Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including NEUROPEPTIDES; CYTOSKELETAL PROTEINS; proteins from SMOOTH MUSCLE; CARDIAC MUSCLE; liver; platelets; and erythrocytes. Two subclasses having high and low calcium sensitivity are known. Removes Z-discs and M-lines from myofibrils. Activates phosphorylase kinase and cyclic nucleotide-independent protein kinase. This enzyme was formerly listed as EC 3.4.22.4.
Peptides composed of two amino acid units.
Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.
Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.
Acrylates are a group of synthetic compounds based on acrylic acid, commonly used in various industrial and medical applications such as adhesives, coatings, and dental materials, known to cause allergic reactions and contact dermatitis in sensitive individuals.
A high molecular weight (220-250 kDa) water-soluble protein which can be extracted from erythrocyte ghosts in low ionic strength buffers. The protein contains no lipids or carbohydrates, is the predominant species of peripheral erythrocyte membrane proteins, and exists as a fibrous coating on the inner, cytoplasmic surface of the membrane.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
A group of acylated oligopeptides produced by Actinomycetes that function as protease inhibitors. They have been known to inhibit to varying degrees trypsin, plasmin, KALLIKREINS, papain and the cathepsins.
A heterogenous group of inherited muscular dystrophy that can be autosomal dominant or autosomal recessive. There are many forms (called LGMDs) involving genes encoding muscle membrane proteins such as the sarcoglycan (SARCOGLYCANS) complex that interacts with DYSTROPHIN. The disease is characterized by progressing wasting and weakness of the proximal muscles of arms and legs around the HIPS and SHOULDERS (the pelvic and shoulder girdles).
A 235-kDa cytoplasmic protein that is also found in platelets. It has been localized to regions of cell-substrate adhesion. It binds to INTEGRINS; VINCULIN; and ACTINS and appears to participate in generating a transmembrane connection between the extracellular matrix and the cytoskeleton.
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)
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
An enzyme that catalyzes the conversion of L-CYSTEINE to 3-sulfinoalanine (3-sulfino-L-alanine) in the CYSTEINE metabolism and TAURINE and hypotaurine metabolic pathways.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.

Cyclin D1 proteolysis: a retinoid chemoprevention signal in normal, immortalized, and transformed human bronchial epithelial cells. (1/2088)

BACKGROUND: Retinoids (derivatives of vitamin A) are reported to reduce the occurrence of some second primary cancers, including aerodigestive tract tumors. In contrast, beta-carotene does not reduce the occurrence of primary aerodigestive tract cancers. Mechanisms explaining these effective retinoid and ineffective carotenoid chemoprevention results are poorly defined. Recently, the all-trans-retinoic acid (RA)-induced proteolysis of cyclin D1 that leads to the arrest of cells in G1 phase of the cell cycle was described in human bronchial epithelial cells and is a promising candidate for such a mechanism. In this study, we have investigated this proteolysis as a common signal used by carotenoids or receptor-selective and receptor-nonselective retinoids. METHODS: We treated cultured normal human bronchial epithelial cells, immortalized human bronchial epithelial cells (BEAS-2B), and transformed human bronchial epithelial cells (BEAS-2BNNK) with receptor-selective or receptor-nonselective retinoids or with carotenoids and studied the effects on cell proliferation by means of tritiated thymidine incorporation and on cyclin D1 expression by means of immunoblot analysis. We also examined whether calpain inhibitor I, an inhibitor of the 26S proteasome degradation pathway, affected the decline (i.e., proteolysis) of cyclin D1. RESULTS: Receptor-nonselective retinoids were superior to the carotenoids studied in mediating the decline in cyclin D1 expression and in suppressing the growth of bronchial epithelial cells. Retinoids that activated retinoic acid receptor beta or retinoid X receptor pathways preferentially led to a decrease in the amount of cyclin D1 protein and a corresponding decline in growth. The retinoid-mediated degradation of cyclin D1 was blocked by cotreatment with calpain inhibitor I. CONCLUSIONS: Retinoid-dependent cyclin D1 proteolysis is a common chemoprevention signal in normal and neoplastic human bronchial epithelial cells. In contrast, carotenoids did not affect cyclin D1 expression. Thus, the degradation of cyclin D1 is a candidate intermediate marker for effective retinoid-mediated cancer chemoprevention in the aerodigestive tract.  (+info)

Modifications to rat lens major intrinsic protein in selenite-induced cataract. (2/2088)

PURPOSE: To identify modifications to rat lens major intrinsic protein (MIP) isolated from selenite-induced cataract and to determine whether m-calpain (EC 3.4.22.17) is responsible for cleavage of MIP during cataractogenesis. METHODS: Cataracts were induced in rats by a single injection of sodium selenite. Control and cataract lenses were harvested on day 16 and dissected into cortical and nuclear regions. Membranes were washed with urea buffer followed by NaOH. The protein was reduced/alkylated, delipidated, and cleaved with cyanogen bromide (CNBr). Cleavage products were fractionated by high-performance liquid chromatography (HPLC), and peptides were characterized by mass spectrometry and tandem mass spectrometry. MIP cleavage by m-calpain was carried out by incubation with purified enzyme, and peptides released from the membrane were analyzed by Edman sequencing. RESULTS: The intact C terminus, observed in the control nuclear and cataractous cortical membranes, was not observed in the cataractous nuclear membranes. Mass spectrometric analysis revealed heterogeneous cleavage of the C terminus of MIP in control and cataract nuclear regions. The major site of cleavage was between residues 238 and 239, corresponding to the major site of in vitro cleavage by m-calpain. However, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and mass spectrometric analysis indicated that in vivo proteolysis during cataract formation also included sites closer to the C terminus not produced by m-calpain in vitro. Evidence for heterogeneous N-terminal cleavage was also observed at low levels with no differences between control and cataractous lenses. The major site of phosphorylation was determined to be at serine 235. CONCLUSIONS: Specific sites of MIP N- and C-terminal cleavage in selenite-induced cataractous lenses were identified. The heterogeneous cleavage pattern observed suggests that m-calpain is not the sole enzyme involved in MIP C-terminal processing in rat lens nuclei.  (+info)

Caspase-dependent activation of calpain during drug-induced apoptosis. (3/2088)

We have previously demonstrated that calpain is responsible for the cleavage of Bax, a proapoptotic protein, during drug-induced apoptosis of HL-60 cells (Wood, D. E., Thomas, A., Devi, L. A., Berman, Y., Beavis, R. C., Reed, J. C., and Newcomb, E. W. (1998) Oncogene 17, 1069-1078). Here we show the sequential activation of caspases and calpain during drug-induced apoptosis of HL-60 cells. Time course experiments using the topoisomerase I inhibitor 9-amino-20(S)-camptothecin revealed that cleavage of caspase-3 substrates poly(ADP-ribose) polymerase (PARP) and the retinoblastoma protein as well as DNA fragmentation occurred several hours before calpain activation and Bax cleavage. Pretreatment with the calpain inhibitor calpeptin blocked calpain activation and Bax cleavage but did not inhibit PARP cleavage, DNA fragmentation, or 9-amino-20(S)-camptothecin-induced morphological changes and cell death. Pretreatment with the pan-caspase inhibitor benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (Z-VAD-fmk) inhibited PARP cleavage, DNA fragmentation, calpain activation, and Bax cleavage and increased cell survival by 40%. Interestingly, Z-VAD-fmk-treated cells died in a caspase- and calpain-independent manner that appeared morphologically distinct from apoptosis. Our results suggest that excessive or uncontrolled calpain activity may play a role downstream of and distinct from caspases in the degradation phase of apoptosis.  (+info)

Degradation of protein kinase Malpha by mu-calpain in a mu-calpain-protein kinase Calpha complex. (4/2088)

In previous studies, we isolated and identified a mu-calpain-PKCalpha complex from rabbit skeletal muscle. At the same time we pointed out that an association between mu-calpain and PKCalpha could occur at the level of the plasma membrane of muscle cells, and that PKCalpha could thus be considered as a potential mu-calpain substrate. In the present study, using the mu-calpain-PKCalpha complex as a model, we report that mu-calpain is activated in the combined presence of physiological calcium concentrations (less than 1 microM) and phosphatidylserine. Furthermore our data also show that: (1) there exists a correlation between the appearance of autolyzed mu-calpain forms and PKCalpha hydrolysis which leads to the formation of PKMalpha; (2) in certain experimental conditions, autolyzed mu-calpain forms are able to hydrolyze PKMalpha independently of the presence of diacylglycerol.  (+info)

Hydrostatic pressure and calcium-induced dissociation of calpains. (5/2088)

The dissociation of mu- and m-calpains was studied by fluorescence spectroscopy under high hydrostatic pressure (up to 650 MPa). Increasing pressure induced a red shift of the tryptophan fluorescence of the calcium-free enzyme. The concentration dependence of the spectral transition was consistent with a pressure-induced dissociation of the subunits. Rising temperature increased the stability of calpain heterodimers and confirmed the predominance of hydrophobic interactions between monomers. At saturating calcium, the spectral transition was not observed for native or iodoacetamide-inactivated calpains, indicating that they were already dissociated by calcium. The reaction volume was about -150 ml mol-1 for both isoforms, and the dissociation constants at atmospheric pressure are approximately 10-12 M and 10-15 M for mu- and m-calpains, respectively. This result indicates a tighter interaction in the isoform that requires higher calcium concentration for activity.  (+info)

Calpain inhibitor I increases beta-amyloid peptide production by inhibiting the degradation of the substrate of gamma-secretase. Evidence that substrate availability limits beta-amyloid peptide production. (6/2088)

The calpain inhibitor N-acetyl-leucyl-leucyl-norleucinal (ALLN) has been reported to have complex effects on the production of the beta-amyloid peptide (Abeta). In this study, the effects of ALLN on the processing of the amyloid precursor protein (APP) to Abeta were examined in 293 cells expressing APP or the C-terminal 100 amino acids of APP (C100). In cells expressing APP or low levels of C100, ALLN increased Abeta40 and Abeta42 secretion at low concentrations, decreased Abeta40 and Abeta42 secretion at high concentrations, and increased cellular levels of C100 in a concentration-dependent manner by inhibiting C100 degradation. Low concentrations of ALLN increased Abeta42 secretion more dramatically than Abeta40 secretion. ALLN treatment of cells expressing high levels of C100 did not alter cellular C100 levels and inhibited Abeta40 and Abeta42 secretion with similar IC50 values. These results suggest that C100 can be processed both by gamma-secretase and by a degradation pathway that is inhibited by low concentrations of ALLN. The data are consistent with inhibition of gamma-secretase by high concentrations of ALLN but do not support previous assertions that ALLN is a selective inhibitor of the gamma-secretase producing Abeta40. Rather, Abeta42 secretion may be more dependent on C100 substrate concentration than Abeta40 secretion.  (+info)

Posttranslational regulation of the retinoblastoma gene family member p107 by calpain protease. (7/2088)

The retinoblastoma protein plays a critical role in regulating the G1/S transition. Less is known about the function and regulation of the homologous pocket protein p107. Here we present evidence for the posttranslational regulation of p107 by the Ca2+-activated protease calpain. Three negative growth regulators, the HMG-CoA reductase inhibitor lovastatin, the antimetabolite 5-fluorouracil, and the cyclic nucleotide dibutyryl cAMP were found to induce cell type-specific loss of p107 protein which was reversible by the calpain inhibitor leucyl-leucyl-norleucinal but not by the serine protease inhibitor phenylmethylsulfonylfluoride, caspase inhibitors, or lactacystin, a specific inhibitor of the 26S proteasome. Purified calpain induced Ca2+-dependent p107 degradation in cell lysates. Transient expression of the specific calpain inhibitor calpastatin blocked the loss of p107 protein in lovastatin-treated cells, and the half-life of p107 was markedly lengthened in lovastatian-treated cells stably transfected with a calpastatin expression vector versus cells transfected with vector alone. The data presented here demonstrate down-regulation of p107 protein in response to various antiproliferative signals, and implicate calpain in p107 posttranslational regulation.  (+info)

Ubiquitination and degradation of ATF2 are dimerization dependent. (8/2088)

Ubiquitination and proteasome-dependent degradation are key determinants of the half-lives of many transcription factors. Homo- or heterodimerization of basic region-leucine zipper (bZIP) transcription factors is required for their transcriptional activities. Here we show that activating transcription factor 2 (ATF2) heterodimerization with specific bZIP proteins is an important determinant of the ubiquitination and proteasome-dependent degradation of ATF2. Depletion of c-Jun as one of the ATF2 heterodimer partners from the targeting proteins decreased the efficiency of ATF2 ubiquitination in vitro, whereas the addition of exogenously purified c-Jun restored it. Similarly, overexpression of c-Jun in 293T human embryo kidney cells increased ATF2 ubiquitination in vivo and reduced its half-life in a dose-dependent manner. Mutations of ATF2 that disrupt its dimerization inhibited ATF2 ubiquitination in vitro and in vivo. Conversely, removal of residues 150 to 248, as in a constitutively active ATF2 spliced form, enhanced ATF2 dimerization and transactivation, which coincided with increased ubiquitination and decreased stability. Our findings indicate the increased sensitivity of transcriptionally active dimers of ATF2 to ubiquitination and proteasome-dependent degradation. Based on these observations, we conclude that increased targeting of a transcriptionally active ATF2 form indicates the mechanism by which the magnitude and the duration of the cellular stress response are regulated.  (+info)

Calpains are a family of calcium-dependent cysteine proteases that play important roles in various cellular processes, including signal transduction, cell death, and remodeling of the cytoskeleton. They are present in most tissues and can be activated by an increase in intracellular calcium levels. There are at least 15 different calpain isoforms identified in humans, which are categorized into two groups based on their calcium requirements for activation: classical calpains (calpain-1 and calpain-2) and non-classical calpains (calpain-3 to calpain-15). Dysregulation of calpain activity has been implicated in several pathological conditions, such as neurodegenerative diseases, muscular dystrophies, and cancer.

A dipeptide is a type of molecule that is formed by the condensation of two amino acids. In this process, the carboxyl group (-COOH) of one amino acid combines with the amino group (-NH2) of another amino acid, releasing a water molecule and forming a peptide bond.

The resulting molecule contains two amino acids joined together by a single peptide bond, which is a type of covalent bond that forms between the carboxyl group of one amino acid and the amino group of another. Dipeptides are relatively simple molecules compared to larger polypeptides or proteins, which can contain hundreds or even thousands of amino acids linked together by multiple peptide bonds.

Dipeptides have a variety of biological functions in the body, including serving as building blocks for larger proteins and playing important roles in various physiological processes. Some dipeptides also have potential therapeutic uses, such as in the treatment of hypertension or muscle wasting disorders.

Cysteine proteinase inhibitors are a type of molecule that bind to and inhibit the activity of cysteine proteases, which are enzymes that cleave proteins at specific sites containing the amino acid cysteine. These inhibitors play important roles in regulating various biological processes, including inflammation, immune response, and programmed cell death (apoptosis). They can also have potential therapeutic applications in diseases where excessive protease activity contributes to pathology, such as cancer, arthritis, and neurodegenerative disorders. Examples of cysteine proteinase inhibitors include cystatins, kininogens, and serpins.

Calcium-binding proteins (CaBPs) are a diverse group of proteins that have the ability to bind calcium ions (Ca^2+^) with high affinity and specificity. They play crucial roles in various cellular processes, including signal transduction, muscle contraction, neurotransmitter release, and protection against oxidative stress.

The binding of calcium ions to these proteins induces conformational changes that can either activate or inhibit their functions. Some well-known CaBPs include calmodulin, troponin C, S100 proteins, and parvalbumins. These proteins are essential for maintaining calcium homeostasis within cells and for mediating the effects of calcium as a second messenger in various cellular signaling pathways.

Acrylates are a group of chemical compounds that are derived from acrylic acid. They are commonly used in various industrial and commercial applications, including the production of plastics, resins, paints, and adhesives. In the medical field, acrylates are sometimes used in the formation of dental restorations, such as fillings and dentures, due to their strong bonding properties and durability.

However, it is important to note that some people may have allergic reactions or sensitivities to acrylates, which can cause skin irritation, allergic contact dermatitis, or other adverse effects. Therefore, medical professionals must use caution when working with these materials and ensure that patients are informed of any potential risks associated with their use.

Spectrin is a type of cytoskeletal protein that is responsible for providing structural support and maintaining the shape of red blood cells (erythrocytes). It is a key component of the erythrocyte membrane skeleton, which provides flexibility and resilience to these cells, allowing them to deform and change shape as they pass through narrow capillaries. Spectrin forms a network of fibers just beneath the cell membrane, along with other proteins such as actin, band 4.1, and band 3. Mutations in spectrin genes can lead to various blood disorders, including hereditary spherocytosis and hemolytic anemia.

Calcium is an essential mineral that is vital for various physiological processes in the human body. The medical definition of calcium is as follows:

Calcium (Ca2+) is a crucial cation and the most abundant mineral in the human body, with approximately 99% of it found in bones and teeth. It plays a vital role in maintaining structural integrity, nerve impulse transmission, muscle contraction, hormonal secretion, blood coagulation, and enzyme activation.

Calcium homeostasis is tightly regulated through the interplay of several hormones, including parathyroid hormone (PTH), calcitonin, and vitamin D. Dietary calcium intake, absorption, and excretion are also critical factors in maintaining optimal calcium levels in the body.

Hypocalcemia refers to low serum calcium levels, while hypercalcemia indicates high serum calcium levels. Both conditions can have detrimental effects on various organ systems and require medical intervention to correct.

Leupeptins are a type of protease inhibitors, which are substances that can inhibit the activity of enzymes called proteases. Proteases play a crucial role in breaking down proteins into smaller peptides or individual amino acids. Leupeptins are naturally occurring compounds found in some types of bacteria and are often used in laboratory research to study various cellular processes that involve protease activity.

Leupeptins can inhibit several different types of proteases, including serine proteases, cysteine proteases, and some metalloproteinases. They work by binding to the active site of these enzymes and preventing them from cleaving their protein substrates. Leupeptins have been used in various research applications, such as studying protein degradation, signal transduction pathways, and cell death mechanisms.

It is important to note that leupeptins are not typically used as therapeutic agents in clinical medicine due to their potential toxicity and lack of specificity for individual proteases. Instead, they are primarily used as research tools in basic science investigations.

Limb-girdle muscular dystrophy (LGMD) is a group of rare inherited disorders that cause progressive weakness and wasting of the muscles in the arms and legs, particularly those around the shoulders and hips (the limb-girdle region). The condition affects both males and females and presents at different ages, depending on the specific type of LGMD.

LGMD is caused by mutations in various genes that play a role in maintaining muscle integrity and function. These genetic defects lead to a deficiency or dysfunction of certain proteins necessary for muscle health, ultimately resulting in muscle degeneration and weakness. There are more than 30 different subtypes of LGMD, each with its own set of causative genes and inheritance patterns (autosomal dominant or autosomal recessive).

Symptoms of limb-girdle muscular dystrophy may include:

1. Progressive muscle weakness and wasting in the arms, legs, shoulders, and hips
2. Difficulty with activities such as climbing stairs, lifting objects, or getting up from a seated position
3. Enlarged calf muscles (pseudohypertrophy) due to muscle degeneration and fat replacement
4. Muscle contractures, joint stiffness, and limited range of motion
5. Difficulty walking, using wheelchair assistance in advanced stages
6. Respiratory complications due to weakened chest muscles in some cases

Diagnosis of LGMD typically involves a combination of clinical evaluation, family history, muscle biopsy, genetic testing, and blood tests for creatine kinase (CK) levels, which are often elevated in muscular dystrophies. Treatment is primarily supportive and focuses on maintaining mobility, preventing complications, and preserving quality of life through physical therapy, assistive devices, and orthopedic interventions as needed. No cure currently exists for limb-girdle muscular dystrophy, but ongoing research aims to develop targeted therapies based on the underlying genetic defects.

I'm sorry for any confusion, but "Talin" is not a medical term that I am aware of. Talin is actually a protein involved in cell-matrix and cell-cell adhesion, acting as a crucial component in connecting the intracellular cytoskeleton to the extracellular matrix. It might be used in scientific or biology research contexts, but it's not a term typically found in medical textbooks or patient-related medical definitions. If you have any questions about medical conditions or terms, I would be happy to help with those!

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.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Cysteine proteases are a type of enzymes that cleave peptide bonds in proteins, and they require a cysteine residue in their active site to do so. These enzymes play important roles in various biological processes, including protein degradation, cell signaling, and inflammation. They can be found in various tissues and organisms, including humans, where they are involved in many physiological and pathological conditions.

Cysteine proteases are characterized by a conserved catalytic mechanism that involves a nucleophilic attack on the peptide bond carbonyl carbon by the thiolate anion of the cysteine residue, resulting in the formation of an acyl-enzyme intermediate. This intermediate is then hydrolyzed to release the cleaved protein fragments.

Some examples of cysteine proteases include cathepsins, caspases, and calpains, which are involved in various cellular processes such as apoptosis, autophagy, and signal transduction. Dysregulation of these enzymes has been implicated in several diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, cysteine proteases have emerged as important therapeutic targets for the development of new drugs to treat these conditions.

Peptide hydrolases, also known as proteases or peptidases, are a group of enzymes that catalyze the hydrolysis of peptide bonds in proteins and peptides. They play a crucial role in various biological processes such as protein degradation, digestion, cell signaling, and regulation of various physiological functions. Based on their catalytic mechanism and the specificity for the peptide bond, they are classified into several types, including serine proteases, cysteine proteases, aspartic proteases, and metalloproteases. These enzymes have important clinical applications in the diagnosis and treatment of various diseases, such as cancer, viral infections, and inflammatory disorders.

Cysteine dioxygenase (CDO) is an enzyme that catalyzes the conversion of the amino acid L-cysteine to L-cysteinesulfinic acid, which is the first step in the catabolism of L-cysteine. This reaction also generates molecular oxygen as a byproduct. CDO plays important roles in various biological processes such as neurotransmitter biosynthesis and oxidative stress response. It exists as two isoforms, CDO1 and CDO2, which are encoded by separate genes and have distinct tissue distributions and functions.

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.

As the first calpain whose three-dimensional structure was determined, m-calpain is the type-protease for the C2 (calpain) ... calpain and m-calpain (or calpain I and II), that differed primarily in their calcium requirements in vitro. Their names ... Calpain for Modulatory Proteolysis Database The Calpain Family of Proteases. (2001). University of Arizona. Calpain Info with ... Calpains constitute the C2 family of protease clan CA in the MEROPS database. The calpain proteolytic system includes the ...
... (also known as calpamodulin) is a protein in humans that is encoded by the CAPN6 gene. Calpains are a ubiquitous, ... "Entrez Gene: Calpain 6". National Center for Biotechnology Information. U.S. National Library of Medicine. Archived from the ... Calpains have been implicated in neurodegenerative processes, as their activation can be triggered by calcium influx and ... Its C-terminal region lacks any homology to the calmodulin-like domain of other calpains. The protein lacks a critical ...
... (EC 3.4.22.53, calcium-activated neutral protease II, m-calpain, milli-calpain) is an intracellular heterodimeric ... "Structure and nomenclature / Calpain Research Portal: Calpain Structure and Nomenclature". calpain.net. Retrieved 2021-01-17. ... Calpain Research Portal CAPN2 Crystal Structure of Human Calpain-2 Strobl S, Fernandez-Catalan C, Braun M, Huber R, Masumoto H ... Calpain-2 heterodimer is highly homologous to calpain-1, which is formed by a catalytic CAPN1 and a regulatory CAPNS1 subunits ...
... (EC 3.4.22.52, mu-calpain, calcium-activated neutral protease I) is an enzyme. This enzyme catalyses the following ... and m-calpain". The Biochemical Journal. 367 (Pt 1): 263-9. doi:10.1042/bj20020485. PMC 1222847. PMID 12014988. Calpain-1 at ...
... is a protein that in humans is encoded by the CAPN9 gene. Calpains are ubiquitous, well-conserved family of calcium- ... "Entrez Gene: CAPN9 calpain 9". Huang Y, Wang KK (2001). "The calpain family and human disease". Trends in Molecular Medicine. 7 ... The calpain proteins are heterodimers consisting of an invariant small subunit and variable large subunits. The large subunit ... Calpains have been implicated in neurodegenerative processes, as their activation can be triggered by calcium influx and ...
... is a protein that in humans is encoded by the CAPN3 gene. Calpain, a heterodimer consisting of a large and a small ... "Entrez Gene: CAPN3 calpain 3, (p94)". Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO, Valgeirsdottir ... Huang Y, de Morrée A, van Remoortere A, Bushby K, Frants RR, den Dunnen JT, van der Maarel SM (2008). "Calpain 3 is a modulator ... Ohno S, Minoshima S, Kudoh J, Fukuyama R, Shimizu Y, Ohmi-Imajoh S, Shimizu N, Suzuki K (1990). "Four genes for the calpain ...
"CAPN8 - Calpain-8 - Homo sapiens (Human) - CAPN8 gene & protein". www.uniprot.org. Retrieved 18 May 2022. "Entrez Gene: Calpain ... Calpain-8 is a protein in humans that is encoded by the CAPN8 gene. GRCh38: Ensembl release 89: ENSG00000203697 - Ensembl, May ...
... (CANP 1) is a protein that in humans is encoded by the CAPN1 gene. The calpains, calcium-activated ... "Entrez Gene: CAPN1 calpain 1, (mu/I) large subunit". Shinozaki K, Maruyama K, Kume H, Tomita T, Saido TC, Iwatsubo T, Obata K ( ... The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of ... This gene encodes the large subunit of the ubiquitous enzyme, calpain 1. CAPN1 has been shown to interact with PSEN2. GRCh38: ...
... (CSS1), is a protein that in humans is encoded by the CAPNS1 gene. Calpains are a ubiquitous, well- ... "Entrez Gene: CAPNS1 calpain, small subunit 1". Lin GD, Chattopadhyay D, Maki M, Wang KK, Carson M, Jin L, Yuen PW, Takano E, ... Calpain I and II are heterodimeric with distinct large subunits associated with common small subunits, all of which are encoded ... Ohno S, Minoshima S, Kudoh J, Fukuyama R, Shimizu Y, Ohmi-Imajoh S, Shimizu N, Suzuki K (1990). "Four genes for the calpain ...
... is a protein that in humans is encoded by the CAPN2 gene. The calpains, calcium-activated neutral ... m-calpains and calpastatin and capture of mu-calpain activation in endothelial cells". J. Cell. Biochem. 66 (2): 197-209. doi: ... "Entrez Gene: CAPN2 calpain 2, (m/II) large subunit". Gil-Parrado S, Fernández-Montalván A, Assfalg-Machleidt I, Popp O, ... Potential role of calpain, protein tyrosine phosphatase 1b, and p130Cas in integrin-mediated signaling events". J. Biol. Chem. ...
Calpain. "Kiki Memorial and Art Gathering". Equestria Daily. Retrieved February 15, 2015. Sporeman, Sean (May 6, 2015). "Follow ...
Lokuta, M. A., Nuzzi, P. A., & Huttenlocher, A. (2003). Calpain regulates neutrophil chemotaxis. Proceedings of the National ... involving intracellular proteolysis by the calcium-dependent protease calpain. Her laboratory was also the first to document ... Calpain-mediated proteolysis of talin regulates adhesion dynamics. Nature cell biology, 6(10), 977-983. https://doi.org/10.1038 ...
Calpain (February 16, 2015). "Season 5 Concept Art at PonyCon Appears! New Characters and More Revealed!". Equestria Daily. ... Calpain (January 19, 2015). "PonyCon 2015 To Premiere New Season 5 Trailer With MLP Directors!". Equestria Daily. Retrieved ...
Calpain (September 20, 2017). "America's Got Talent Special MLP Movie Sneak Peak". Equestria Daily. Retrieved September 27, ...
Calpain (September 29, 2015). "Ratings For The 'Friendship Games' Are In". Equestria Daily. Archived from the original on ...
Calpain 3 is unique from other calpain proteases in that it is relatively specific to muscle. Calpain 3 is both a protease and ... Research is being done to identify the proteins cleaved by calpain-3. Gene therapy is being studied to replace the function of ... Mutation in the gene CAPN3, which encodes the protein calpain-3 (CAPN3), is the cause of calpainopathy. As of 2019, more than ... The structural role of calpain 3 is stabilization of the triad protein complexes. A triad protein complex plays a role ...
"Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members". The Journal of Biological Chemistry ...
Löfvenberg L, Backman L (1999). "Calpain-induced proteolysis of beta-spectrins". FEBS Lett. 443 (2): 89-92. doi:10.1016/S0014- ...
1997). "Identification of mu-, m-calpains and calpastatin and capture of mu-calpain activation in endothelial cells". J. Cell. ... 1989). "Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene". J. Biol. ... It consists of an N-terminal domain L and four repetitive calpain-inhibition domains (domains 1-4), and it is involved in the ... 1990). "Cloning and expression of the genes for calpains and calpastatins". Biochem. Soc. Symp. 55: 29-44. PMID 2559735. Asada ...
This protein is a substrate of calpain II. A second transcript from this gene has been described, but its full length nature ...
The protease calpain has also been shown to be involved in this type of cell destruction; just as the use of calpain inhibitors ... Wang KK (Jan 2000). "Calpain and caspase: can you tell the difference?". Trends in Neurosciences. 23 (1): 20-26. doi:10.1016/ ... Villa PG, Henzel WJ, Sensenbrenner M, Henderson CE, Pettmann B (Mar 1998). "Calpain inhibitors, but not caspase inhibitors, ...
These cysteine proteases include calpain, caspase, and cathepsin. These three proteins are examples of detectable signs of ...
This group includes the calpains. Basic proteases (or alkaline proteases) Proteases are involved in digesting long protein ...
Calpain-5 is a protein that in humans is encoded by the CAPN5 gene. Calpains are calcium-dependent cysteine proteases involved ... "Entrez Gene: CAPN5 calpain 5". Vanderklish PW, Bahr BA (2001). "The pathogenic activation of calpain: a marker and mediator of ... A functional calpain protein consists of an invariant small subunit and 1 of a family of large subunits. CAPN5 is one of the ... 2007). "Calpain-5 gene variants are associated with diastolic blood pressure and cholesterol levels". BMC Med. Genet. 8: 1. doi ...
... interacts with many sarcomeric proteins including: Z line region: telethonin and alpha-actinin I band region: calpain-3 ... July 1998). "Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular ... Kinbara K, Sorimachi H, Ishiura S, Suzuki K (August 1998). "Skeletal muscle-specific calpain, p49: structure and physiological ... Sorimachi H, Ono Y, Suzuki K (2000). "Skeletal Muscle-Specific Calpain, p94, and Connectin/Titin: Their Physiological Functions ...
This may be mediated via the proteasome or calpain. Rogers S, Wells R, Rechsteiner M (1986). "Amino acid sequences common to ... "The PEST Domain of IκBα is necessary and sufficient for in vitro degradation by mu-calpain". J. Biol. Chem. 274 (43): 30874-81 ...
Weber, Jonasz J.; Ortiz Rios, Midea M.; Riess, Olaf; Clemens, Laura E.; Nguyen, Huu P. (2016-01-01). "The calpain-suppressing ... "Olesoxime suppresses calpain activation and mutant huntingtin fragmentation in the BACHD rat". Brain. 138 (12): 3632-3653. doi: ... effects of olesoxime were attributed to modulating the activity of calcium-dependent proteases called calpains. A 2009-2011 ...
May 2002). "Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain". Molecular and Cellular Biology. 22 (10 ...
This includes a binding site for SA1 or SA2, recognition motifs for separase, caspase, and calpain to cleave, as well as a ... Panigrahi AK, Zhang N, Mao Q, Pati D (November 2011). "Calpain-1 cleaves Rad21 to promote sister chromatid separation". ... RAD21 is cleaved by several proteases including Separase and Calcium-dependent cysteine endopeptidase Calpain-1 during mitosis ...
Calpain-10 is a protein that in humans is encoded by the CAPN10 gene. Calpains are ubiquitous, well-conserved family of calcium ... "Entrez Gene: CAPN10 calpain 10". Sorimachi H, Ishiura S, Suzuki K (1998). "Structure and physiological function of calpains". ... 2001). "Characterization and expression of calpain 10. A novel ubiquitous calpain with nuclear localization". J. Biol. Chem. ... Horikawa Y (2007). "Calpain-10 (NIDDM1) as a Susceptibility Gene for Common Type 2 Diabetes". Endocr. J. 53 (5): 567-76. doi: ...
As the first calpain whose three-dimensional structure was determined, m-calpain is the type-protease for the C2 (calpain) ... calpain and m-calpain (or calpain I and II), that differed primarily in their calcium requirements in vitro. Their names ... Calpain for Modulatory Proteolysis Database The Calpain Family of Proteases. (2001). University of Arizona. Calpain Info with ... Calpains constitute the C2 family of protease clan CA in the MEROPS database. The calpain proteolytic system includes the ...
J:237762 Hata S, et al., A Gastrointestinal Calpain Complex, G-calpain, Is a Heterodimer of CAPN8 and CAPN9 Calpain Isoforms, ... Both the conserved and the unique gene structure of stomach-specific calpains reveal processes of calpain gene evolution. J Mol ...
Home Study Estrogen may be acting through calpain, probably boosting learning and memory ... To possibly avert the risks linked to hormone therapy, drug developers in the future may choose to target calpain directly. ... The neuroscientists found the hormone to act through another chemical called calpain. The latter protein was discovered to have ... Apparently not working as a slowly diffusing hormone, estrogen acting through calpain could be functioning as a ...
With the increased invasion of a plethora of immunocytes, a surge in cytokines, such as IL-1, IL-18, and lactate dehydrogenase…. ...
... calpain activation, and cytoskeleton degradation through spectrin break-down. ... Huff, Terry B.; Shi, Yunzhou; Sun, Wenjing; Wu, Wei; Shi, Riyi; and Cheng, Ji-Xin, "Real-Time CARS Imaging Reveals a Calpain- ... Real-Time CARS Imaging Reveals a Calpain-Dependent Pathway for Paranodal Myelin Retraction during High-Frequency Stimulation. ... 2011) Real-Time CARS Imaging Reveals a Calpain-Dependent Pathway for Paranodal Myelin Retraction during High-Frequency ...
Find symptoms and other information about Calpain-3-related limb-girdle muscular dystrophy R1. ... Calpain-3-related LGMD R1; LGMD type 2A; LGMD2A; Limb-girdle muscular dystrophy due to calpain deficiency; Limb-girdle muscular ... Calpain-3-related limb-girdle muscular dystrophy R1. Other Names: Autosomal recessive limb-girdle muscular dystrophy type 2A; ... Calpain-3-related LGMD R1; LGMD type 2A; LGMD2A; Limb-girdle muscular dystrophy due to calpain deficiency; Limb-girdle muscular ...
Calpain 2 is required for the invasion of glioblastoma cells in the zebrafish brain microenvironment.. Title. Calpain 2 is ... Knockdown of calpain 2 resulted in a 2.9-fold decrease in the invasion of human glioblastoma cells in zebrafish brain. Control ... Animals, Animals, Genetically Modified, Brain Neoplasms, Calpain, Cell Line, Tumor, Gene Expression Profiling, Gene Expression ... Calpain 2 is required for the invasion of glioblastoma cells in the zebrafish brain microenvironment. ...
Human Calpain Small Subunit 1 Antibody Human Calpain Small Subunit 1 Antibody (Biotin Conjugate) Human Calpain Small Subunit 1 ... Human Calpain small subunit 1 AssayLite RPE-Conjugated Antibody ICC Kit Human Calpain small subunit 1 ... Human Calpain Small Subunit 1 AssayLite Antibody (RPE Conjugate) Human Calpain Small Subunit 1 AssayLite Antibody (APC ... Calpain Small Subunit 1, CSS1, Calcium-Activated Neutral Proteinase Small Subunit, CANP Small Subunit, Calcium-Dependent ...
NOVEL SNP OF CALPAIN-1 (CAPN1) GENE AND ITS ASSOCIATION WITH CARCASS AND MEAT CHARACTERISTICS TRAITS IN BALI CATTLE ... Calpain-1 gene (CAPN1) produces an calpain enzyme controlling structure of meat protein and tenderness. The aims of this study ... Calpain-1 gene (CAPN1) produces an calpain enzyme controlling structure of meat protein and tenderness. The aims of this study ... Association of Calpain gene with carcass percentage in Sumba Ongole cattle. P. P. Agung, S. Said, E. M. Kaiin, M. Gunawan, N. D ...
Calpain Inhibitor VI inhibits purified m-calpain with the IC50 of 80 nM. Calpain Inhibitor VI can be used for the research of ... We do not sell to patients.Calpain Inhibitor VICAS No. : 190274-53-4Biological Activity:Calpain Inhibitor VI (SJA6017) is a ... Calpain Inhibitor VI inhibits purified m-calpain with the IC50 of 80 nM. Calpain Inhibitor VI can be used for the research of ... Calpain Inhibitor VI. CAS No. : 190274-53-4. Biological Activity:Calpain Inhibitor VI (SJA6017) is a synthesized peptide ...
Calpain-13. Vendor: Triple Point Biologics, Inc.. Product information will be uploaded soon. If you have any questions, ...
DiscoveryPak™ Calpain Inhibitors Set Biovision DiscoveryPak™ Calpain Inhibitors Set. (No reviews yet) Write a Review Write a ... 1835), 250 μg of Calpain Inhibitor Z-LLY-FMK (Cat. No. B1506), 10 mg of MDL 28170 (Cat. No. 2195) and 5 mg of PD-150, 606 (Cat ... A convenient set containing five Calpain inhibitors. Each set contains 5 mg of ALLN (Cat. No. 1834), 5 mg of ALLM (Cat. No. ...
More CalPain on Budgets. The Mercury Times has an article on the on-going Caltrain outreach program to figure out how to close ...
Calpain research in the CNS has focused almost exclusively on the classical calpains, Calpains 1 and 2. Calpain 5 (CAPN5), ... which lacks the penta-EF hand domain of classical calpains, is the 2nd most highly expressed calpain in the CNS. Calpain 5 has ... The purpose of this proposal is gain insight into the CNS functions of Calpain 5. Aim 1 will identify Calpain 5 binding ... Very little is known regarding the functions and substrates of Calpain 5. The C. elegans orthologue of Calpain 5, Tra-3, ...
... 可查询Calpain 2 (large subunit) (CAPN2)价格,提供Calpain 2 (large subunit) (CAPN2)技术资料,Calpain 2 (large ... 克拉玛尔专业提供Calpain 2 (large subunit) (CAPN2)高品质试剂, ... Calpain M-type antibody, Calpain large polypeptide L2 antibody, Calpain-2 large subunit antibody, Millimolar-calpain. ... isoforms, calpain 1 and calpain 2, was demonstrated previously in Alzheimers disease. Calpain 2 could be
Calpain-2 inhibitor therapy in Non-severe Hemophilia A Calpain-2 inhibitors ...
Calpain-2 inhibitor therapy in Non-severe Hemophilia A Calpain-2 inhibitors ...
Rat CAPN1(Calpain 1, Large Subunit) ELISA Kit. Rat CAPN1(Calpain 1, Large Subunit) ELISA Kit ... Description: A sandwich ELISA kit for detection of Calpain 1, Large Subunit from Rat in samples from blood, serum, plasma, cell ... Description: A sandwich ELISA kit for detection of Calpain 1, Large Subunit from Mouse in samples from blood, serum, plasma, ... Description: A sandwich ELISA kit for detection of Calpain 1, Large Subunit from Human in samples from blood, serum, plasma, ...
... and calpains. We also describe how the proteolytic activities are determined by different platelet populations in a thrombus ... caspases and calpains. We also describe how the proteolytic activities are determined by different platelet populations in a ... Regarding calpain receptor substrates in platelets, a marked finding was that calpains under certain, high-Ca2+ conditions can ... Intracellular Calpains and Caspases. The calpain isoforms mu, 1 and 2, act as cytosolic proteases, which rely for their ...
To better understand the regulation of calpains, we have investigated potential interactions of miRNA with five target calpain ... calpain 5 (CAPN5), and the endogenous inhibitor of multiple members of the calpain family, designated calpastatin (CAST). This ... As regulation of these two targets would affect activity of several members of the calpain family it is of note that they have ... There have not been any investigations into regulation of the calpain system by the newly discovered microRNA (miRNA) system of ...
Synthesis and investigation of dihydroxychalcones as calpain and cathepsin inhibitors. Kyung Hye Baek, Radha Karki, Eung Seok ... Dive into the research topics of Synthesis and investigation of dihydroxychalcones as calpain and cathepsin inhibitors. ...
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Lp82 is the dominant form of calpain in young mouse lens. H. Ma, I. Hata, M. Shih, C. Fukiage, Y. Nakamura, M. Azuma, T. R. ... Lp82 is the dominant form of calpain in young mouse lens. / Ma, H.; Hata, I.; Shih, M. et al. In: Experimental Eye Research, ... Ma, H, Hata, I, Shih, M, Fukiage, C, Nakamura, Y, Azuma, M & Shearer, TR 1999, Lp82 is the dominant form of calpain in young ... Lp82 is the dominant form of calpain in young mouse lens. Experimental Eye Research. 1999 Apr;68(4):447-456. doi: 10.1006/exer. ...
Investigating Calpain Expression on Tau Toxicity., 2013. Download whole document (PDF) (2.34 MB) ...
Dive into the research topics of Calpains can do it alone: Implications for cancer therapy. Together they form a unique ...
CAPN3: calpain 3. *CARD9: caspase recruitment domain family member 9. *CARD11: caspase recruitment domain family member 11 ...
Investigation of the influence of calpain on membrane ruffling. Research output: Contribution to conference › Conference ...
  • The calpain proteolytic system includes the calpain proteases, the small regulatory subunit CAPNS1, also known as CAPN4, and the endogenous calpain-specific inhibitor, calpastatin. (wikipedia.org)
  • Biological Activity: Calpain Inhibitor VI (SJA6017) is a synthesized peptide aldehyde inhibitor of calpain. (epigenetics-modulation-frontier.com)
  • Calpain Inhibitor VI inhibits purified m-calpain with the IC 50 of 80 nM. (epigenetics-modulation-frontier.com)
  • Calpain Inhibitor VI can be used for the research of cataract. (epigenetics-modulation-frontier.com)
  • No. 1835), 250 μg of Calpain Inhibitor Z-LLY-FMK (Cat. (transcriptionfactor.org)
  • The chosen targets were the catalytic subunits of calpains 1 (CAPN1) and 2 (CAPN2), the small subunit CAPNS1 required for their proper folding, calpain 5 (CAPN5), and the endogenous inhibitor of multiple members of the calpain family, designated calpastatin (CAST). (umaine.edu)
  • Endogenous Lp82 in lens soluble proteins was activated by addition of calcium and caused limited proteolysis of crystallins even in the presence of large amounts of recombinant domain I from the natural calpain inhibitor calpastatin. (elsevierpure.com)
  • Inhibition of calpain activation by prophylactic administration of the precise calpain inhibitor Z-Val-Phe methyl ester (ZVP) decreases cerulein-induced pancreatic harm (Weber 2004). (academicediting.org)
  • Moreover, activation of SOCE by thapsigargin , an inhibitor of Ca2+ pump on the endoplasmic/ sarcoplasmic reticulum membrane , significantly increased the activity of calpain , which was inhibited by BTP2. (bvsalud.org)
  • Finally, the calpain -1/ calpain -2 inhibitor calpeptin significantly blunted the nephrin protein reduction induced by HG treatment . (bvsalud.org)
  • Calpains are Ca2+- dependent proteases and together with the Ca2+-dependent specific inhibitor of calpains, calpastatin, are widely distributed in eukaryotic cells. (arizona.edu)
  • Results reveal an increased association of calpain I, II, calpastatin, and the 30-kDa regulatory subunit with the endoplasmic reticulum and Golgi apparatus as evidenced by their position in the gradient relative to calnexin, Rab6, caveolin, and beta1 integrin after laminin stimulation. (klamar-reagent.com)
  • and m-calpain, calpastatin, atrogin-1, and MuRF1 was determined by real-time polymerase chain reaction. (fabiopacelli.it)
  • The hypothesis to be further evaluated is that some dystrophies are characterized by increased calpain activity, caused either by an increased expression of m- or μ- calpain or decreased inhibition by calpastatin, or both. (arizona.edu)
  • Structurally, these two heterodimeric isoforms share an identical small (28 kDa) subunit (CAPNS1 (formerly CAPN4)), but have distinct large (80 kDa) subunits, known as calpain 1 and calpain 2 (each encoded by the CAPN1 and CAPN2 genes, respectively). (wikipedia.org)
  • Western blot analysis on (A) PC-3, (B) HeLa, (C) A431, and (D) 293T cell lysates using anti-Calpain 2 (large subunit) RabMAb (cat. (klamar-reagent.com)
  • A synthetic peptide corresponding to residues in human Calpain 2 (large subunit) was used as an immunogen. (klamar-reagent.com)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Rat Calpain 1, Large Subunit (CAPN1) in samples from Tissue homogenates, cell lysates and other biological fluids. (clinical-trial-logistics.com)
  • Description: A sandwich ELISA kit for detection of Calpain 1, Large Subunit from Rat in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (clinical-trial-logistics.com)
  • Description: A sandwich quantitative ELISA assay kit for detection of Human Calpain 1, Large Subunit (CAPN1) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids. (clinical-trial-logistics.com)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Calpain 1, Large Subunit (CAPN1) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (clinical-trial-logistics.com)
  • Calpains are Ca2+-activated, neutral (non-lysosomal) proteases implicated in neurodegeneration following acute insults such as stroke and traumatic brain injury, as well as in neurodegenerative disorders such as Alzheimer's disease. (uky.edu)
  • Misregulation of the calcium dependent family of proteases known as calpains contributes to several pathologies including Alzheimer's disease1 and altered cellular functions including regulation of cell cycle2 and the cell motility3. (umaine.edu)
  • Lp82 is a lens-specific, calcium-activated isozyme from the calpain super family of cysteine proteases (EC 34.22.17). (elsevierpure.com)
  • Calpain represents a family group of Ca2+-dependent cytosolic cysteine proteases found in almost all eukaryotes and some bacteria, and is involved in a variety of biological phenomena, including brain function. (ecolowood.com)
  • Calpains are calcium-regulated cysteine proteases that have been implicated in the regulation of cell death pathways. (uic.edu)
  • To date, these two isoforms remain the best characterised members of the calpain family. (wikipedia.org)
  • As regulation of these two targets would affect activity of several members of the calpain family it is of note that they have the most evidence indicating miRNA regulation. (umaine.edu)
  • When the sequence of this enzyme became known, it was given the name "calpain", to recognize its common properties with two well-known proteins at the time, the calcium-regulated signalling protein, calmodulin, and the cysteine protease of papaya, papain. (wikipedia.org)
  • Calpain 5 has homology to other calpains in the cysteine protease domain and also has a unique C2 domain at the C-terminus. (uky.edu)
  • The cytosolic cysteine protease calpain is implicated in a multitude of cellular functions but also Gefitinib (Iressa) plays a role in cell damage. (academicediting.org)
  • Calpain , a Ca2+-dependent cysteine protease , was recently shown to be involved in podocyte injury . (bvsalud.org)
  • To better understand the regulation of calpains, we have investigated potential interactions of miRNA with five target calpain system members to screen for miRNA interactions possessing a high likelihood of regulating calpain activity. (umaine.edu)
  • Calpains constitute the C2 family of protease clan CA in the MEROPS database. (wikipedia.org)
  • As the first calpain whose three-dimensional structure was determined, m-calpain is the type-protease for the C2 (calpain) family in the MEROPS database. (wikipedia.org)
  • We previously reported that the calcium-activated protease calpain 2 is critical for glioblastoma cell invasion in vitro. (oregonstate.edu)
  • 产品介绍】The calcium-activated protease calpain cleaves a variety of biologically important proteins and serves, therefore, as a key regulator of many cellular functions. (klamar-reagent.com)
  • The two ubiquitous isoforms of this protease, calpain I and II, are considered to be cytosolic proteins that can translocate to both focal complexes/adhesions or the plasma membrane. (klamar-reagent.com)
  • The protease activation was accompanied by a decrease in the E-cadherin level and formation of calpain-specific breakdown products of αII-spectrin. (academicediting.org)
  • The outcomes claim that CCK-induced acinar cell harm needs activation of calpain which the actin cytoskeleton is one of the mobile targets from the protease. (academicediting.org)
  • Shortly thereafter, the activity was found to be attributable to two main isoforms, dubbed μ ("mu")-calpain and m-calpain (or calpain I and II), that differed primarily in their calcium requirements in vitro. (wikipedia.org)
  • The Human Genome Project has revealed that more than a dozen other calpain isoforms exist, some with multiple splice variants. (wikipedia.org)
  • Activation of both main isoforms, calpain 1 and calpain 2, was demonstrated previously in Alzheimer's disease. (klamar-reagent.com)
  • Immediately after administration CCK led to activation of both calpain isoforms μ- and m-calpain. (academicediting.org)
  • Certainly we noticed that both ubiquitous calpain isoforms are turned on in the pancreatic tissues of rats experiencing cerulein-induced severe pancreatitis. (academicediting.org)
  • Calpains have been shown to be involved in several physiological processes such as cell motility, proliferation, cell cycle, signal transduction, and apoptosis. (elsevierpure.com)
  • In vivo, calpain-1 null mice show significantly less neural degeneration and apoptosis and a smaller contusion 3 days post-injury than wild type littermates. (uic.edu)
  • Protection from traumatic brain injury corroborated with the resistance of calpain-1 neurons to apoptosis induced by oxidative stress. (uic.edu)
  • Biochemical analysis revealed that caspase-3 activation, extracellular calcium entry, mitochondrial membrane permeability, and release of apoptosis-inducing factor from mitochondria are partially blocked in the calpain-1 null neurons. (uic.edu)
  • These findings suggest that the calpain-1 knock-out mice may serve as a useful model system for neuronal protection and apoptosis in traumatic brain injury and other neurodegenerative disorders in which oxidative stress plays a role. (uic.edu)
  • Calpain is also involved in skeletal muscle protein breakdown due to exercise and altered nutritional states. (wikipedia.org)
  • Chromosomal localization of the porcine skeletal muscle calpain gene. (tamu.edu)
  • Calpain activity is increased in skeletal muscle from gastric cancer patients with no or minimal weight loss. (fabiopacelli.it)
  • The influence of cancer on skeletal muscle calpain expression and activity in humans is poorly understood. (fabiopacelli.it)
  • SNP}, abstract = { Calpain-1 gene (CAPN1) produces an calpain enzyme controlling structure of meat protein and tenderness. (undip.ac.id)
  • Calpain-3-related limb-girdle muscular dystrophy R1 (also known as LGMD2A) is an autosomal recessive limb-girdle muscular dystrophy characterized by progressive, symmetrical weakness of the proximal limb and girdle muscles (mainly those around the hips and shoulders) without heart involvement or intellectual disability. (nih.gov)
  • Additionally, phosphorylation by protein kinase A and dephosphorylation by alkaline phosphatase have been found to positively regulate the activity of μ-calpains by increasing random coils and decreasing β-sheets in its structure. (wikipedia.org)
  • Calpain 2 could be directly involved in tau hyperphosphorylation by modulating protein kinase activities. (klamar-reagent.com)
  • Lp82 and m-calpain protein levels and proteolytic activities in lenses were measured by casein zymography, immunoblotting, and ELISA after partial purification by DEAE- HPLC. (elsevierpure.com)
  • Published data show that increased RONS production is associated with increased calpain activation and/or elevated calpain protein level, leading to epithelial or endothelial barrier dysfunction, neovascularization, lung inflammation, increased smooth muscle cell proliferation, and deposition of extracellular matrix protein. (elsevierpure.com)
  • Calpains are an essential protein that regulates this process, prompting researchers to investigate whether silencing calpains minimizes TBI-related brain damage. (asbmb.org)
  • Very little is known regarding the functions and substrates of Calpain 5. (uky.edu)
  • The calcium-dependent cytosolic, neutral, thiol endopeptidases, calpains, perform limited cleavage of their substrates thereby irreversibly changing their functions. (elsevierpure.com)
  • mining calpain substrates. (ecolowood.com)
  • As our previous study [28] demonstrated that p94 has substrate specificities very similar to those of the - and m-calpains, studies on p94 substrates would contribute to the understanding of brain-specific diseases that involve the conventional calpains. (ecolowood.com)
  • Considering that more than 100 proteins have been identified as substrates of conventional calpains [1], many p94 substrates have not yet been identified because of the constraints of conventional detection methods. (ecolowood.com)
  • reagents prior to MS allows identification and quantification of the same peptide derived from different origins, substrates of conventional calpains that is proteolyzed during ischemia, was readily detected to be proteolyzed by p94. (ecolowood.com)
  • To possibly avert the risks linked to hormone therapy, drug developers in the future may choose to target calpain directly. (healthjockey.com)
  • Under these physiological conditions, a transient and localized influx of calcium into the cell activates a small local population of calpains (for example, those close to Ca2+ channels), which then advance the signal transduction pathway by catalyzing the controlled proteolysis of its target proteins. (wikipedia.org)
  • Label-free CARS imaging of myelin coupled with multiphoton fluorescence imaging of immuno-labeled proteins at the nodes of Ranvier revealed that high-frequency stimulation induced paranodal myelin retraction via pathologic calcium influx into axons, calpain activation, and cytoskeleton degradation through spectrin break-down. (purdue.edu)
  • Gefitinib (Iressa) Inhibition of calpain by ZVP decreased CCK-induced harm from the actin-associated proteins as well as the mobile ultrastructure like the actin cytoskeleton. (academicediting.org)
  • Support of our data is normally provided by a report demonstrating a defensive aftereffect of calpain inhibition in cerulein-induced severe pancreatitis from the mouse (Virlos 2004). (academicediting.org)
  • Enhanced calpain activity, regulated by CAPNS1, significantly contributes to platelet hyperreactivity under hypoxic environment. (wikipedia.org)
  • channel/calpain signaling contributes to high glucose-induced podocyte injury. (bvsalud.org)
  • Taken together, our results suggest that enhanced signaling via an Orai1/SOCE/ Calpain axis contributes to HG-induced podocyte injury . (bvsalud.org)
  • An analysis of all miRNA interaction data was performed for each database to determine trends in miRNA interaction data and to compare the interactions for the calpain system targets to interaction data for all other genes. (umaine.edu)
  • Overactivation of calpain or mutations in the calpain genes contribute to a number of pathological conditions including neurodegenerative disorders, rheumatoid arthritis, cancer, and lung diseases. (elsevierpure.com)
  • Variants in Genes of Calpain System as Modifiers of Spinocerebellar Ataxia Type 3 Phenotype. (cdc.gov)
  • CAST and CAPNS1 appear to be the most highly targeted by miRNA among the five calpain system members investigated. (umaine.edu)
  • We investigated PDE6A expression, cyclic guanosine mono-phosphate accumulation, calpain and caspase activity, in vivo retinal function and morphology, as well as photoreceptor cell death and survival. (nih.gov)
  • While calpain activity was strongly increased in all four mutants, caspase activity was not. (nih.gov)
  • Arguably, the best currently available fluorogenic calpain substrate is (EDANS)-Glu-Pro-Leu-Phe=Ala-Glu-Arg-Lys-(DABCYL), with cleavage occurring at the Phe=Ala bond. (wikipedia.org)
  • Calpain activity was determined using a calpain-specific substrate in the absence or presence of calcium. (fabiopacelli.it)
  • Calpain 5 (CAPN5), which lacks the penta-EF hand domain of classical calpains, is the 2nd most highly expressed calpain in the CNS. (uky.edu)
  • Here, we used our calpain-1 null mouse model to evaluate the function of calpain-1 in neural degeneration following a rodent model of traumatic brain injury. (uic.edu)
  • Furthermore, we determined that calcium overload-induced calpain activation and subsequent oxidative stress and mitochondrial dysfunction are required for epi-1-mediated cytotoxicity. (tmu.edu.tw)
  • Phosphorylation improves proteolytic activity and stimulates auto-activation of μ-calpains. (wikipedia.org)
  • In the present study, we sought to determine whether increased SOCE contributed to high glucose (HG)-induced podocyte injury through activation of the calpain pathway. (bvsalud.org)
  • Real-Time CARS Imaging Reveals a Calpain-Dependent Pathway for Paranod" by Terry B. Huff, Yunzhou Shi et al. (purdue.edu)
  • Real-Time CARS Imaging Reveals a Calpain-Dependent Pathway for Paranodal Myelin Retraction during High-Frequency Stimulation. (purdue.edu)
  • and Cheng, Ji-Xin, "Real-Time CARS Imaging Reveals a Calpain-Dependent Pathway for Paranodal Myelin Retraction during High-Frequency Stimulation. (purdue.edu)
  • In the brain, while μ-calpain is mainly located in the cell body and dendrites of neurons and to a lesser extent in axons and glial cells, m-calpain is found in glia and a small number in axons. (wikipedia.org)
  • Results provide evidence of the important role of the calpain proteolytic system in the pathogenesis of neurodegenerative diseases with tau neurofibrillary pathology (1). (klamar-reagent.com)
  • Although the physiological role of calpains is still poorly understood, they have been shown to be active participants in processes such as cell mobility and cell cycle progression, as well as cell-type specific functions such as long-term potentiation in neurons and cell fusion in myoblasts. (wikipedia.org)
  • Their results showed therapeutic promise, with observed reductions in cell death and tissue degeneration when silencing calpain-1. (asbmb.org)
  • Further investigation of the redox-dependent calpain signaling may provide future targets for the prevention and treatment of COPD. (elsevierpure.com)
  • Here, we show that expression of calpain 2 is required for the dispersal of glioblastoma cells in a living brain microenvironment. (oregonstate.edu)
  • This study demonstrates that calpain 2 expression is required for the dispersal of glioblastoma cells within the dynamic microenvironment of the brain, identifying zebrafish as a valuable orthotopic system for studying glioblastoma cell invasion. (oregonstate.edu)
  • 2013, Graduate Research, Investigating Calpain Expression on Tau Toxicity. (cmich.edu)
  • Detergent fractionation revealed the cytosolic localization of calpain. (wikipedia.org)
  • However, increased calcium concentration overruns the effects of phosphorylation and dephosphorylation on calpain activity, and thus calpain activity ultimately depends on the presence of calcium. (wikipedia.org)
  • In this respect calpain continues to be reported to are likely involved in a number of illnesses including neurodegenerative illnesses muscular dystrophies and cataract advancement (Carafoli & Molinari Gefitinib (Iressa) 1998). (academicediting.org)
  • Calpain activity may be increased in muscle from gastric cancer patients even before changes in molecular markers of muscle wasting and significant weight loss occur. (fabiopacelli.it)
  • The C. elegans orthologue of Calpain 5, Tra-3, regulates transcriptional activity involved in sex determination. (uky.edu)
  • Lp82 was lens-specific, and the lens nucleus contained the highest specific activity of Lp82 and very little m-calpain. (elsevierpure.com)
  • Calpain activity was increased by 70% in cancer patients compared with controls. (fabiopacelli.it)
  • The invasion study was repeated in organotypic mouse brain tissues, and calpain 2 knockdown cells demonstrated a 2.3-fold lower area of dispersal compared with control cells. (oregonstate.edu)