Amino Acid Sequence
Molecular Sequence Data
Intracellular localization of proteasomal degradation of a viral antigen. (1/198)To better understand proteasomal degradation of nuclear proteins and viral antigens we studied mutated forms of influenza virus nucleoprotein (NP) that misfold and are rapidly degraded by proteasomes. In the presence of proteasome inhibitors, mutated NP (dNP) accumulates in highly insoluble ubiquitinated and nonubiquitinated species in nuclear substructures known as promyelocytic leukemia oncogenic domains (PODs) and the microtubule organizing center (MTOC). Immunofluorescence revealed that dNP recruits proteasomes and a selective assortment of molecular chaperones to both locales, and that a similar (though less dramatic) effect is induced by proteasome inhibitors in the absence of dNP expression. Biochemical evidence is consistent with the idea that dNP is delivered to PODs/MTOC in the absence of proteasome inhibitors. Restoring proteasome activity while blocking protein synthesis results in disappearance of dNP from PODs and the MTOC and the generation of a major histocompatibility complex class I-bound peptide derived from dNP but not NP. These findings demonstrate that PODs and the MTOC serve as sites of proteasomal degradation of misfolded dNP and probably cellular proteins as well, and imply that antigenic peptides are generated at one or both of these sites. (+info)
Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae. (2/198)Rad23 is a member of a novel class of proteins that contain unprocessed ubiquitin-like (UbL) domains. We showed recently that a small fraction of Rad23 can form an interaction with the 26S proteasome. Similarly, a small fraction of Rpn10 is a component of the proteasome. Rpn10 can bind multiubiquitin chains in vitro, but genetic studies have not clarified its role in vivo. We report here that the loss of both Rad23 and Rpn10 results in pleiotropic defects that are not observed in either single mutant. rad23Delta rpn10Delta displays slow growth, cold sensitivity, and a pronounced G2/M phase delay, implicating overlapping roles for Rad23 and Rpn10. Although rad23Delta rpn10Delta displays similar sensitivity to DNA damage as a rad23Delta single mutant, deletion of RAD23 in rpn10Delta significantly increased sensitivity to canavanine, a phenotype associated with an rpn10Delta single mutant. A mutant Rad23 that is unable to bind the proteasome ((DeltaUbL)rad23) does not suppress the canavanine or cold-sensitive defects of rad23Delta rpn10Delta, demonstrating that Rad23/proteasome interaction is related to these effects. Finally, the accumulation of multiubiquitinated proteins and the stabilization of a specific proteolytic substrate in rad23Delta rpn10Delta suggest that proteasome function is altered. (+info)
Heat-shock protein 70 antisense oligomers enhance proteasome inhibitor-induced apoptosis. (3/198)Recent evidence supports a role for heat-shock protein 70 (hsp70) and the 26 S proteasome in regulating apoptosis, although the precise nature of their involvement is not known. In the present study, control and Bcl-x(L)-overexpressing, interleukin-3-dependent FL5.12 cell lines were treated with the proteasome inhibitor N-benzoyloxycarbonyl (Z)-Leu-Leu-leucinal (MG132). Basal proteasome activity appeared to be approximately 30% lower in bcl-x(L) cells compared with control cells using a substrate for the chymotrypsin-like activity. However, no difference in proteasome activity was detected using substrates for the trypsin-like or peptidylglutamyl peptide-hydrolysing activities. In addition, protein levels of the 20 S proteasome beta-subunit, as determined by Western blot analyses, were similar in control and bcl-x(L) cells, leading to the conclusion that proteasome activities were the same in these two cell lines. At 24 h after treatment with 500 nM MG132, apoptosis in bcl-x(L) cells (22%) was less than that observed in control cells (34%). Concomitantly, caspase activity in control cells, as assessed by N-acetyl-l-aspartyl-l-glutamyl-l-valyl-l-aspartyl-7-amino-4-methylcou marin (Ac-DEVD-AMC), was twice that observed in bcl-x(L) cells. By 48 h after MG132 treatment, apoptosis and caspase activity in bcl-x(L) cells were similar to those observed in control cells at 24 h. Proteasome inhibition stimulated increases in hsp70 protein levels in control and bcl-x(L) cells by 12 h, although the maximal increases found in bcl-x(L) cells were less. Blocking this induction with hsp70 antisense oligonucleotides potentiated apoptosis after treatment with MG132. Inhibiting caspase activity with a broad-spectrum caspase inhibitor, t-butoxycarbonyl-Asp(OMe)-fluoromethyl ketone, prevented MG132-induced apoptosis. The more specific caspase-3 inhibitor, Ac-DEVD-aldehyde, afforded less protection, although both inhibitors completely inhibited Ac-DEVD-AMC cleavage. These data indicate that both hsp70 and Bcl-x(L) provide some protection against proteasome inhibitor-induced apoptosis. (+info)
How an inhibitor of the HIV-I protease modulates proteasome activity. (4/198)The human immunodeficiency virus, type I protease inhibitor Ritonavir has been used successfully in AIDS therapy for 4 years. Clinical observations suggested that Ritonavir may exert a direct effect on the immune system unrelated to inhibition of the human immunodeficiency virus, type I protease. In fact, Ritonavir inhibited the major histocompatibility complex class I restricted presentation of several viral antigens at therapeutically relevant concentrations (5 microM). In search of a molecular target we found that Ritonavir inhibited the chymotrypsin-like activity of the proteasome whereas the tryptic activity was enhanced. In this study we kinetically analyzed how Ritonavir modulates proteasome activity and what consequences this has on cellular functions of the proteasome. Ritonavir is a reversible effector of proteasome activity that protected the subunits MB-1 (X) and/or LMP7 from covalent active site modification with the vinyl sulfone inhibitor(125)I-NLVS, suggesting that they are the prime targets for competitive inhibition by Ritonavir. At low concentrations of Ritonavir (5 microM) cells were more sensitive to canavanine but proliferated normally whereas at higher concentrations (50 microM) protein degradation was affected, and the cell cycle was arrested in the G(1)/S phase. Ritonavir thus modulates antigen processing at concentrations at which vital cellular functions of the proteasome are not yet severely impeded. Proteasome modulators may hence qualify as therapeutics for the control of the cytotoxic immune response. (+info)
Protein farnesylation is critical for maintaining normal cell morphology and canavanine resistance in Schizosaccharomyces pombe. (5/198)Protein farnesyltransferase (FTase) plays important roles in the growth and differentiation of eukaryotic cells. In this paper, we report the identification of the Schizosaccharomyces pombe gene cpp1(+) encoding the beta-subunit of FTase. The predicted amino acid sequence of the cpp1(+) gene product shares significant similarity with FTase beta-subunits from a variety of organisms. S. pombe FTase purified from E. coli exhibits high enzymatic activity toward the CAAX farnesylation motif substrates (where C represents cysteine, A represents aliphatic amino acid, and X is preferentially methionine, cysteine, serine, alanine, or glutamine) while showing little preference for CAAL geranylgeranylation motif substrates (where L represents leucine or phenylalanine). cpp1(+) is not essential for growth as shown by gene disruption; however, mutant cells exhibit rounded or irregular cell morphology. Expression of a geranylgeranylated mutant form, Ras1-CVIL, which can bypass farnesylation, rescues these morphological defects. We also identify a novel phenotype of cpp1(-) mutants, hypersensitivity to canavanine. This appears to be due to a 3-4-fold increase in the rate of arginine uptake as compared with wild-type cells. Expression of the geranylgeranylated mutant form of a novel farnesylated small GTPase, SpRheb, is able to suppress the elevated arginine uptake rate. These results demonstrate that protein farnesylation is critical for maintaining normal cell morphology through Ras1 and canavanine resistance through SpRheb. (+info)
Competition between a sterol biosynthetic enzyme and tRNA modification in addition to changes in the protein synthesis machinery causes altered nonsense suppression. (6/198)The Saccharomyces cerevisiae Mod5 protein catalyzes isopentenylation of A to i(6)A on tRNAs in the nucleus, cytosol, and mitochondria. The substrate for Mod5p, dimethylallyl pyrophosphate, is also a substrate for Erg20p that catalyzes an essential step in sterol biosynthesis. Changing the distribution of Mod5p so that less Mod5p is present in the cytosol decreases i(6)A on cytosolic tRNAs and alters tRNA-mediated nonsense suppression. We devised a colony color/growth assay to assess tRNA-mediated nonsense suppression and used it to search for genes, which, when overexpressed, affect nonsense suppression. We identified SAL6, TEF4, and YDL219w, all of which likely affect nonsense suppression via alteration of the protein synthesis machinery. We also identified ARC1, whose product interacts with aminoacyl synthetases. Interestingly, we identified ERG20. Midwestern analysis showed that yeast cells overproducing Erg20p have reduced levels of i(6)A on tRNAs. Thus, Erg20p appears to affect nonsense suppression by competing with Mod5p for substrate. Identification of ERG20 reveals that yeast have a limited pool of dimethylallyl pyrophosphate. It also demonstrates that disrupting the balance between enzymes that use dimethylallyl pyrophosphate as substrate affects translation. (+info)
The Saccharomyces cerevisiae Rheb G-protein is involved in regulating canavanine resistance and arginine uptake. (7/198)The new member of the Ras superfamily of G-proteins, Rheb, has been identified in rat and human, but its function has not been defined. We report here the identification of Rheb homologues in the budding yeast Saccharomyces cerevisiae (ScRheb) as well as in Schizosaccharomyces pombe, Drosophila melanogaster, zebrafish, and Ciona intestinalis. These proteins define a new class of G-proteins based on 1) their overall sequence similarity, 2) high conservation of their effector domain sequence, 3) presence of a unique arginine in their G1 box, and 4) presence of a conserved CAAX farnesylation motif. Characterization of an S. cerevisiae strain deficient in ScRheb showed that it is hypersensitive to growth inhibitory effects of canavanine and thialysine, which are analogues of arginine and lysine, respectively. Accordingly, the uptake of arginine and lysine was increased in the ScRheb-deficient strain. This increased arginine uptake requires the arginine-specific permease Can1p. The function of ScRheb is dependent on having an intact effector domain since mutations in the effector domain of ScRheb are incapable of complementing canavanine hypersensitivity of scrheb disruptant cells. Furthermore, the conserved arginine in the G1 box plays a role in the activity of ScRheb, as a mutation of this arginine to glycine significantly reduced the ability of ScRheb to complement canavanine hypersensitivity of ScRheb-deficient yeast. Finally, a mutation in the C-terminal CAAX farnesylation motif resulted in a loss of ScRheb function. This result, in combination with our finding that ScRheb is farnesylated, suggests that farnesylation plays a key role in ScRheb function. Our findings assign the regulation of arginine and lysine uptake as the first physiological function for this new farnesylated Ras superfamily G-protein. (+info)
Proteasome mutants, pre4-2 and ump1-2, suppress the essential function but not the mitochondrial RNase P function of the Saccharomyces cerevisiae gene RPM2. (8/198)The Saccharomyces cerevisiae nuclear gene RPM2 encodes a component of the mitochondrial tRNA-processing enzyme RNase P. Cells grown on fermentable carbon sources do not require mitochondrial tRNA processing activity, but still require RPM2, indicating an additional function for the Rpm2 protein. RPM2-null cells arrest after 25 generations on fermentable media. Spontaneous mutations that suppress arrest occur with a frequency of approximately 9 x 10(-6). The resultant mutants do not grow on nonfermentable carbon sources. We identified two loci responsible for this suppression, which encode proteins that influence proteasome function or assembly. PRE4 is an essential gene encoding the beta-7 subunit of the 20S proteasome core. A Val-to-Phe substitution within a highly conserved region of Pre4p that disrupts proteasome function suppresses the growth arrest of RPM2-null cells on fermentable media. The other locus, UMP1, encodes a chaperone involved in 20S proteasome assembly. A nonsense mutation in UMP1 also disrupts proteasome function and suppresses Deltarpm2 growth arrest. In an RPM2 wild-type background, pre4-2 and ump1-2 strains fail to grow at restrictive temperatures on nonfermentable carbon sources. These data link proteasome activity with Rpm2p and mitochondrial function. (+info)
Canavanine is an amino acid that is found in some plants, particularly in the almonds and seeds of certain legumes. It is structurally similar to the amino acid arginine but is toxic to many organisms, including humans. Canavanine can interfere with the function of enzymes involved in the synthesis of proteins, nucleic acids, and other important molecules, leading to a variety of adverse health effects.
In medical terms, exposure to canavanine can result in symptoms such as vomiting, diarrhea, weakness, and seizures. Prolonged or high-dose exposure may also lead to more serious complications, including liver and kidney damage. However, it is important to note that canavanine poisoning is relatively rare in humans, as the toxic effects of this compound are generally only seen at high levels of exposure.
If you suspect that you or someone else has been exposed to canavanine and is experiencing symptoms, it is important to seek medical attention promptly. A healthcare professional can evaluate the situation and provide appropriate treatment if necessary.
Arginine is an α-amino acid that is classified as a semi-essential or conditionally essential amino acid, depending on the developmental stage and health status of the individual. The adult human body can normally synthesize sufficient amounts of arginine to meet its needs, but there are certain circumstances, such as periods of rapid growth or injury, where the dietary intake of arginine may become necessary.
The chemical formula for arginine is C6H14N4O2. It has a molecular weight of 174.20 g/mol and a pKa value of 12.48. Arginine is a basic amino acid, which means that it contains a side chain with a positive charge at physiological pH levels. The side chain of arginine is composed of a guanidino group, which is a functional group consisting of a nitrogen atom bonded to three methyl groups.
In the body, arginine plays several important roles. It is a precursor for the synthesis of nitric oxide, a molecule that helps regulate blood flow and immune function. Arginine is also involved in the detoxification of ammonia, a waste product produced by the breakdown of proteins. Additionally, arginine can be converted into other amino acids, such as ornithine and citrulline, which are involved in various metabolic processes.
Foods that are good sources of arginine include meat, poultry, fish, dairy products, nuts, seeds, and legumes. Arginine supplements are available and may be used for a variety of purposes, such as improving exercise performance, enhancing wound healing, and boosting immune function. However, it is important to consult with a healthcare provider before taking arginine supplements, as they can interact with certain medications and have potential side effects.
Arginine-tRNA ligase is an enzyme that plays a crucial role in protein synthesis. Its primary function is to join arginine, an essential amino acid, to its corresponding transfer RNA (tRNA) molecule. This enzyme catalyzes the formation of a peptide bond between the arginine and the tRNA during translation, the process by which genetic information encoded in messenger RNA (mRNA) is converted into a protein sequence.
The reaction catalyzed by arginine-tRNA ligase involves two main steps:
1. Activation of arginine: The enzyme binds to and activates an arginine molecule by attaching adenosine triphosphate (ATP) to it, forming an arginine-AMP intermediate.
2. Transfer of arginine to tRNA: The activated arginine is then transferred from the arginine-AMP complex onto the appropriate tRNA molecule, releasing AMP and forming an ester bond between the carboxyl group of arginine and the 3'-hydroxyl group of the ribose moiety in the tRNA.
The resulting arginine-tRNA complex is now ready to participate in protein synthesis, where it will contribute to the formation of a polypeptide chain under the direction of mRNA. The enzyme's role in ensuring accurate amino acid attachment to their corresponding tRNAs is essential for maintaining proper protein folding and function.
There are two main types of arginine-tRNA ligases, based on their structure and mechanism:
1. Class I arginine-tRNA ligase (also known as ArgRS): This enzyme contains an alpha/beta Rossmann-fold domain that binds ATP and a catalytic domain with a characteristic HIGH motif. It follows the standard two-step reaction mechanism for class I aminoacyl-tRNA synthetases.
2. Class II arginine-tRNA ligase (also known as ArgQ): This enzyme has an alpha/beta/alpha sandwich fold and a distinct catalytic mechanism compared to Class I enzymes. It follows the three-step reaction mechanism for class II aminoacyl-tRNA synthetases, which includes an intermediate step of adenylate formation before transferring arginine to tRNA.
Both types of arginine-tRNA ligases are found in various organisms, including bacteria and eukaryotes. In humans, the Class I enzyme is encoded by the RARS gene, while the Class II enzyme is encoded by the QARS gene. Dysfunction or mutations in these genes can lead to neurological disorders and other health issues due to impaired protein synthesis and folding.
Beta-lipotropin (β-LPH) is a 91-amino acid polypeptide hormone that is derived from proopiomelanocortin (POMC), along with other bioactive peptides such as adrenocorticotropic hormone (ACTH), melanocyte-stimulating hormones (MSH), and β-endorphin. It is produced and released by the anterior pituitary gland in response to stress or corticotropin-releasing hormone (CRH) stimulation.
β-Lipotropin has been found to have several physiological functions, including the regulation of lipid metabolism, appetite control, and pain perception. It also exhibits opioid activity due to its ability to bind to opioid receptors in the brain, although its potency is much lower compared to other endogenous opioids like β-endorphin.
In addition to its role as a hormone, β-lipotropin has been studied for its potential therapeutic applications, particularly in the treatment of obesity and addiction. However, further research is needed to fully understand its mechanisms and clinical efficacy.
Peptide biosynthesis is the process by which cells synthesize peptides, short chains of amino acids. This process is mediated by enzymes called peptide synthetases, which catalyze the formation of peptide bonds between individual amino acids to create a longer chain. Peptide biosynthesis typically occurs through one of two pathways: ribosomal or non-ribosomal.
Ribosomal peptide biosynthesis involves the use of the cell's translational machinery, including the ribosome and transfer RNAs (tRNAs), to synthesize peptides from a messenger RNA (mRNA) template. This process is highly regulated and typically results in the production of small, linear peptides that are further modified by enzymes to create bioactive molecules such as hormones or neurotransmitters.
Non-ribosomal peptide biosynthesis (NRPS), on the other hand, is a more complex process that involves large multifunctional enzyme complexes called non-ribosomal peptide synthetases (NRPSs). These enzymes are capable of synthesizing a wide variety of structurally diverse peptides, including cyclic and branched peptides, as well as those containing non-proteinogenic amino acids. NRPSs typically consist of multiple modules, each responsible for adding a single amino acid to the growing peptide chain. The modular nature of NRPS systems allows for great diversity in the types of peptides that can be synthesized, making them important sources of bioactive molecules with potential therapeutic applications.
I'm sorry for any confusion, but there seems to be no established medical definition or recognition of a "Rauscher Virus" in human or veterinary medicine. It is possible that you may have misspelled or misremembered the name of a specific virus or medical term. If you have more information or context about where this term was used, I'd be happy to help you further research the topic.
Hemolymph is not a term typically used in human medicine, but it is commonly used in the study of invertebrates, particularly arthropods such as insects and crustaceans. Hemolymph is the fluid that circulates within the open circulatory system of these animals, serving multiple functions similar to both blood and lymphatic systems in vertebrates.
In simpler terms, hemolymph is a combined fluid that performs the functions of both blood and lymph in invertebrates. It serves as a transport medium for nutrients, waste products, hormones, and immune cells (hemocytes) throughout the body. Hemolymph does not contain red and white blood cells like human blood; instead, hemocytes are the primary cellular components responsible for immune responses and wound healing in these animals.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
A peptide fragment is a short chain of amino acids that is derived from a larger peptide or protein through various biological or chemical processes. These fragments can result from the natural breakdown of proteins in the body during regular physiological processes, such as digestion, or they can be produced experimentally in a laboratory setting for research or therapeutic purposes.
Peptide fragments are often used in research to map the structure and function of larger peptides and proteins, as well as to study their interactions with other molecules. In some cases, peptide fragments may also have biological activity of their own and can be developed into drugs or diagnostic tools. For example, certain peptide fragments derived from hormones or neurotransmitters may bind to receptors in the body and mimic or block the effects of the full-length molecule.
A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.
Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:
1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.
Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.
In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.
The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.
In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.
In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."
1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.
2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.
3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.
4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).
Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.
Into the Wild (book)
The Call of the Wild (2007 film)
Non-protein amino acid-accumulating clade
Non-proteinogenic amino acids
Plant defense against herbivory
Proteinogenic amino acid
Canavanine - Wikipedia
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Amino acid l-canavanine1
- This is because alfalfa seeds contain the toxic amino acid L-canavanine (arginine analog). (stillwater-medical.org)
- Alfalfa seeds and sprouts contain L-canavanine. (wikipedia.org)
- Alfalfa sprouts have made the news many times due to contamination with salmonella and e. coli, however even when not contaminated they contain a natural chemical called canavanine that has been found to cause a lupus-like autoimmune disease in an animal study. (losethebackpain.com)
- The sprouting process reduces the levels of canavanine, making the alfalfa sprouts a great source of essential nutrients. (growyourpantry.com)
- Alfalfa sprouts contain an amino acid called L-canavanine. (everyanswer.org)
- Garlic contains joene, thiosulfinates and allicin, which can mess with your immune system and trigger lupus flares The alfalfa contain L-canavanine in its sprouts, and this is an amino acid that can also lead to symptom flares. (everyanswer.org)
- But studies show that L-canavanine, a nonprotein amino acid in alfalfa (in the seeds and sprouts), may cause lupus or make existing lupus worse. (stillwater-medical.org)
- In summary, while alfalfa hay is a great food for guinea pigs, alfalfa sprouts should be avoided due to the presence of canavanine. (blogdevt.com)
- Of note, L-canavanine in alfalfa sprouts has been implicated in causing lupus, and excess use should be avoided. (medscape.com)
- In this study, Emr and co-workers screened the collection of 4,652 knockout strains for improved sensitivity to canavanine, a toxic arginine analogue that enters the cellular through the arginine transporter Can1. (bioskinrevive.com)
- Combination of ADT with low doses of the natural arginine analog canavanine effectively sensitizes malignant cells to irradiation. (ox.ac.uk)
- NZB/W F1, NZB, and DBA/2 mice fed L-canavanine develop a syndrome similar to systemic lupus erythematosus, while BALB/c mice fed a steady diet of protein containing 1% canavanine showed no change in lifespan. (wikipedia.org)
- The L-canavanine in alfalfa has been linked to lupus-like symptoms in primates, including humans, and other auto-immune diseases. (wikipedia.org)
- Canavanine is a toxic compound found in alfalfa seeds. (juicingsecret.com)
- l-Canavanine, a structural analog of l-arginine, has recently been studied as an anticancer agent. (korea.ac.kr)
- The results presented here may provide a basis for the design of new anticancer drugs, such as l-canavanine analogs. (korea.ac.kr)
- L-canavanine has anticancer and antiviral activity and it is useful against the influenza virus and retroviruses. (medicoherbs.co.za)
- Canavanine is accumulated primarily in the seeds of the organisms which produce it, where it serves both as a highly deleterious defensive compound against herbivores (due to cells mistaking it for arginine) and a vital source of nitrogen for the growing embryo. (wikipedia.org)
- The toxicity of canavanine may be enhanced under conditions of protein starvation, and canavanine toxicity, resulting from consumption of Hedysarum alpinum seeds with a concentration of 1.2% canavanine weight/weight, has been implicated in the death of a malnourished Christopher McCandless. (wikipedia.org)
- Dioclea megacarpa seeds contain high levels of canavanine. (wikipedia.org)
- 2015). "Presence of l-canavanine in Hedysarum alpinum seeds and its potential role in the death of Christopher McCandless. (wikipedia.org)
- The seeds contain a compound known as canavanine. (growyourpantry.com)
- Sutherlandia seeds contain canavanine, an amino acid with anti-tumourigenic properties which accounts for plants traditional medicinal use. (capemountainoils.co.za)
- Yeast strains impaired in the endocytic removal of plasma-membrane proteins accumulated Can1 at the plasma membrane, leading to unwanted transporter activity (uptake of toxic canavanine) and impaired development. (bioskinrevive.com)
- While they are high in nutrients like vitamin C and calcium, they also contain a compound called canavanine. (blogdevt.com)
- A wild type strain was exposed to the selective pressure canavanine for various lengths of time, incubated with an oxidation-specific dye (CellRox Green) and analyzed using fluorescence microscopy. (plu.edu)
- These larvae fastidiously avoid incorporation of L-canavanine into their nascent proteins (presumably by virtue of highly discriminatory arginine-tRNA ligase, the enzyme responsible for the first step in the incorporation of arginine into proteins). (wikipedia.org)
- In this insect, the level of radiolabeled L-canavanine incorporated into newly synthesized proteins is barely measurable. (wikipedia.org)
Contain high levels1
- Warnings: Alfalfa seed should never be ingested as they contain high levels of amino acid canavanine. (pharrah13.com)
- Thus, we investigated whether canavanine-induced growth arrest had a similar effect. (plu.edu)
- The particular strong supra-additive effect of ADT, canavanine and irradiation in both intrinsically more and less sensitive cancer cells supports the rational of ER stress pathways as novel target for improving multi-modal metabolic anti-cancer therapy. (ox.ac.uk)
- Similar interactions were formed upon binding to l-canavanine or l-arginine, but the interaction between Tyr312 and the oxygen of the oxyguanidino group was a little bit different. (korea.ac.kr)
- Canavanine in Cancerbush is an arginine mimic that documented anti-carcenogenic activity. (greenpharmonline.com)
- But comparative studies of the incorporation of radiolabeled L-arginine and L-canavanine have shown that in Manduca sexta, the ratio of incorporation is about 3 to 1. (wikipedia.org)
Detection of L-canavanine1
- Here we report that three gustatory receptors, GR8a, GR66a and GR98b function together in the detection of L-canavanine, a plant-derived insecticide. (elsevierpure.com)
- Alfalfa seeds and sprouts contain L-canavanine. (wikipedia.org)
- The L-canavanine in alfalfa has been linked to lupus-like symptoms in primates, including humans, and other auto-immune diseases. (wikipedia.org)
- Alfalfa contains canavanine, an amino acid and some essential minerals. (searchherbalremedy.com)
- Alfalfa sprouts also contain potent phytochemicals with cytotoxic and anticancer effects, such as alfalfa L-canavanine, β-carotene, and lutein 3-terpene derivatives and 5-flavonoid 14,15 . (anoasisofhealing.com)
- 3. Disseminated cryptococcosis in an AIDS patient caused by a canavanine-resistant strain of Cryptococcus neoformans var. (nih.gov)
- This is a mutation that results in canavanine resistance and maps near argP , but does not affect arginine transport. (yale.edu)
- In contrast, larvae of the tobacco hornworm Manduca sexta can only tolerate tiny amounts (1.0 microgram per kilogram of fresh body weight) of dietary canavanine because their arginine-tRNA ligase has little, if any, discriminatory capacity. (wikipedia.org)