scholarly journals RUBELLA INFECTION OF SYNOVIAL CELLS AND THE RESISTANCE OF CELLS DERIVED FROM PATIENTS WITH RHEUMATOID ARTHRITIS

1970 ◽  
Vol 131 (2) ◽  
pp. 367-375 ◽  
Author(s):  
Arthur I. Grayzel ◽  
Carolyn Beck

The mechanism of growth stimulation in allogeneic lymphocytes mixed in vitro was studied at the cell level by means of cytophotometric techniques. A pronounced increase in fluorescence intensity of fixed and acridine orange (AO) stained lymphocytes was observed as soon as after 1–3 hr in mixed culture. No increase in the amount of DNA took place during this time. The higher fluorescence intensity was due to an increased accessibility of AO binding sites in the deoxyribonucleoprotein (DNP) complex, most probably as a result of weakened bonds between the DNA and the protein moiety in the DNP complex. Similar DNP changes have been found in other systems of growth stimulation and may be one prerequisite for later induction of cellular synthetic processes. Increased AO binding only occurred when the lymphocyte donors were incompatible at the major histocompatibility locus (HL-A); there was no change in AO binding in cases of HL-A identity. The AO binding reaction probably reflects a specific recognition of HL-A antigens, whereas other antigenic discrepancies between the individuals do not seem to cause an analogous response.

1970 ◽  
Vol 131 (2) ◽  
pp. 355-366 ◽  
Author(s):  
J. Andersson ◽  
D. Killander ◽  
E. Möller ◽  
G. Möller

The mechanism of growth stimulation in allogeneic lymphocytes mixed in vitro was studied at the cell level by means of cytophotometric techniques. A pronounced increase in fluorescence intensity of fixed and acridine orange (AO) stained lymphocytes was observed as soon as after 1–3 hr in mixed culture. No increase in the amount of DNA took place during this time. The higher fluorescence intensity was due to an increased accessibility of AO binding sites in the deoxyribonucleoprotein (DNP) complex, most probably as a result of weakened bonds between the DNA and the protein moiety in the DNP complex. Similar DNP changes have been found in other systems of growth stimulation and may be one prerequisite for later induction of cellular synthetic processes. Increased AO binding only occurred when the lymphocyte donors were incompatible at the major histocompatibility locus (HL-A); there was no change in AO binding in cases of HL-A identity. The AO binding reaction probably reflects a specific recognition of HL-A antigens, whereas other antigenic discrepancies between the individuals do not seem to cause an analogous response.


2020 ◽  
Vol 48 (12) ◽  
pp. 030006052097142
Author(s):  
Xiao-qing Yang ◽  
Sheng-you Yu ◽  
Li Yu ◽  
Lin Ge ◽  
Yao Zhang ◽  
...  

Objective To investigate the mechanism through which tacrolimus, often used to treat refractory nephropathy, protects against puromycin-induced podocyte injury. Methods An in vitro model of puromycin-induced podocyte injury was established by dividing podocytes into three groups: controls, puromycin only (PAN group), and puromycin plus tacrolimus (FK506 group). Podocyte morphology, number, apoptosis rate and microtubule associated protein 1 light chain 3 alpha ( LC3) expression were compared. Results Puromycin caused podocyte cell body shrinkage and loose intercellular connections, but podocyte morphology in the FK506 group was similar to controls. The apoptosis rate was lower in the FK506 group versus PAN group. The low level of LC3 mRNA observed in untreated podocytes was decreased by puromycin treatment; however, levels of LC3 mRNA were higher in the FK506 group versus PAN group. Although LC3-I and LC3-II protein levels were decreased by puromycin, levels in the FK506 group were higher than the PAN group. Fewer podocyte autophagosomes were observed in the control and FK506 groups versus the PAN group. Cytoplasmic LC3-related fluorescence intensity was stronger in control and FK506 podocytes versus the PAN group. Conclusions Tacrolimus inhibited puromycin-induced mouse podocyte damage by regulating LC3 expression and enhancing autophagy.


2007 ◽  
Vol 27 (2) ◽  
pp. 157-164 ◽  
Author(s):  
Samuel Baron ◽  
Jessica Hernandez ◽  
Joseph Bekisz ◽  
Joyce Poast ◽  
Neil Goldman ◽  
...  

1998 ◽  
Vol 180 (5) ◽  
pp. 1135-1147 ◽  
Author(s):  
Scott W. Bearden ◽  
Teanna M. Staggs ◽  
Robert D. Perry

ABSTRACT The acquisition of iron is an essential component in the pathogenesis of Yersinia pestis, the agent of bubonic and pneumonic plague. A cosmid library derived from the genomic DNA ofY. pestis KIM6+ was used for transduction of anEscherichia coli mutant (SAB11) defective in the biosynthesis of the siderophore enterobactin. Recombinant plasmids which had a common 13-kb BamHI fragment were isolated from SAB11 transductants in which growth but not enterobactin synthesis was restored on media containing the iron chelator EDDA [ethylenediamine-di(o-hydroxyphenyl acetic acid)]. Subcloning and transposon mutagenesis revealed a 5.6-kb region, designated yfe, essential for SAB11 growth stimulation. In vitro transcription-translation analysis identified polypeptides of 18, 29.5, 32, and 33 kDa encoded by the yfe locus. Sequence analysis shows this locus to be comprised of five genes in two separate operons which have potential Fur-binding sequences in both promoters. A putative polycistronic operon, yfeABCD, is Fur regulated and responds to iron and manganese. A functional Fur protein is required for the observed manganese repression of this operon. This operon encodes polypeptides which have strong similarity to the ATP-binding cassette (ABC) family of transporters and include a periplasmic binding protein (YfeA), an ATP-binding protein (YfeB), and two integral membrane proteins (YfeC and -D), which likely function in the acquisition of inorganic iron and possibly other ions. The ∼21-kDa protein encoded by the separately transcribedyfeE gene may be located in the cell envelope, since ayfeE::TnphoA fusion is PhoA+. Mutations in this gene abrogate growth of SAB11 on iron-chelated media.


2006 ◽  
Vol 505-507 ◽  
pp. 667-672 ◽  
Author(s):  
Chih Hui Yang ◽  
Kuo Chin Lin ◽  
Yu Huai Chang ◽  
Yu Cheng Lin

This paper described and characterized the quantum dots (QDs) with/without the polymeric PLGA applied in MC3T3E-1 delivery. Neat QDs were treated with various solvents, temperatures, exposure time and concentration to evaluate their stability and efficacy. We found that the intensity degree of fluorescence spectra (QDs) in different solvents follows the order: ether > THF > acetone > chloroform > methanol. Importantly, the QDs become inactive after 8-hr dissolution in the solvents of ether, THF or chloroform. According to this result, acetone and methanol are ideal solvents for QDs. The optimum concentration range of QDs in acetone is 5 to 10 mg/mL. We found that no obvious difference of fluorescence intensity was detected in QDs stored respectively at 4 °C, 24 °C and 44 °C (8-hour). When QDs were exposed to UV light (312 nm) for 2 hr, serious decay of fluorescence intensity was observed. In order to extend the application of QDs in medical areas, we encapsulated them in individual biocompatible poly(d,l-lactide-co-glycolide) (PLGA) nanoparticles for in-vitro imaging of endocytosis in MC3T3E-1 cells. We demonstrated that the polymeric PLGA have the ability to permeate the cells for cellular internalization; the endocytotic activity could be enhanced by the polymeric QDs-encapsulated PLGA.


2007 ◽  
Vol 123 ◽  
pp. S172-S173
Author(s):  
Philippe Goyette ◽  
Todd Green ◽  
Paul de Bakker ◽  
Daniel Mirel ◽  
Christine Stevens ◽  
...  

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