A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.
A metabolic disease characterized by the defective transport of CYSTINE across the lysosomal membrane due to mutation of a membrane protein cystinosin. This results in cystine accumulation and crystallization in the cells causing widespread tissue damage. In the KIDNEY, nephropathic cystinosis is a common cause of RENAL FANCONI SYNDROME.
Amino acid sequence in which two disulfide bonds (DISULFIDES) and their connecting backbone form a ring that is penetrated by a third disulfide bond. Members include CYCLOTIDES and agouti-related protein.
'Amino Acid Transport System y+', also known as System Y+, is a sodium-independent cationic amino acid transporter that mediates the uptake of primarily basic amino acids, such as arginine and lysine, into cells through a facilitated diffusion process.
An inherited disorder due to defective reabsorption of CYSTINE and other BASIC AMINO ACIDS by the PROXIMAL RENAL TUBULES. This form of aminoaciduria is characterized by the abnormally high urinary levels of cystine; LYSINE; ARGININE; and ORNITHINE. Mutations involve the amino acid transport protein gene SLC3A1.
A mercaptoethylamine compound that is endogenously derived from the COENZYME A degradative pathway. The fact that cysteamine is readily transported into LYSOSOMES where it reacts with CYSTINE to form cysteine-cysteamine disulfide and CYSTEINE has led to its use in CYSTINE DEPLETING AGENTS for the treatment of CYSTINOSIS.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
'Sulfur-containing amino acids' are a category of amino acids, the building blocks of proteins, that include methionine and cysteine, which contain sulfur atoms as part of their side chains, playing crucial roles in protein structure, enzyme function, and antioxidant defense.
A hereditary or acquired form of generalized dysfunction of the PROXIMAL KIDNEY TUBULE without primary involvement of the KIDNEY GLOMERULUS. It is usually characterized by the tubular wasting of nutrients and salts (GLUCOSE; AMINO ACIDS; PHOSPHATES; and BICARBONATES) resulting in HYPOKALEMIA; ACIDOSIS; HYPERCALCIURIA; and PROTEINURIA.
A continuous circle of peptide bonds, typically of 2-3 dozen AMINO ACIDS, so there is no free N- or C-terminus. They are further characterized by six conserved CYSTEINE residues that form CYSTINE KNOT MOTIFS.
A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
A radiation-protective agent that interferes with sulfhydryl enzymes. It may also protect against carbon tetrachloride liver damage.
Amino acid transporter systems capable of transporting neutral amino acids (AMINO ACIDS, NEUTRAL).
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A sulfur-containing essential L-amino acid that is important in many body functions.
Amino acid transporter systems capable of transporting basic amino acids (AMINO ACIDS, BASIC).
A plant genus of the family RUBIACEAE. Some species are used as an ingredient in Chinese and African traditional medicines. Members contain kalata B1, a macrocyclic peptide.
A structurally-related family of small proteins that form a stable tertiary fold pattern which is supported by a series of disulfide bonds. The arrangement of disulfide bonds between the CYSTEINE moieties results in a knotted structure which is unique to this family of proteins.
Eating of excrement by animal species.
Compounds containing the -SH radical.
**Maleates** are organic compounds that contain a carboxylic acid group and a hydroxyl group attached to adjacent carbon atoms, often used as intermediates in the synthesis of pharmaceuticals and other chemicals, or as drugs themselves, such as maleic acid or its salts.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
**Mercaptoethanol, also known as β-mercaptoethanol or BME, is an organosulfur compound with the formula HOCH2CH2SH, functionally serving as a reducing agent and a sulfhydryl group protector in biochemical and molecular biology applications.**
NATIONAL LIBRARY OF MEDICINE service for health professionals and consumers. It links extensive information from the National Institutes of Health and other reviewed sources of information on specific diseases and conditions.
A reagent commonly used in biochemical studies as a protective agent to prevent the oxidation of SH (thiol) groups and for reducing disulphides to dithiols.

N,N'-Diacetyl-L-cystine-the disulfide dimer of N-acetylcysteine-is a potent modulator of contact sensitivity/delayed type hypersensitivity reactions in rodents. (1/972)

Oral N-acetyl-L-cysteine (NAC) is used clinically for treatment of chronic obstructive pulmonary disease. NAC is easily oxidized to its disulfide. We show here that N,N'-diacetyl-L-cystine (DiNAC) is a potent modulator of contact sensitivity (CS)/delayed type hypersensitivity (DTH) reactions in rodents. Oral treatment of BALB/c mice with 0.003 to 30 micromol/kg DiNAC leads to enhancement of a CS reaction to oxazolone; DiNAC is 100 to 1000 times more potent than NAC in this respect, indicating that it does not act as a prodrug of NAC. Structure-activity studies suggest that a stereochemically-defined disulfide element is needed for activity. The DiNAC-induced enhancement of the CS reaction is counteracted by simultaneous NAC-treatment; in contrast, the CS reaction is even more enhanced in animals treated with DiNAC together with the glutathione-depleting agent buthionine sulfoximine. These data suggest that DiNAC acts via redox processes. Immunohistochemically, ear specimens from oxazolone-sensitized and -challenged BALB/c mice treated with DiNAC display increased numbers of CD8(+) cells. DiNAC treatment augments the CS reaction also when fluorescein isothiocyanate is used as a sensitizer in BALB/c mice; this is a purported TH2 type of response. However, when dinitrofluorobenzene is used as a sensitizer, inducing a purported TH1 type of response, DiNAC treatment reduces the reaction. Treatment with DiNAC also reduces a DTH footpad-swelling reaction to methylated BSA. Collectively, these data indicate that DiNAC in vivo acts as a potent and effective immunomodulator that can either enhance or reduce the CS or DTH response depending on the experimental conditions.  (+info)

The bspA locus of Lactobacillus fermentum BR11 encodes an L-cystine uptake system. (2/972)

BspA is a basic surface-exposed protein from Lactobacillus fermentum BR11. Sequence comparisons have shown that it is a member of family III of the solute binding proteins. It is 89% identical to the collagen binding protein, Cnb, from Lactobacillus reuteri. Compared with the database of Escherichia coli proteins, BspA is most similar to the L-cystine binding protein FliY. To investigate the function of BspA, mutants depleted for BspA were generated by homologous recombination with a temperature-sensitive plasmid. These mutants were significantly impaired in their abilities to take up L-cystine. Uptake rates of L-glutamine, L-histidine, and L-lysine, which are substrates for other binding proteins with similarity to BspA, were unaffected. Evidence was obtained that BspA is necessary for maximal resistance to oxidative stress. Specifically, inactivation of BspA causes defective growth in the presence of oxygen and sensitivity to paraquat. Measurements of sulfhydryl levels showed that incubation of L. fermentum BR11 with L-cystine resulted in increased levels of sulfhydryl groups both inside and outside the cell; however, this was not the case with a BspA mutant. The role of BspA as an extracellular matrix protein adhesin was also addressed. L. fermentum BR11 does not bind to immobilized type I collagen or laminin above background levels but does bind immobilized fibronectin. Inactivation of BspA did not significantly affect fibronectin binding; therefore, we have not found evidence to support the notion that BspA is an extracellular matrix protein binding adhesin. As BspA is most probably not a lipoprotein, this report provides evidence that gram-positive bacterial solute binding proteins do not necessarily have to be anchored to the cytoplasmic membrane to function in solute uptake.  (+info)

Degradation of hepatic zinc-thionein after parenteral zinc administration. (3/972)

A low-molecular-weight protein, zinc-thionein, a metallothionein, was implicated as having a regulatory function in zinc metabolism. The half-life (t 1/2) of hepatic zinc-thionein was determined by pulse-labelling with either L-[35S] cystine and/or 65Zn. In two experiments with L-[35S]cystine, the t 1/2 of zinc-thionein was 18h and 19h. Most of the soluble 35S-labelled hepatic proteins had a t 1/2 of 4 days. The t 1/2 of zinc-thionein calculated by using 65Zn was 20h. The close similarity between the calculated and measured t 1/2 values for zinc-thionein suggests that release of Zn2+ from zinc-thionein probably occurs simultaneously with degradation of the protein moiety.  (+info)

Stimulation of cystine uptake by nitric oxide: regulation of endothelial cell glutathione levels. (4/972)

Nitric oxide (NO) is known to produce some of its biological activity through modification of cellular thiols. Return of cellular thiols to their basal state requires the activity of the GSH redox cycle, suggesting important interactions between NO signaling and regulation of cellular redox status. Because continuous exposure to NO may lead to adaptive responses in cellular redox systems, we investigated the effects of NO on cellular GSH levels in vascular endothelial cells. Acute exposure (1 h) of cells to >1 mM S-nitroso-N-acetyl-penicillamine (SNAP) led to depletion of GSH. On the other hand, chronic exposure to lower concentrations of SNAP (+info)

Elevated expression of liver gamma-cystathionase is required for the maintenance of lactation in rats. (5/972)

Liver gamma-cystathionase activity increases in rats during lactation; its inhibition due to propargylglycine is followed by a significant decrease in lactation. This is reversible by N-acetylcysteine administration. To study the role of liver gamma-cystathionase and the intertissue flux of glutathione during lactation, we used lactating and virgin rats fed liquid diets. Virgin rats were divided into two groups as follows: one group was fed daily a diet containing the same amount of protein that was consumed the previous day by lactating rats (high protein diet-fed rats); the other virgin group was fed the normal liquid diet (control). The expression and activity of liver gamma-cystathionase were significantly greater in lactating rats and in high protein diet-fed virgin rats compared with control rats. The total glutathione [reduced glutathione (GSH) + oxidized glutathione (GSSG)] released per gram of liver did not differ in lactating rats or in high protein diet-fed rats, but it was significantly higher in these two groups than in control virgin rats. Liver size and the GSH + GSSG released by total liver were significantly higher in lactating rats than in high protein diet-fed virgin rats, and this difference was similar to the amount of glutathione taken up by the mammary gland (454.2 +/- 36.0 nmol/min). The uptake of total glutathione by the lactating mammary gland was much higher than the uptakes of free L-cysteine and L-cystine, which were negligible. These data suggest that the intertissue flux of glutathione is an important mechanism of L-cysteine delivery to the lactating mammary gland, which lacks gamma-cystathionase activity. This emphasizes the physiologic importance of the increased expression and activity of liver gamma-cystathionase during lactation.  (+info)

1H-NMR structural studies of a cystine-linked peptide containing residues 71-93 of transthyretin and effects of a Ser84 substitution implicated in familial amyloidotic polyneuropathy. (6/972)

The Ile-->Ser84 substitution in the thyroid hormone transport protein transthyretin is one of over 50 variations found to be associated with familial amyloid polyneuropathy, a hereditary type of lethal amyloidosis. Using a peptide analogue of the loop containing residue 84 in transthyretin, we have examined the putative local structural effects of this substitution using 1H-NMR spectroscopy. The peptide, containing residues 71-93 of transthyretin with its termini linked via a disulfide bond, was found to possess the same helix-turn motif as in the corresponding region of the crystallographically derived structure of transthyretin in 20% trifluoroethanol (TFE) solution. It therefore, represents a useful model with which to examine the effects of amyloidogenic substitutions. In a peptide analogue containing the Ile84-->Ser substitution it was found that the substitution does not greatly disrupt the overall three-dimensional structure, but leads to minor local differences at the turn in which residue 84 is involved. Coupling constant and NOE measurements indicate that the helix-turn motif is still present, but differences in chemical shifts and amide-exchange rates reflect a small distortion. This is in keeping with observations that several other mutant forms of transthyretin display similar subunit interactions and those that have been structurally analysed possess a near native structure. We propose that the Ser84 mutation induces only subtle perturbations to the transthyretin structure which predisposes the protein to amyloid formation.  (+info)

PCR random mutagenesis into Escherichia coli serine acetyltransferase: isolation of the mutant enzymes that cause overproduction of L-cysteine and L-cystine due to the desensitization to feedback inhibition. (7/972)

PCR random mutagenesis in the cysE gene encoding Escherichia coli serine acetyltransferase was employed to isolate the mutant enzymes that, due to a much less feedback inhibition by L-cysteine, cause overproduction of L-cysteine and L-cystine in the recombinant strains. The L-cysteine auxotrophic and non-utilizing E. coli strain was transformed with plasmids having the altered cysE genes. Then, several transformants overproducing L-cysteine were selected by detecting the halo formation of the L-cysteine auxotroph. The production test of amino acids and analysis of the catalytic property on the mutant enzymes suggest that the carboxy-terminal region of serine acetyltransferase plays an important role in the desensitization to feedback inhibition and the high level production of L-cysteine and L-cystine.  (+info)

Differential reconstitution of mitochondrial respiratory chain activity and plasma redox state by cysteine and ornithine in a model of cancer cachexia. (8/972)

The mechanism of wasting, as it occurs in malignant diseases and various etiologically unrelated conditions, is still poorly understood. We have, therefore, studied putative cause/effect relationships in a murine model of cancer cachexia, C57BL/6 mice bearing the fibrosarcoma MCA-105. The plasma of these mice showed decreased albumin and increased glutamate levels, which are typically found in practically all catabolic conditions. Skeletal muscles from tumor-bearing mice were found to have an abnormally low mitochondrial respiratory chain activity (mito.RCA) and significantly decreased glutathione (GSH) levels. The decrease in mito.RCA was correlated with an increase in the i.m. GSH disulfide/GSH ratio, the plasma cystine/thiol ratio, and the GSH disulfide/GSH ratio in the bile. This is indicative of a generalized shift in the redox state extending through different body fluids. Treatment of tumor-bearing mice with ornithine, a precursor of the radical scavenger spermine, reversed both the decrease in mito.RCA and the change in the redox state, whereas treatment with cysteine, a GSH precursor, normalized only the redox state. Treatment of normal mice with difluoromethyl-ornithine, a specific inhibitor of ornithine decarboxylase and spermine biosynthesis, inhibited the mito.RCA in the skeletal muscle tissue, thus illustrating the importance of the putrescine/spermine pathway in the maintenance of mito.RCA. Ornithine, cysteine, and N-acetyl-cysteine (NAC) also reconstituted the abnormally low concentrations of the GSH precursor glutamate in the skeletal muscle tissue of tumor-bearing mice. Higher doses, however, enhanced tumor growth and increased the plasma glucose level in normal mice. In the latter, cysteine and NAC also decreased i.m. catalase and GSH peroxidase activities. Taken together, our studies on the effects of ornithine, cysteine, and NAC illuminate some of the mechanistic pathways involved in cachexia and suggest targets for therapeutic intervention.  (+info)

Cystine is a naturally occurring amino acid in the body, which is formed from the oxidation of two cysteine molecules. It is a non-essential amino acid, meaning that it can be produced by the body and does not need to be obtained through diet. Cystine plays important roles in various biological processes, including protein structure and antioxidant defense. However, when cystine accumulates in large amounts, it can form crystals or stones, leading to conditions such as cystinuria, a genetic disorder characterized by the formation of cystine kidney stones.

Cystinosis is a rare, inherited metabolic disorder that affects primarily the eyes, kidneys, and liver. It is characterized by an abnormal accumulation of the amino acid cystine within lysosomes (cellular organelles responsible for breaking down and recycling waste products) due to a defect in the gene CTNS that encodes for a protein called cystinosin. This leads to the formation of crystals, which can cause cell damage and multi-organ dysfunction.

There are three main types of cystinosis:

1. Nephropathic or infantile cystinosis: This is the most severe form, with symptoms appearing within the first year of life. It primarily affects the kidneys, leading to Fanconi syndrome (a condition characterized by excessive loss of nutrients in urine), growth failure, and kidney dysfunction. If left untreated, it can progress to end-stage renal disease (ESRD) around the age of 10.
2. Intermediate cystinosis: This form presents during childhood with milder kidney involvement but can still lead to ESRD in adolescence or early adulthood. Eye and central nervous system abnormalities may also be present.
3. Non-nephropathic or ocular cystinosis: This is the mildest form, primarily affecting the eyes. Symptoms include photophobia (sensitivity to light), corneal opacities, and decreased vision. Kidney function remains normal in this type.

Treatment for cystinosis typically involves a combination of medications to manage symptoms and slow disease progression. Cysteamine therapy, which helps remove excess cystine from cells, is the primary treatment for all types of cystinosis. Regular monitoring and management of complications are essential to maintain quality of life and prolong survival.

Cystine knot motifs are a type of protein structure characterized by the formation of a unique knotted pattern through the linking of three conserved cysteine residues. In this structure, two of the cysteines form a disulfide bond, while the third crosses under and forms an additional disulfide bond with one of the first pair, creating a knot-like shape. This motif is found in a variety of proteins, including some that are involved in important biological processes such as cell signaling, wound healing, and tumor suppression. The cystine knot motif confers stability to these proteins and helps them maintain their function even under harsh conditions.

The amino acid transport system y+ is a type of sodium-independent cationic amino acid transporter that is responsible for the uptake of positively charged amino acids, such as arginine and lysine, into cells. It is a part of a larger family of amino acid transporters that are involved in the transport of various types of amino acids across cell membranes.

The y+ system is composed of several different transporter proteins, including rBAT/4F2hc heteromeric amino acid transporter (Cat1), and light chains such as y+LAT1, y+LAT2, and y+LAT3. These transporters are widely expressed in various tissues, including the small intestine, kidney, liver, and brain.

The y+ system plays important roles in various physiological processes, including protein synthesis, immune function, and neurotransmitter metabolism. Dysregulation of this transport system has been implicated in several diseases, such as cancer, neurological disorders, and kidney disease.

Cystinuria is a genetic disorder that affects the way the body handles certain amino acids, specifically cystine, arginine, lysine, and ornithine. These amino acids are normally reabsorbed in the kidneys and released into the bloodstream. However, people with cystinuria have a defect in the transport mechanism that causes large amounts of cystine to be excreted in the urine, where it can form stones in the urinary tract. These stones can cause pain, blockages, and infection. Cystinuria is inherited in an autosomal recessive manner, meaning that an individual must inherit two copies of the defective gene, one from each parent, to have the condition.

Cysteamine is a medication and a naturally occurring aminothiol compound, which is composed of the amino acid cysteine and a sulfhydryl group. It has various uses in medicine, including as a treatment for cystinosis, a rare genetic disorder that causes an accumulation of cystine crystals in various organs and tissues. Cysteamine works by reacting with cystine to form a compound that can be more easily eliminated from the body. It is available in oral and topical forms and may also be used for other indications, such as treating lung diseases and radiation-induced damage.

Cysteine is a semi-essential amino acid, which means that it can be produced by the human body under normal circumstances, but may need to be obtained from external sources in certain conditions such as illness or stress. Its chemical formula is HO2CCH(NH2)CH2SH, and it contains a sulfhydryl group (-SH), which allows it to act as a powerful antioxidant and participate in various cellular processes.

Cysteine plays important roles in protein structure and function, detoxification, and the synthesis of other molecules such as glutathione, taurine, and coenzyme A. It is also involved in wound healing, immune response, and the maintenance of healthy skin, hair, and nails.

Cysteine can be found in a variety of foods, including meat, poultry, fish, dairy products, eggs, legumes, nuts, seeds, and some grains. It is also available as a dietary supplement and can be used in the treatment of various medical conditions such as liver disease, bronchitis, and heavy metal toxicity. However, excessive intake of cysteine may have adverse effects on health, including gastrointestinal disturbances, nausea, vomiting, and headaches.

Sulfur-containing amino acids are a type of amino acid that contain sulfur atoms in their side chains. There are three sulfur-containing amino acids that are considered essential for human health: methionine, cysteine, and homocysteine.

Methionine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. It contains a sulfur atom in its side chain and plays important roles in various biological processes, including methylation reactions, protein synthesis, and detoxification.

Cysteine is a semi-essential amino acid, which means that it can be synthesized by the human body under normal conditions but may become essential during periods of growth or illness. It contains a sulfhydryl group (-SH) in its side chain, which allows it to form disulfide bonds with other cysteine residues and contribute to the stability and structure of proteins.

Homocysteine is a non-proteinogenic amino acid that is derived from methionine metabolism. It contains a sulfur atom in its side chain and has been linked to various health problems, including cardiovascular disease, when present at elevated levels in the blood.

Other sulfur-containing amino acids include taurine, which is not incorporated into proteins but plays important roles in bile acid conjugation, antioxidant defense, and neuromodulation, and cystathionine, which is an intermediate in methionine metabolism.

Fanconi syndrome is a medical condition that affects the proximal tubules of the kidneys. These tubules are responsible for reabsorbing various substances, such as glucose, amino acids, and electrolytes, back into the bloodstream after they have been filtered through the kidneys.

In Fanconi syndrome, there is a defect in the reabsorption process, causing these substances to be lost in the urine instead. This can lead to a variety of symptoms, including:

* Polyuria (excessive urination)
* Polydipsia (excessive thirst)
* Dehydration
* Metabolic acidosis (an imbalance of acid and base in the body)
* Hypokalemia (low potassium levels)
* Hypophosphatemia (low phosphate levels)
* Vitamin D deficiency
* Rickets (softening and weakening of bones in children) or osteomalacia (softening of bones in adults)

Fanconi syndrome can be caused by a variety of underlying conditions, including genetic disorders, kidney diseases, drug toxicity, and heavy metal poisoning. Treatment typically involves addressing the underlying cause, as well as managing symptoms such as electrolyte imbalances and acid-base disturbances.

Cyclotides are a group of naturally occurring cyclic peptides that contain a head-to-tail cyclized structure and a conserved cystine knot motif. They are produced by plants, particularly those in the Rubiaceae family, as a defense mechanism against herbivores and pathogens.

Cyclotides have unique structural features, including a circular arrangement of amino acids and a knotted pattern of disulfide bonds, which contribute to their stability and resistance to degradation. These properties make them attractive candidates for drug development and therapeutic applications.

In addition to their potential use as drugs, cyclotides have also been studied for their potential as insecticides, antimicrobial agents, and anti-cancer therapies. They have been shown to have potent activity against a variety of targets, including cancer cells, bacteria, fungi, and viruses.

Overall, the unique structural and functional properties of cyclotides make them an exciting area of research in the fields of medicinal chemistry, pharmacology, and drug discovery.

Glutathione is a tripeptide composed of three amino acids: cysteine, glutamic acid, and glycine. It is a vital antioxidant that plays an essential role in maintaining cellular health and function. Glutathione helps protect cells from oxidative stress by neutralizing free radicals, which are unstable molecules that can damage cells and contribute to aging and diseases such as cancer, heart disease, and dementia. It also supports the immune system, detoxifies harmful substances, and regulates various cellular processes, including DNA synthesis and repair.

Glutathione is found in every cell of the body, with particularly high concentrations in the liver, lungs, and eyes. The body can produce its own glutathione, but levels may decline with age, illness, or exposure to toxins. As such, maintaining optimal glutathione levels through diet, supplementation, or other means is essential for overall health and well-being.

Disulfides are a type of organic compound that contains a sulfur-sulfur bond. In the context of biochemistry and medicine, disulfide bonds are often found in proteins, where they play a crucial role in maintaining their three-dimensional structure and function. These bonds form when two sulfhydryl groups (-SH) on cysteine residues within a protein molecule react with each other, releasing a molecule of water and creating a disulfide bond (-S-S-) between the two cysteines. Disulfide bonds can be reduced back to sulfhydryl groups by various reducing agents, which is an important process in many biological reactions. The formation and reduction of disulfide bonds are critical for the proper folding, stability, and activity of many proteins, including those involved in various physiological processes and diseases.

Cystamine is a chemical compound that is formed in the body from the breakdown of cysteine, an amino acid. It exists as a disulfide bond-containing molecule, which can be reduced to form two molecules of cysteamine. Cystamine has been studied for its potential therapeutic effects in various medical conditions, including neurodegenerative disorders and cancer.

In the body, cystamine functions as an antioxidant and helps to regulate cellular processes such as apoptosis (programmed cell death) and autophagy (a process by which cells break down and recycle their own components). It has been shown to have neuroprotective effects in animal models of neurodegenerative diseases, such as Huntington's disease and Parkinson's disease.

Cystamine has also been investigated for its potential anticancer effects. It has been shown to induce apoptosis in various cancer cell lines, including leukemia, lung cancer, and colon cancer cells. Additionally, cystamine has been found to enhance the effectiveness of chemotherapy drugs in some studies.

Cystamine is available as a dietary supplement and is sometimes used as a treatment for cystinosis, a rare genetic disorder that causes an accumulation of cystine crystals in various organs of the body. However, more research is needed to fully understand the potential therapeutic uses and safety profile of cystamine.

Neutral amino acid transport systems refer to a group of membrane transporters that facilitate the movement of neutral amino acids across cell membranes. Neutral amino acids are those that have a neutral charge at physiological pH and include amino acids such as alanine, serine, threonine, valine, leucine, isoleucine, methionine, cysteine, tyrosine, phenylalanine, and tryptophan.

There are several different transport systems that have been identified for neutral amino acids, each with its own specificity and affinity for different amino acids. Some of the major neutral amino acid transport systems include:

1. System A: This transporter preferentially transports small, neutral amino acids such as alanine, serine, and threonine. It is found in many tissues, including the intestines, kidneys, and brain.
2. System B0+: This transporter preferentially transports large, neutral amino acids such as leucine, isoleucine, valine, methionine, and phenylalanine. It is found in many tissues, including the intestines, kidneys, and brain.
3. System L: This transporter preferentially transports large, neutral amino acids such as leucine, isoleucine, valine, methionine, and phenylalanine. It is found in many tissues, including the intestines, kidneys, and brain.
4. System y+: This transporter preferentially transports cationic amino acids such as lysine and arginine, but it can also transport some neutral amino acids. It is found in many tissues, including the intestines, kidneys, and brain.
5. System b0,+: This transporter preferentially transports cationic amino acids such as lysine and arginine, but it can also transport some neutral amino acids. It is found in many tissues, including the intestines, kidneys, and brain.

These transport systems play important roles in maintaining amino acid homeostasis in the body, as well as in various physiological processes such as protein synthesis, neurotransmitter synthesis, and cell signaling. Dysregulation of these transport systems has been implicated in several diseases, including cancer, neurological disorders, and metabolic disorders.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Methionine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. It plays a crucial role in various biological processes, including:

1. Protein synthesis: Methionine is one of the building blocks of proteins, helping to create new proteins and maintain the structure and function of cells.
2. Methylation: Methionine serves as a methyl group donor in various biochemical reactions, which are essential for DNA synthesis, gene regulation, and neurotransmitter production.
3. Antioxidant defense: Methionine can be converted to cysteine, which is involved in the formation of glutathione, a potent antioxidant that helps protect cells from oxidative damage.
4. Homocysteine metabolism: Methionine is involved in the conversion of homocysteine back to methionine through a process called remethylation, which is essential for maintaining normal homocysteine levels and preventing cardiovascular disease.
5. Fat metabolism: Methionine helps facilitate the breakdown and metabolism of fats in the body.

Foods rich in methionine include meat, fish, dairy products, eggs, and some nuts and seeds.

Amino acid transport systems are specialized cellular mechanisms responsible for the active transport of amino acids across cell membranes. These systems are essential for maintaining proper amino acid homeostasis within cells and organisms. They consist of several types of transporters that can be categorized based on their energy source, electrochemical gradient, substrate specificity, and functional characteristics.

The term 'basic' in this context typically refers to the fundamental understanding of these transport systems, including their structure, function, regulation, and physiological roles. Amino acid transport systems play a crucial role in various biological processes, such as protein synthesis, neurotransmission, cell signaling, and energy metabolism.

There are two primary types of amino acid transport systems:

1. **Na+-dependent transporters:** These transporters utilize the sodium gradient across the cell membrane to drive the uptake of amino acids. They can be further divided into subtypes based on their substrate specificity and functional properties, such as system A, system ASC, system B0, system B, system L, and system y+.
2. **Na+-independent transporters:** These transporters do not rely on the sodium gradient for amino acid transport. Instead, they use other energy sources like proton gradients or direct coupling to membrane potential. Examples of Na+-independent transporters include system L, system y+, and system x-AG.

Understanding the basic aspects of amino acid transport systems is essential for elucidating their roles in health and disease. Dysregulation of these systems has been implicated in various pathological conditions, such as neurological disorders, cancer, and metabolic diseases.

"Oldenlandia" is not a term that has a specific medical definition. It is a genus of flowering plants in the coffee family, Rubiaceae, and it includes over 200 species that are found primarily in tropical and subtropical regions around the world. Some species of Oldenlandia have been used in traditional medicine in various cultures, but there is limited scientific evidence to support their effectiveness or safety.

In modern medical contexts, if "Oldenlandia" is mentioned, it may refer to a specific plant species that has been studied for its potential medicinal properties. For example, Oldenlandia diffusa (also known as Hedyotis diffusa) has been investigated for its anti-inflammatory, antioxidant, and anticancer effects. However, it is important to note that the use of any plant or herbal remedy should be discussed with a qualified healthcare provider, as they can interact with other medications and have potential side effects.

Cystine-knot miniproteins, also known as "cyclic peptides" or "constrained peptides," are a class of small protein molecules that contain a unique structural motif called a cystine knot. This motif is formed by the presence of three intramolecular disulfide bonds that create a knotted structure, which confers stability and resistance to proteolytic degradation on these miniproteins.

Cystine-knot miniproteins are found in various organisms, including plants, animals, and microorganisms, and have diverse biological functions. Some cystine-knot miniproteins act as toxins or hormones, while others have been shown to have therapeutic potential as drugs or drug delivery agents.

Due to their small size, stability, and specificity, cystine-knot miniproteins are attractive candidates for the development of new drugs and diagnostic tools. They can be engineered to bind to specific targets with high affinity and selectivity, making them useful for a variety of applications in medicine and biotechnology.

Coprophagia is a medical term that refers to the consumption or eating of feces. This behavior is generally considered abnormal in humans and most other animals, but it is a natural part of the life cycle for some species such as certain insects and rodents. In animals, coprophagia can sometimes be a sign of an underlying medical condition, nutritional deficiency, or behavioral issue. In humans, coprophagia is often associated with mental health disorders such as pica or obsessive-compulsive disorder (OCD). It's important to note that coprophagia can pose serious health risks, including the transmission of diseases and parasites, so it should be addressed with a healthcare professional if it occurs.

Sulfhydryl compounds, also known as thiol compounds, are organic compounds that contain a functional group consisting of a sulfur atom bonded to a hydrogen atom (-SH). This functional group is also called a sulfhydryl group. Sulfhydryl compounds can be found in various biological systems and play important roles in maintaining the structure and function of proteins, enzymes, and other biomolecules. They can also act as antioxidants and help protect cells from damage caused by reactive oxygen species. Examples of sulfhydryl compounds include cysteine, glutathione, and coenzyme A.

"Maleate" is not a medical term in and of itself, but it is a chemical compound that can be found in some medications. Maleic acid or its salts (maleates) are used as a keratolytic agent in topical medications, which means they help to break down and remove dead skin cells. They can also be used as a preservative or a buffering agent in various pharmaceutical preparations.

Maleic acid is a type of organic compound known as a dicarboxylic acid, which contains two carboxyl groups. In the case of maleic acid, these carboxyl groups are located on a single carbon atom, which makes it a cis-conjugated diacid. This structural feature gives maleic acid unique chemical properties that can be useful in various pharmaceutical and industrial applications.

It's worth noting that maleic acid and its salts should not be confused with "maleate" as a gender-specific term, which refers to something related to or characteristic of males.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

Mercaptoethanol, also known as β-mercaptoethanol or BME, is not a medical term itself but is commonly used in laboratories including medical research. It is a reducing agent and a powerful antioxidant with the chemical formula HOCH2CH2SH.

Medical Definition:
Mercaptoethanol (β-mercaptoethanol) is a colorless liquid with an unpleasant odor, used as a reducing agent in biochemical research and laboratory experiments. It functions by breaking disulfide bonds between cysteine residues in proteins, allowing them to unfold and denature. This property makes it useful for various applications such as protein purification, enzyme assays, and cell culture.

However, it is important to note that Mercaptoethanol has a high toxicity level and should be handled with caution in the laboratory setting.

MedlinePlus is not a medical term, but rather a consumer health website that provides high-quality, accurate, and reliable health information, written in easy-to-understand language. It is produced by the U.S. National Library of Medicine, the world's largest medical library, and is widely recognized as a trusted source of health information.

MedlinePlus offers information on various health topics, including conditions, diseases, tests, treatments, and wellness. It also provides access to drug information, medical dictionary, and encyclopedia, as well as links to clinical trials, medical news, and patient organizations. The website is available in both English and Spanish and can be accessed for free.

Dithiothreitol (DTT) is a reducing agent, which is a type of chemical compound that breaks disulfide bonds between cysteine residues in proteins. DTT is commonly used in biochemistry and molecular biology research to prevent the formation of disulfide bonds during protein purification and manipulation.

Chemically, DTT is a small molecule with two sulfhydryl groups (-SH) that can donate electrons to oxidized cysteine residues in proteins, converting them to their reduced form (-S-H). This reaction reduces disulfide bonds and helps to maintain the solubility and stability of proteins.

DTT is also used as an antioxidant to prevent the oxidation of other molecules, such as DNA and enzymes, during experimental procedures. However, it should be noted that DTT can also reduce other types of bonds, including those in metal ions and certain chemical dyes, so its use must be carefully controlled and monitored.

... stones account for about 1-2% of kidney stone disease in adults. Cystine serves as a substrate for the cystine- ... Other isomers include d,d-cystine and the meso isomer d,l-cystine, neither of which is biologically significant. Cystine is ... "Cystine stones". UpToDate. Archived from the original on 26 February 2014. Retrieved 20 February 2014. Media related to Cystine ... In 1884, the German chemist Eugen Baumann found that when cystine was treated with a reducing agent, cystine revealed itself to ...
The growth factor cystine knot (GFCK) inhibitor cystine knot (ICK) common in spider and snail toxins Cyclic Cystine Knot, or ... Novel proteins are being added to the cystine knot motif family, also known as the C-terminal cystine knot (CTCK) proteins. ... "The Cystine Knot Motif in Toxins and Implications for Drug Design." Toxicon, vol. 39, no. 1, 2001, pp. 43-60., doi:10.1016/ ... A cystine knot is a protein structural motif containing three disulfide bridges (formed from pairs of cysteine residues). The ...
Other names in common use include cystine reductase (NADH), NADH-dependent cystine reductase, cystine reductase (NADH2), and ... L-cystine + NADH + H+ Thus, the two substrates of this enzyme are L-cysteine and NAD+, whereas its 3 products are L-cystine, ... In enzymology, a cystine reductase (EC 1.8.1.6) is an enzyme that catalyzes the chemical reaction 2 L-cysteine + NAD+ ⇌ {\ ... ROMANO AH, NICKERSON WJ (1954). "Cystine reductase of pea seeds and yeasts". J. Biol. Chem. 208 (1): 409-16. PMID 13174550. ...
... (CTA), also known as cystine trypticase agar, is a growth medium used for the identification of ... Cystine tryptic agar typically contains (w/v): 2.0 % casein 0.05 % L-cystine 0.5 % sodium chloride 0.05% sodium sulfite 0.25% ...
Knottins are one of three folds in the cystine knot motif; the other closely related knots are the growth factor cystine knot ( ... The growth factor cystine knot (GFCK) is similar to the ICK but its topology is such that it is the bond between the first and ... Cystine knot motifs are found frequently in nature in a plethora of plants, animals, and fungi and serve diverse functions from ... An inhibitor cystine knot (also known as ICK or Knottin) is a protein structural motif containing three disulfide bridges. ...
The systematic name of this enzyme class is glutathione:cystine oxidoreductase. Other names in common use include GSH-cystine ... In enzymology, a glutathione-cystine transhydrogenase (EC 1.8.4.4) is an enzyme that catalyzes the chemical reaction 2 ... the two substrates of this enzyme are glutathione and cystine, whereas its two products are glutathione disulfide and cysteine ... transhydrogenase, and NADPH-dependent GSH-cystine transhydrogenase. This enzyme participates in cysteine metabolism and ...
The reaction believed to be catalyzed by cystinosin is: Cystine (intralysosomal space) + H+ (intralysosomal space) → Cystine ( ... The lysosomal cystine transporter (LCT) family (TC# 2.A.43) is part of the TOG Superfamily and includes secondary transport ... The few that have been characterized transport Cystine (TC# 2.A.43.1.1), basic amino acids such as L-lysine and L-arginine (TC# ... The cells then take up cystine in a pmf-dependent process. Distant homologues include the Lec15/Lec35 suppressor, SL15, of ...
Cystine promotes the formation of cystine-dependent dwarf colonies. Bromothymol blue is the indicator used in the agar, it ... "55420 CLED Agar (Cystine-Lactose-Electrolyte Deficient Agar; Bromothymol-blue Lactose Cystine Agar)" (PDF). Fluka Analytical. ... CLED agar (cystine-lactose-electrolyte-deficient agar or medium) is a valuable non-inhibitory growth medium used in the ... It contains cystine and lactose and is electrolyte-deficient; the latter trait prevents the swarming of Proteus species. ...
But if there is a defect in the carrier protein, cystine is accumulated in lysosomes. As cystine is highly insoluble, when its ... The only symptom is photophobia due to cystine crystals in the cornea. Cystine crystals are hexagonal in shape and are ... The accumulation is caused by abnormal transport of cystine from lysosomes, resulting in a massive intra-lysosomal cystine ... the lysosomal membrane-specific transporter for cystine. Intracellular metabolism of cystine, as it happens with all amino ...
For example, those with cystinuria, cystinosis, and Fanconi syndrome may form stones composed of cystine. Cystine stone ... Cystine calculi are only faintly radiodense, while uric acid stones are usually entirely radiolucent. In people with a history ... Including cystine stone incidence of 1% Becker KL (2001). Principles and practice of endocrinology and metabolism (3 ed.). ... "Cystine stones". UpToDate. Archived from the original on 26 February 2014. Retrieved 20 February 2014. Bailey & Love's/25th/ ...
Examples include cystine from hydrolysis of hair, tryptophane from casein, histidine from red blood cells, and arginine from ... Gortner, R. A.; Hoffman, W. F. (1925). "l-Cystine". Organic Syntheses. 5: 39. doi:10.15227/orgsyn.005.0039. Cox, G.J.; King, H ...
Cystine tryptic agar "TSI Reactions". Retrieved 2008-11-17. "TSI". Archived from the original on 2012-12-12. Retrieved 2008-11- ...
Cystine tryptic agar Veron et al. Int. J. Syst. Bacteriol. 30::335 1959 "Acid Detection Test- Gonorrhea - STD information from ...
As the levels of cystine in the urine increase, it forms cystine crystals, resulting in kidney stones. Cystine crystals form ... People with cystine stones should consume 5 to 7 liters a day. The rationale behind alkalizing the urine is that cystine tends ... The goal is to increase the urine volume because the concentration of cystine in the urine is reduced which prevents cystine ... Penicillamine is a drug that acts to form a complex with cystine that is 50 times more soluble than cystine itself. ...
It removes the excessive cystine that builds up in cells of people with the disease. It is available by mouth (capsule and ... This ultimately leads to buildup of cystine in lysosomes, where it crystallizes and damages cells. Cysteamine enters lysosomes ... People with cystinosis lack a functioning transporter (cystinosin) which transports cystine from the lysosome to the cytosol. ... Shams F, Livingstone I, Oladiwura D, Ramaesh K (10 October 2014). "Treatment of corneal cystine crystal accumulation in ...
a Sun PD, Davies DR (1995). "The cystine-knot growth-factor superfamily". Annu Rev Biophys Biomol Struct. 24: 269-91. doi: ... "A structural superfamily of growth factors containing a cystine knot motif". Cell. 73 (3): 421-4. doi:10.1016/0092-8674(93) ...
Two crosslinked cysteines form a cystine molecule. Cysteine and methionine are generally produced by direct sulfurylation, but ... cystine cystathionine lanthionine djenkolic acid diaminopimelic acid In meteorites and in prebiotic experiments (e.g. Miller- ...
The selenium-selenium bond length is 2.321 Å, which is 14% longer than the disulfide bond in cystine at 2.040 Å. "L- ... "Crystal structure of seleno-L-cystine dihydrochloride". Acta Crystallogr. E. 71 (Pt 6): 726-729. doi:10.1107/S205698901501021X ...
Toxins, 2(12), 2851-2871.DOI:[4]. Craik, D. J., Daly, N. L., & Waine, C. (2001). The cystine knot motif in toxins and ... Nmbe.ch.[2]. Zhu, S., Darbon, H., Dyason, K., Verdonck, F., & Tytgat, J. (2003). Evolutionary origin of inhibitor cystine knot ... which demonstrate three disulfide bonds that assemble an inhibitor cystine knot (ICK) scaffold. Generally, ICK peptides are ...
This conformation is called a "cystine knot". BMP4 can form homodimers or heterodimers with similar BMPS. One example of this ...
Görbitz, C. H.; Levchenko, V.; Semjonovs, J.; Sharif, M. Y. (2015). "Crystal structure of seleno-L-cystine dihydrochloride". ...
"Reductive cleavage of cystine disulfides with tributylphosphine". Methods Enzymol. Methods in Enzymology. 47: 111-116. doi: ...
Maresca B, Jacobson E, Medoff G, Kobayashi G (September 1978). "Cystine reductase in the dimorphic fungus Histoplasma ...
Her research focused on metabolism, and her dissertation was on the intermediary metabolism of cystine. She spent the majority ... Stearns, Genevieve (1930). Studies on the intermediary metabolism of cystine (Thesis). Baltimore. OCLC 637167242. Boyd, Julian ...
"Redox imbalance in cystine/glutamate transporter-deficient mice". The Journal of Biological Chemistry. 280 (45): 37423-9. doi: ... The latter protein is required for the activity of the cystine/glutamate antiporter (2.A.3.8.5), which maintains cellular redox ...
... cystine, leucine, and isoleucine; 40 mg lysine hydrochloride; 30 mg serine; 20 mg each aspartic acid, glutamic acid, ...
The toxin belongs to the inhibitory cystine knot structural family (ICK) that has a core of disulfide bonds with four loops ... Disulfide bridges are made by forming a cysteine dimer, called cystine. Due to this, it has a high disulfide content, making ... Its structure belongs to the inhibitory cystine knot family. This is a structural motif that contains at least three disulfide ... They both share the inhibitor cystine knot motif. Their structure is 17% and 23% homologous, respectively Besides the ICK motif ...
At the same time, cysteine is oxidized into cystine. 2 C3H7NO2S + I2 → C6H12N2O4S2 + 2 I− + 2 H+ Similar to thiosulfate case, ...
... , sold under the brand name Thiola, is a medication used to control the rate of cystine precipitation and excretion in ... Tiopronin is indicated, in combination with high fluid intake, alkali, and diet modification, for the prevention of cystine ... Lindell A, Denneberg T, Hellgren E, Jeppsson JO, Tiselius HG (1995). "Clinical course and cystine stone formation during ...
Agouti signalling peptide adopts an inhibitor cystine knot motif. Along with the homologous Agouti-related peptide, these are ...
Cystine stones account for about 1-2% of kidney stone disease in adults. Cystine serves as a substrate for the cystine- ... Other isomers include d,d-cystine and the meso isomer d,l-cystine, neither of which is biologically significant. Cystine is ... "Cystine stones". UpToDate. Archived from the original on 26 February 2014. Retrieved 20 February 2014. Media related to Cystine ... In 1884, the German chemist Eugen Baumann found that when cystine was treated with a reducing agent, cystine revealed itself to ...
CAS Number: 53-89-3 Spec (Assay): 98.5% min Melting point: 99°C Application: Building Block Packaging: 25Kg Drum Chemical Drawing:
We have recently cloned, sequenced, and characterized a rat kidney cDNA (D2) that stimulates cystine as well as dibasic and ... Microinjection of in vitro transcribed D2H cRNA into Xenopus oocytes induced uptake of cystine as well as dibasic and neutral ... Cloning and chromosomal localization of a human kidney cDNA involved in cystine, dibasic, and neutral amino acid transport.. ... Cloning and chromosomal localization of a human kidney cDNA involved in cystine, dibasic, and neutral amino acid transport.. ...
D, Normalized sEPSC during baseline and cystine. See E for legend and n at each concentration of cystine. A representative 1 s ... 2D) were both reduced by cystine. In parallel with the dialysis data (Fig. 1A), the effect of cystine was biphasic with respect ... Cystine regulates glutamate levels and excitatory transmission. A, Cystine increased extracellular glutamate in NA slices, as ... Cystine increases extracellular glutamate. Restoring physiological levels of extracellular cystine (100-300 nm) (Baker et al., ...
Learn about the veterinary topic of Cystine-Binding Agents Used to Treat Urinary Disease in Animals. Find specific details on ... Cystine stones are dissolved by means of dietary modification, administration of cystine-binding agents, or urinary ... Cystine-Binding Agents Used to Treat Urinary Disease in Animals By Patricia M. Dowling , DVM, MSc, DACVIM, DACVCP, Department ... The Cystine-Binding Agent Allopurinol for Treatment of Urinary Disease in Animals Allopurinol is a synthetic isomer of ...
Ideal Ratios of Isoleucine, Methionine, Methionine Plus Cystine, Threonine, Tryptophan, and Valine Relative to Lysine for White ... Ideal Ratios of Isoleucine, Methionine, Methionine Plus Cystine, Threonine, Tryptophan, and Valine Relative to Lysine for White ... Ideal Ratios of Isoleucine, Methionine, Methionine Plus Cystine, Threonine, Tryptophan, and Valine Relative to Lysine for White ...
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antimicrobial peptide, beta-sheet, clotting factors, crystal-structure, hemocytes, immunology, inhibitory cystine-knot (ICK), ... The solution structure of horseshoe crab antimicrobial peptide tachystatin B with an inhibitory cystine-knot motif. Error ... The solution structure of horseshoe crab antimicrobial peptide tachystatin B with an inhibitory cystine-knot motif. ...
Objective To assess the effectiveness of L-cystine dimethyl ester (CDME) an inhibitor of cystine crystal growth for the ... indicating that CDME did not interfere with cystine metabolism. SEM analysis of cystine stones from your CDME group exhibited a ... Objective To assess the effectiveness of L-cystine dimethyl ester (CDME) an. * Post author By exposed ... Combined with the lack of observed adverse effects our findings cIAP2 support the use of CDME as a viable treatment for cystine ...
H-Cys-OH)2; L-CYSTINE; .β.,.β.-Diamino-.β.,.β.-dicarboxydiethyl disulfide; Cystin; 1-cystine; Nephrin; Dicysteine; l-cystin ... R,R)-cystine; h-(cys); (R,R)-3,3-Dithiobis(2-aminopropionicacid); (CYS)2; L-CYTISINE; [3H]-Cystine; ...
More information about cystine in vaccines coming soon. ...
Any cystine-supplem 페이지 정보. 작성자 xoyojadarux 작성일23-09-16 04:25 조회2회 댓글0건 관련링크. * https://oceanfrontjupiter.com/tretinoin/ 0회 연결 ...
Cystine is an amino acid that offers potential hydration and skin barrier benefits. Learn more at Paulas Choice. ... Cystine description Cystine is an amino acid that offers potential hydration and skin barrier benefits. ...
... lysosomal storage disorder caused by defective transport of the amino acid cystine out of lysosomes. The stored cystine is ... Used as a cystine-depleting agent in cystinosis. It is a weak base that enters the cystinotic lysosome and reacts with cystine ... Goal of therapy is to keep leukocyte cystine levels , 1 nmol/half-cystine/mg protein measured 5-6 h following administration of ... It converts cystine to cysteine-cysteamine mixed disulfides and reduces corneal cystine crystal accumulation. ...
Cystine is the oxidized disulfide form of cysteine (Cys) and is the predominant form of cysteine in the blood d… ... What does it mean if your Cystine result is too low?. Cystine may be low as a result of dietary protein insufficiency, ... Cystine is a major component of tissue antioxidant mechanisms.. - Suspect oxidative stress if: Significantly elevated cystine, ... High levels might be due to excessive dietary intake or impaired cystine metabolism. Converted to cysteine (reduced cystine) ...
Browse our selection of L-cystine reference standards for pharmaceuticals, chemicals, and other industries. Order now for fast ... Discover our range of L-cystine high-quality reference standards, expertly manufactured in-house for precise and reliable ... N,N-Diacetyl-L-cystine Bis(tert-Butyl) Diester-d6 L-cystine Stable Isotopes ... DL-Cystine-2,2,3,3,3,3-d6 L-cystine Stable Isotopes ... L-cystine Stable Isotopes CS-O-40541 L-Cystine-S34 L-cystine ...
What is L Cystine, When to take, how to take, health benefits, dosage, side effects, and customer reviews. ... Shop the Best L-Cystine Powder at Bulk Supplements. ... Cystine Benefits † Cystine is believed to play a role in ... Cystine Benefits † Cystine is believed to play a role in protein synthesis, supports the heart, cardiovascular health, and ... L-Cystine is an amino acid that supports the heart and contributes to a calm sense of well-being. It also aids memory and ...
Book Cystine Quantitative Urine Test in bharatpur online from Dr. B. Lal Lab at the best prices. ✔️Free Home Collection ✔ ... resulting from poor absorption and reabsorption of the amino acid cystine in the intestines and kidneys. This results in the ...
Anti Mouse Cystine/Glutamic acid transp. Manufactured by Gentaur. Gentaur is the biggest antibody manufacturer worldwide. ... Decrease Quantity of Anti Mouse Cystine/Glutamic acid transp. , Gentaur Increase Quantity of Anti Mouse Cystine/Glutamic acid ... Anti Mouse Cystine/Glutamic acid transp.. Mammalian amino acid transport system is consisted of large variety of transporters, ... Anti Mouse Cystine/Glutamic acid transp. , Gentaur. Rating Required Select Rating. 1 star (worst). 2 stars. 3 stars (average). ...
The only phenotypic manifestation of cystinuria is cystine urolithiasis, which often recurs throughout an affected individuals ... Cystinuria is an autosomal-recessive defect in reabsorptive transport of cystine and the dibasic amino acids ornithine, ... Effect of cystine-binding thiol drugs on urinary cystine capacity in patients with cystinuria. J Endourol. 2005 Apr. 19(3):429- ... Dent and Senior demonstrated that the solubility of cystine is pH-dependent. [18] The solubility of cystine in urine is ...
View top 100 beef products with cystine. Learn more about the nutrients your food contains and what they can do for your health ... fig 2. Beef Products with cystine rank 21 to 40. Beef Products Ranked 41 - 60 With Cystine. Click on a food to explore all of ... fig 3. Beef Products with cystine rank 41 to 60. Beef Products Ranked 61 - 63 With Cystine. Click on a food to explore all of ... Cystine supplements available online. Heres a few supplements available through Amazon that contain cystine. Please click on ...
Food, high content: Cystine. Display low content food. Cystine per 100 grams. ...
... Finfish and Shellfish Products ... In 100 g (Grams) of Mollusks, whelk, unspecified, cooked, moist heat there is 0.374 g of Cystine. ...
L-cystine supports the growth of dwarf coliform colony. Bromo thymol blue is the pH indicator which turns yellow at acidic pH. ... Cystine Lactose Electrolyte Deficient (CLED) agar is a type of differential medium generally used for isolation and enumeration ...
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CTNS cystinosin, lysosomal cystine transporter [Homo sapiens] CTNS cystinosin, lysosomal cystine transporter [Homo sapiens]. ... cystinosin, lysosomal cystine transporterprovided by HGNC. Primary source. HGNC:HGNC:2518 See related. Ensembl:ENSG00000040531 ... 2A43; Lysosomal Cystine Transporter. pfam04193. Location:128 → 185. PQ-loop; PQ loop repeat. ... 2A43; Lysosomal Cystine Transporter. pfam04193. Location:122 → 175. PQ-loop; PQ loop repeat. ...
This health supplement product contains high purity of placental extract powder, vitamin C, and cystine to help improving skin ... JBP - LNC placenta VC whitening + L- cystine supplement Regular price RM 313.00 ...
Cystine is some hardcore sh*t when it comes to hair products, and the structural changes it makes in your hair are permanent ( ... A cystine solution. This is a chemical solution thats applied to the hair for about 20 minutes. There are of course other ... Chemicals like the cystine solution can play havoc with your hair and scalps pH balance. Neutralizers bring them back to the ... After the cystine solution is washed out, your stylist will apply some conditioning treatment. As we said, Japanese hair ...
... find complete details about L-Cystine, L-Cystine - Hunan Huakang Biotech Inc. ... L-Cystine Product Name:L-Cystine. Botanical Source:. Part Used:. Specification:. Appearance:White crystalline powder ... L-Cystine is one of the important products the amino acid series. It is widely used in medical, chemical and food industries. ... L-Cystine is one of the important products the amino acid series. It is widely used in medical, chemical and food industries. ...
  • Cystine is the oxidized derivative of the amino acid cysteine and has the formula (SCH2CH(NH2)CO2H)2. (wikipedia.org)
  • Cystine is the disulfide derived from the amino acid cysteine. (wikipedia.org)
  • The presence of cystine in urine is often indicative of amino acid reabsorption defects. (wikipedia.org)
  • Cloning and chromosomal localization of a human kidney cDNA involved in cystine, dibasic, and neutral amino acid transport. (jci.org)
  • We have recently cloned, sequenced, and characterized a rat kidney cDNA (D2) that stimulates cystine as well as dibasic and neutral amino acid transport. (jci.org)
  • Microinjection of in vitro transcribed D2H cRNA into Xenopus oocytes induced uptake of cystine as well as dibasic and neutral amino acids in a pattern similar to that of rat D2 and rabbit rBAT. (jci.org)
  • Both neutral and dibasic amino acids inhibited the D2H-induced uptake of cystine. (jci.org)
  • Despite the morbidity associated with cystine urolithiasis treatments for cystinuria have not substantially changed in the past 30 years7 8 At the molecular level cystinuria is usually characterized by defective transport of cystine and dibasic amino acids in the kidney and small intestine7-9. (exposed-skin-care.net)
  • Cystine is an amino acid that offers potential hydration and skin barrier benefits. (paulaschoice.co.uk)
  • L-Cystine is an amino acid that supports the heart and contributes to a calm sense of well-being. (bulksupplements.com)
  • Cystinuria is an autosomal-recessive defect in reabsorptive transport of cystine and the dibasic amino acids ornithine, arginine, and lysine from the luminal fluid of the renal proximal tubule and small intestine. (medscape.com)
  • In 1993, Lee et al cloned a human complementary DNA, rBAT (renal basic amino acid transporter) in chromosome 2, encoding a transport protein for cystine and dibasic amino acids. (medscape.com)
  • The high-affinity system mediates uptake of 10% of L-cystine and the dibasic amino acids at the apical membrane of the straight third segment (S3) of the proximal tubule. (medscape.com)
  • Cystinuria is an inborn error of metabolism(autosomal recessive disease) resulting from poor absorption and reabsorption of the amino acid cystine in the intestines and kidneys. (blallab.com)
  • L-Cystine is one of the important products the amino acid series. (huakangsw.com)
  • Cystinosis is a rare, inherited disorder that affects the body's ability to process an amino acid called cystine. (medicinenet.com)
  • The great majority of the literature concerns the l,l-cystine, derived from l-cysteine. (wikipedia.org)
  • Typical thiols for this reaction are mercaptoethanol and dithiothreitol: (SCH2CH(NH2)CO2H)2 + 2 RSH → 2 HSCH2CH(NH2)CO2H + RSSR Because of the facility of the thiol-disulfide exchange, the nutritional benefits and sources of cystine are identical to those for the more-common cysteine. (wikipedia.org)
  • Cystine is quickly reduced to cysteine. (wikipedia.org)
  • citation needed] Cysteine is more easily absorbed by the body than cystine, so most supplements contain cysteine rather than cystine. (wikipedia.org)
  • N-acetyl-cysteine (NAC) is better absorbed than other cysteine or cystine supplements. (wikipedia.org)
  • It converts cystine to cysteine-cysteamine mixed disulfides and reduces corneal cystine crystal accumulation. (medscape.com)
  • Cystine is the oxidized disulfide form of cysteine (Cys) and is the predominant form of cysteine in the blood due to its greater relative stability. (healthmatters.io)
  • Converted to cysteine (reduced cystine) via a B2 and copper-dependent step. (healthmatters.io)
  • In 1954, while studying skin sensitivity to penicillin and its derivatives, Tabachnick et al noted that one of the degradation products of penicillin, penicillamine, reacted with cystine to form a mixed disulfide, penicillamine cysteine. (medscape.com)
  • After absorption, each molecule of cystine is intracellularly converted to 2 molecules of cysteine. (medscape.com)
  • DMEM:F12, 1:1 Mix without L-Cystine, without L-Cysteine hydrochloride, without L-Methionine, with Glucose with 4.7g/L NaHCO3, sterile filtered solution for cell culture. (genaxxon.com)
  • Specification: with L-Glutamine without L-Cystine without L-Cysteine x HCl without Methionine. (genaxxon.com)
  • Here you will find information and further literature on DMEM:F12, 1:1 Mix w/o L-Cystine, w/o L-Cysteine hydrochloride, w/o L-Methionine, with Glucose. (genaxxon.com)
  • Cells were cultured + cystine for 16 hour's at 37C and 5% CO2, or used immediately to determine GSH-reductase activity (GSH-R). Determination of cysteine and GSH levels in MBB-strained cells and derivitized culture supernatant was achieved via reverse phase high performance liquid chromatography (HPLC). (cdc.gov)
  • Both AM and LNC showed enhanced levels of cysteine when incubated with cystine. (cdc.gov)
  • DEP was found to interact directly with cystine, cysteine, and to a lesser extent with GSH. (cdc.gov)
  • Supplementation of cystine along with antioxidant nutrients, Nacetylcysteine, or cofactors involved in methionine metabolism may be beneficial. (healthmatters.io)
  • Cystine serves as a substrate for the cystine-glutamate antiporter. (wikipedia.org)
  • This transport system, which is highly specific for cystine and glutamate, increases the concentration of cystine inside the cell. (wikipedia.org)
  • In this system, the anionic form of cystine is transported in exchange for glutamate. (wikipedia.org)
  • Cystine increased glutamate efflux and decreased miniature EPSC (mEPSC) and spontaneous EPSC (sEPSC) frequency as well as evoked EPSC amplitude. (jneurosci.org)
  • Along these lines, our present goal was to evaluate the effect(s) of the fumarate ester and antipsoriatic agent monomethylfumarate (MMF) on the expression and functional activity of the cystine/glutamate exchanger SLC7A11 (system x c - ), a transport system critical to potentiation of antioxidant signaling in retina. (elsevierpure.com)
  • We have previously demonstrated that glutamate (Glu) suppresses cellular proliferation toward self-renewal through a mechanism associated with the depletion of intracellular GSH after promoting the retrograde operation of the bidirectional cystine/Glu antiporter in undifferentiated osteoblastic MC3T3-E1 cells. (elsevierpure.com)
  • These results suggest that Runx2 expression would be negatively regulated by the cystine/glutamate antiporter expressed by osteoblastic cells at the level of gene transactivation. (elsevierpure.com)
  • The conversion can be viewed as an oxidation: 2 HO2CCH(NH2)CH2SH + 0.5 O2 → (HO2CCH(NH2)CH2S)2 + H2O Cystine contains a disulfide bond, two amine groups, and two carboxylic acid groups. (wikipedia.org)
  • It is a weak base that enters the cystinotic lysosome and reacts with cystine, forming a mixed disulfide of half-cystine and cysteamine. (medscape.com)
  • In humans the excretion of high levels of cystine crystals can be indicative of cystinosis, a rare genetic disease. (wikipedia.org)
  • SEM analysis of cystine stones from your CDME group exhibited a change in crystal habit with numerous small crystals. (exposed-skin-care.net)
  • In addition to the oral product that is available, an ophthalmic product was approved by the FDA in October 2012 to decrease corneal cystine crystals, which develop with nephropathic cystinosis. (medscape.com)
  • Electron microscopic picture showing cystine crystals. (medscape.com)
  • Cystine crystals can accumulate in cells throughout your body, including your eyes. (medicinenet.com)
  • Cystine crystals can form in people with a rare inherited disorder called cystinosis. (medicinenet.com)
  • Using two smartphones to look for corneal cystine crystals. (cdc.gov)
  • Anti Mouse Cystine/Glutamic acid transp. (caslab.com)
  • Overall cystine excretion in PAC-1 urine was the same between the two groups (p = 0.23) indicating that CDME did not interfere with cystine metabolism. (exposed-skin-care.net)
  • Only 0.4% of the filtered cystine appears in the urine. (medscape.com)
  • Cystine Lactose Electrolyte Deficient (CLED) agar is a type of differential medium generally used for isolation and enumeration of bacteria from urine specimen form patients suspected of urinary tract infection. (microbesinfo.com)
  • Conversely, uric acid and cystine calculi are associated with acidic urine (although pH is more important for treatment than formation of cystine stones). (medscape.com)
  • The delayed-release capsule (Procysbi) allows twice daily dosing (ie, q12h), whereas the immediate-release capsule (Cystagon) has to be administered every 6 hours, including throughout the night, to prevent nocturnal accumulation of cystine. (medscape.com)
  • The accumulation of cystine can cause various serious health problems. (medicinenet.com)
  • The most severe form of cystinosis, which is characterized by the accumulation of cystine in the kidneys and other organs. (medicinenet.com)
  • Cystine stones account for about 1-2% of kidney stone disease in adults. (wikipedia.org)
  • After cystine stones have been dissolved, a prevention protocol can be instituted. (merckvetmanual.com)
  • Conclusions These data demonstrate that CDME promotes formation of small stones but does not prevent stone formation consistent with the hypothesis that CDME inhibits cystine crystal growth. (exposed-skin-care.net)
  • Stone formation secondary to cystinuria often presents in the first decade of life and the majority of patients have their first stone by the end of their teenage years4 5 Although rare cystine stones can lead to serious effects for patients because they are large and tend to recur often resulting in multiple treatments and progressive decline in renal function in pediatric and adult patients3-5. (exposed-skin-care.net)
  • Patients with cystine stones have a greater incidence of chronic kidney PAC-1 disease than patients suffering from the more common calcium oxalate stones6. (exposed-skin-care.net)
  • Cystine stones form in people who have an inherited condition called cystinuria . (healthline.com)
  • Among those with current stones, cystine patients scored lower than noncystine patients for total score and in two of four domains. (psu.edu)
  • Conclusions: Using a stone-specific questionnaire, patients with cystine stones have lower HRQOL compared with noncystine stone formers. (psu.edu)
  • Identifying and addressing specific areas of decrement in patients with cystine stones may improve disease management and patients' HRQOL. (psu.edu)
  • About 85% of the stones are composed of calcium, and the remainder are composed of various substances, including uric acid, cystine, or struvite. (msdmanuals.com)
  • Objective To assess the effectiveness of L-cystine dimethyl ester (CDME) an inhibitor of cystine crystal growth for the treatment of cystine urolithiasis in a knockout mouse model of cystinuria. (exposed-skin-care.net)
  • Used as a cystine-depleting agent in cystinosis. (medscape.com)
  • Cysteamine ophthalmic is a cystine-depleting agent indicated for corneal cystine crystal accumulation in patients with cystinosis. (medscape.com)
  • Cystinosis is treated with medications that help remove excess cystine from the body and prevent kidney damage. (medicinenet.com)
  • Cystinuria, with subsequent cystine urolith formation, results from a breed-related inherited disorder of renal tubular transport in dogs. (merckvetmanual.com)
  • The only phenotypic manifestation of cystinuria is cystine urolithiasis, which often recurs throughout an affected individual's lifetime. (medscape.com)
  • Dissolution of bilateral staghorn cystine renal calculi. (bmj.com)
  • Low-affinity system: This system is present in the S1-S2 part of the proximal tubule and is responsible for 90% of L-cystine reabsorption. (medscape.com)
  • Combined with the lack of observed adverse effects our findings cIAP2 support the use of CDME as a viable treatment for cystine urolithiasis. (exposed-skin-care.net)
  • In 1899, cystine was first isolated from protein (horn tissue) by the Swedish chemist Karl A. H. Mörner (1855-1917). (wikipedia.org)
  • 1 nmol/half-cystine/mg protein measured 5-6 h following administration of cysteamine. (medscape.com)
  • Cystine is believed to play a role in protein synthesis, supports the heart, cardiovascular health, and lungs. (bulksupplements.com)
  • This gene encodes a seven-transmembrane domain protein that functions to transport cystine out of lysosomes. (nih.gov)
  • Cystine is a protein-building block found in all cells of the body. (medicinenet.com)
  • The directed movement of L-cystine from the lysosomal lumen across the lysosomal membrane and into the cytosol. (planteome.org)
  • High levels might be due to excessive dietary intake or impaired cystine metabolism. (healthmatters.io)
  • The gene that codes for the cystine transporter, initially termed rBAT, is now known as SLC3A1 (SLC for solute carrier) in the international Genome Database. (medscape.com)
  • Results: Cystine patients had significantly lower total WISQOL scores than noncystine patients. (psu.edu)
  • On specific items, cystine patients reported significantly more sleep problems (p = 0.02), more bother with nocturia (p = 0.03), and feeling tired or fatigued (p = 0.02). (psu.edu)
  • Physiological levels of cystine (100-300 n m ) were restored to acute tissue slices from the nucleus accumbens or prefrontal cortex. (jneurosci.org)
  • Cystine is a major component of tissue antioxidant mechanisms. (healthmatters.io)
  • [ 5 ] Berzelius recognized that the compound was not an oxide, and he named it cystine because the material originated from the bladder. (medscape.com)
  • We assessed the health-related quality of life (HRQOL) of cystine stone-forming patients using the disease-specific Wisconsin Stone Quality of Life questionnaire (WISQOL). (psu.edu)
  • Compared with noncystine stone formers, cystine stone formers also had lower HRQOL scores for subscales (domains) related to social impact, emotional impact, disease impact, and vitality (p ≤ 0.04 for all). (psu.edu)
  • As a residue in proteins, cystine serves two functions: a site of redox reactions and a mechanical linkage that allows proteins to retain their three-dimensional structure. (wikipedia.org)
  • In cell biology, cystine residues (found in proteins) only exist in non-reductive (oxidative) organelles, such as the secretory pathway (endoplasmic reticulum, Golgi apparatus, lysosomes, and vesicles) and extracellular spaces (e.g., extracellular matrix). (wikipedia.org)
  • There are of course other ingredients, but cystine is the key player. (greatist.com)
  • Here's a few supplements available through Amazon that contain cystine. (careomnia.com)
  • Nexxus VitaTress Cystine Treatment 3.3 oz Body building conditioning, structurizer for fine, fragile, thinning hair. (overstock-beauty.com)
  • After the cystine solution is washed out, your stylist will apply some conditioning treatment. (greatist.com)
  • The chemical structure of cystine was determined by synthesis in 1903 by the German chemist Emil Erlenmeyer. (wikipedia.org)
  • Cystine is common in many foods such as eggs, meat, dairy products, and whole grains as well as skin, horns and hair. (wikipedia.org)
  • Below we list 100 Beef Products with cystine. (careomnia.com)
  • We recommend you also check out our top ranked list of all foods with cystine or take a look at what other foods there are in Beef Products . (careomnia.com)
  • Cystine is some hardcore sh*t when it comes to hair products, and the structural changes it makes in your hair are permanent (until the treated hair grows out). (greatist.com)
  • Intracellular GSH levels in LNC were decreased in the DEP exposed cells cultured with or without cystine. (cdc.gov)
  • Conclusion : La lithiase submandibulaire bilatérale est un fait clinique rare mais qu'il faut savoir rechercher même en cas de lithiase submandibulaire isolée. (bvsalud.org)
  • Human hair and skin contain approximately 10-14% cystine by mass. (wikipedia.org)