽  
Karl-Klaus Conzelmann
Keyword(s):  
Respiratory Syncytial Virus ◽  
Peripheral Blood Lymphocytes ◽  
Human Cells ◽  
Protein G ◽  
Human Beings ◽  
Protein Subunit ◽  
Attachment Protein ◽  
Specific Manner ◽  
Syncytial Virus ◽  
Species Specific

ABSTRACT Human respiratory syncytial virus (HRSV) and bovine RSV (BRSV) infect human beings and cattle in a species-specific manner. We have here analyzed the contribution of RSV envelope proteins to species-specific entry into cells. In contrast to permanent cell lines, primary cells of human or bovine origin, including differentiated respiratory epithelia, peripheral blood lymphocytes, and macrophages, showed a pronounced species-specific permissivity for HRSV and BRSV infection, respectively. Recombinant BRSV deletion mutants lacking either the small hydrophobic (SH) protein gene or both SH and the attachment glycoprotein (G) gene retained their specificity for bovine cells, whereas corresponding mutants carrying the HRSV F gene specifically infected human cells. To further narrow the responsible region of F, two reciprocal chimeric F constructs were assembled from BRSV and HRSV F1 and F2 subunits. The specificity of recombinant RSV carrying only the chimeric F proteins strictly correlated with the origin of the membrane-distal F2 domain. A contribution of G to the specificity of entry could be excluded after reintroduction of BRSV or HRSV G. Virus with F1 and G from BRSV and with only F2 from HRSV specifically infected human cells, whereas virus expressing F1 and G from HRSV and F2 from BRSV specifically infected bovine cells. The introduction of G enhanced the infectivities of both chimeric viruses to equal degrees. Thus, the role of the nominal attachment protein G is confined to facilitating infection in a non-species-specific manner, most probably by binding to cell surface glycosaminoglycans. The identification of the F2 subunit as the determinant of RSV host cell specificity facilitates identification of virus receptors and should allow for development of reagents specifically interfering with RSV entry.

Non-species-specific effects of unacylated homoserine lactone and hexylresorcinol, low molecular weight autoregulators, on the growth and development of bacteria

Microbiology ◽  
2006 ◽  
Vol 75 (4) ◽  
pp. 405-414 ◽  
Author(s):  
A. L. Mulyukin ◽  
S. N. Filippova ◽  
A. N. Kozlova ◽  
N. A. Surgucheva ◽  
T. I. Bogdanova ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Growth And Development ◽  
Homoserine Lactone ◽  
Low Molecular Weight ◽  
Specific Effects ◽  
Species Specific

Small Molecular Weight Vitamin B12 Binders in Normal Human Serum

Nature ◽  
1968 ◽  
Vol 217 (5125) ◽  
pp. 272-274 ◽  
Author(s):  
EVANGELOS GIZIS ◽  
LEO M. MEYER
Keyword(s):  
Molecular Weight ◽  
Vitamin B12 ◽  
Human Serum ◽  
Normal Human Serum ◽  
Small Molecular Weight ◽  
Normal Human

scholarly journals The translation inhibitor cycloheximide affects ribosome profiling data in a species-specific manner

2019 ◽  
Author(s):  
Puneet Sharma ◽  
Benedikt S. Nilges ◽  
Jie Wu ◽  
Sebastian A. Leidel
Keyword(s):  
Positional Information ◽  
Human Cells ◽  
Ribosome Profiling ◽  
Model Organisms ◽  
Specific Effects ◽  
Treatment Conditions ◽  
Yeast Data ◽  
Translation Inhibitor ◽  
Pre Treatment ◽  
Species Specific

AbstractRibosome profiling provides genome-wide snapshots of translation dynamics by determining ribosomal positions at sub-codon resolution. To maintain this positional information, the translation inhibitor cycloheximide (CHX) has been widely used to arrest translating ribosomes prior to library preparation. Several studies have reported CHX-induced biases in yeast data casting uncertainty about its continued use and questioning the accuracy of many ribosome profiling studies. However, the presence of these biases has not been investigated comprehensively in organisms other than Saccharomyces cerevisiae. Here, we use a highly standardized and optimized protocol to compare different CHX-treatment conditions in yeast and human cells. Our data suggest that unlike in S. cerevisiae, translating ribosomes in human cells are not susceptible to conformational restrictions by CHX. Furthermore, CHX-induced codon-specific effects on ribosome occupancy are not detectable in human cells nor in other model organisms including Schizosaccharomyces pombe and Candida albicans. In fact, we find that even in S. cerevisiae most biases can be avoided by omitting CHX pre-treatment, indicating that other parameters of library generation contribute to differences between ribosome profiling experiments. Together our findings provide a framework for researchers who plan their own ribosome profiling experiments or who analyze published datasets to draw judicious conclusions.

Analysis of Intrinsic Fibrinolysis in Human Plasma Induced by Dextran Sulfate

1992 ◽  
Vol 67 (04) ◽  
pp. 440-444 ◽  
Author(s):  
Hiroko Tsuda ◽  
Toshiyuki Miyata ◽  
Sadaaki Iwanaga ◽  
Tetsuro Yamamoto
Keyword(s):  
Molecular Weight ◽  
Human Plasma ◽  
Dextran Sulfate ◽  
Tissue Type ◽  
Factor Xii ◽  
Normal Human Plasma ◽  
High Molecular Weight Kininogen ◽  
Single Chain ◽  
Major Pathway ◽  
Normal Human

SummaryThe analysis of normal human plasma by fibrin autography revealed four species of plasminogen activator (PA) activity related to tissue-type PA, factor XII, prekallikrein and urokinase-type PA (u-PA). The u-PA activity increased significantly by incubating plasma with dextran sulfate. This increase was coincident with both the cleavage of factor XII and the complex formation of activated factor XII with its plasma inhibitors, which were determined by immunoblotting procedure. The dextran sulfate-dependent activation of u-PA required both factor XII and prekallikrein, but did not require either plasminogen or factor XI. High molecular weight kininogen was required only at a low concentration of dextran sulfate. Thus the results indicate that the factor XII and prekallikrein-mediated activation of single chain u-PA (scu-PA) operates as a major pathway of scu-PA activation in whole plasma in contact with dextran sulfate.

The Relation Between VIIIR:AG and VIII:C Studied with Two Antisera

1979 ◽  
Author(s):  
H. P. Muller ◽  
N. H. van Tilburg ◽  
R. M. Bertina ◽  
J. J. Veltkamp
Keyword(s):  
Molecular Weight ◽  
High Salt ◽  
Low Molecular Weight ◽  
Gel Chromatography ◽  
Specific Antibodies ◽  
Specific Effects ◽  
Normal Plasma ◽  
Coagulant Activity ◽  
Sterical Hindrance ◽  
Inhibitory Antibodies

FVIII was separated into low molecular weight FVIII (LMW FVIII) and high molecular weight FVIII (HMW FVIII) by gel chromatography in the presence of high salt concentration or by high salt elution of LMW FVIII from FVIII bound to anti HMW FVII-Sepharose. Specific antibodies were raised in rabbits against HMW FVIII and LMW FVIII. After removal of the contaminating anti HMW activities the rabbit anti LMW FVIII was still able to neutralize the FVIII coagulant activity of normal plasma and of IMW FVIII with canparable efficiency and it had no effect on the VIIIR:WF of FVIII in normal plasma or in HMW FVIII. Anti LMW FVIII does not bind to HMW FVIII and does not precipitate FVIII as tested by counter immunoelectrophoresis. Rabbit anti HMW FVIII precipitates FVIII in normal plasma, inhibits VIIIR:WF activity, while it has no effect on the FVIII coagulant activity of LMW FVIII. The coagulant activity of FVIII in normal plasma is slightly inhibited by anti HMW FVIII presumably by non-specific effects (sterical hindrance). It is concluded that inhibitory antibodies against VIII:C raised in rabbits recognize antigenic structures only present on LMW FVIII. Antibodies against HMW FVIII raised in rabbits appears to recognize structures only present on HMW FVIII.

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