Patricia Román-Carrasco- Immunology PhD
- PostDoc Position at FH Campus Wien
Patricia Román-Carrasco
- Immunology PhD
- PostDoc Position at FH Campus Wien
About
9
Publications
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271
Citations
Introduction
Current institution
Education
March 2014 - October 2018
Publications
Publications (9)
The carbohydrate galactose-α-1,3-galactose (α-Gal) is expressed bound to proteins and lipids in all mammals, except for apes, old-world monkeys and humans. Instead, we produce IgM, IgG and IgA antibodies against α-Gal. Some individuals bitten by ticks develop IgE antibodies to α-Gal, which can cause allergic reactions to mammalian meat, known as α-...
The α-Gal syndrome is a delayed form of anaphylaxis following red meat consumption, where patients develop IgE antibodies against the carbohydrate moiety galactose-α-1,3-galactose (α-Gal). Another interesting fact of this disease is that the primary sensitization to α-Gal occurs after a tick bite. However, the mechanisms behind this unusual way of...
Red meat is a staple food of Western diets, but it can also induce IgE-mediated allergic reactions. Yet, apart from the heat-labile protein serum albumin and the carbohydrate α-Gal, the molecules involved in allergic reactions to red meat remain unknown.
IgE reactivity profiles of beef-sensitized individuals were analyzed by IgE-immunoblotting wit...
The α-Gal syndrome is a complex allergic disease characterized by the development of specific IgE antibodies against the carbohydrate galactose-α-1,3-galactose (α-Gal), an oligosaccharide present in cells and tissues of non-primate mammals. Individuals with IgE antibodies to α-Gal suffer from a delayed form of anaphylaxis following red meat consump...
We observed differences in the anti-carbohydrate IgG subclass antibody response in patients with and without IgE antibodies against carbohydrate moieties. Highest levels of IgG1 and IgG2 antibodies to α-Gal were detected in meat allergic patients that also showed high IgE levels to α-Gal. Interestingly, moderate levels of anti-α-Gal IgG1 antibodies...
Gal syndrome (AGS) is a type of anaphylactic reaction to mammalian meat characterized by an immunoglobulin (Ig)E immune response to the oligosaccharide α-Gal (Galα1-3Galβ1-4GlcNAc-R). Tick bites seems to be a prerequisite for the onset of the allergic disease in humans, but the implication of non-tick parasites in α-Gal sensitization has also been...
Background
Poultry meat can induce severe allergic reactions. So far, the molecules causing poultry meat allergy are largely unknown.
Objective
To identify and characterize poultry meat allergens.
Methods
Patients’ IgE reactivity profiles to chicken muscle were analyzed in immunoblots and proteins recognized by the majority of patients were subje...
Background
The oligosaccharide galactose‐α‐1,3‐galactose (α‐Gal), present in mammalian proteins and lipids, causes an unusual delayed allergic reaction 3 to 6 hours after ingestion of mammalian meat in individuals with IgE antibodies against α‐Gal. To better understand the delayed onset of allergic symptoms and investigate whether protein‐bound or...
The α-Gal syndrome (AGS) is a type of allergy characterized by an IgE antibody (Ab) response against the carbohydrate Galα1-3Galβ1-4GlcNAc-R (α-Gal), which is present in glycoproteins from tick saliva and tissues of non-catarrhine mammals. Recurrent tick bites induce high levels of anti-α-Gal IgE Abs that mediate delayed hypersensitivity to consume...
Questions
Questions (14)
Hi!
I want to deproteinize a sample and then apply the resulting deproteinized product to cells in culture (PBMCs). Which method can I use for this? I thought about TCA, but I am not sure whether, even after neutralization, the sample would be toxic for the cells.
Thank you in advance.
I want to stain liposomes with Dil (1,1'-Dioctadecyl-3,3,3,3',3'-Tetramethylindocarbocyanine Perchlorate) and evaluate their uptake by macrophages using flow cytometry.
I have read that the fluorescence of Dil is orange-red, and people who have used it in other techniques have told me that the sample gets a reddish/pink color.....
However, I have read that the peak wavelength of the emission spectrum of DiL is about 570 nm, on other sites I have seen that it is 514 nm but that would not be red!!! so I am a bit confused....
Using the blue laser in the flow cytometer.... where would the emission spectrum of the Dil be then? With what other fluorophore would it be comparable...to PE (FL2) for example?
Translated with www.DeepL.com/Translator (free version)
Hello! I have a question about lncRNAs:
most of them undergo post-translational processing (5’capping, polyadenylation, splicing) and also have an ORF... so why are they not translated into proteins?
Thank you!
I need to perform a blood draw from a patient and we are interested in keeping intact the VLDL present in the sample, because we want to do further analysis to them!... which would be the best collection tubes for this? which would affect the less to the lipoproteins? EDTA, heparin, Acid-citrate-dextrose tubes? or non of them would harm or affect the VLDL molecules?
Thanks in adavance!
Hi!
I am trying to develope a sandwich ELISA to detect a molecule in chylomicrons produced by Caco-2 cells.
I normally coat the ELISA plate with anti-ApoB antibody, block with serum albumin, then add either the basolateral media or the chylomicrons isolated in ultracentrifugation and last, the antibody against this other molecule I am looking for (plus the antibody carrying the HRP).
Every time I tried there´s lot of background. Those wells where the chylomicrons shouldn´t have my molecule, show also "positive values" and many times the values make no sense at all, increasing and decreasing with higher dilutions!
Other techniques to detect the molecule of interest worked, but the ELISA doesn´t work!
Should I take any special consideration if I try to do such ELISA with lipoproteins? do they degrade while incubating in the ELISA plate?
Thank you in advance!
Hello!
Quite often, when I ve done a TLC with immunostaining (I overlay with poly isobutyl methacrylate), I get in the picture those ugly huge bright/white areas instead a clean picture!
Does someone know why they do appear and how can I avoid it?
Thanks a lot!
Hi!
I wanted to perform ultracentrifugation to isolate chylomicrons and VLDL particles from culture media (colorless and low glucose DMEM).
I have some questions regarding the procedure:
- Could I do it just adjunting the density of the medium to 1.12 g/ml and centrifugate for 30min, 4hours and 20 hours?
- How can I know the density of the DMEM medium? just dividing the weight by the volume?
- I read in a protocol that it would be possible to stain the lipids of the lipoproteins by using a solution of Fat red 7b (2 mg/mL Fat Red 7B in 0.1 mol/L NaOH with 5 µLof Triton X-100). since I would like to recover intact chylomicrons and VLDL particles I wondered if this procedure could affect the lipoproteins and their structure.
Thanks a lot!
I am trying to perform some TLCs with immunostaining. After developing the TLC, and let it dry, I used to immerse the plate in a solution of 0.5% Polyisobutylmethacrylate in Hexane, last time I´ve tried with Diethylether as solvent, but still I have the same problem... either I lose the silica from the plate or I get some cracks on the surface of the plate!
How can I avoid this? What is the right procedure to overlay the plate to prevent this things?
Thanks a lot!
I have to use a Bio-Rad Criterion tris-tricine gel... but I am not sure if I should use the cathode/anode buffers needed for a tricine-gel electrophoresis or instead, the single buffer described in the "application guide" of Bio-Rad:
100 mM Tris; 100 mM Tricine
0.1% SDS
DO NOT ADJUST pH
Hello!
I did some in vitro digestions according to the INFOGEST (Minekus) protocol. When I analysed by immunobloting the different aliquots of the digestion I observed "background" signals that correspond to the size of the various digestive enzymes: pepsin but specially intense are the signals from trypsin and chymotrypsin (these last ones of a similar size of my protein of interest).
I found some publications where is described that enzymes such trypsin and chymotrypsin can actually break up the substrate and produce chemiluminiscence...
Does someone know a way to avoid this?
Thank you in advance!
