A homologous group of endogenous CYSTEINE PROTEINASE INHIBITORS. The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN, and other peptidases which have a sulfhydryl group at the active site.
A group of closely-related cystatins found in SALIVA.
An intracellular cystatin subtype that is found in a broad variety of cell types. It is a cytosolic enzyme inhibitor that protects the cell against the proteolytic action of lysosomal enzymes such as CATHEPSINS.
Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.
A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.
An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.
A cystatin subtype that has a diverse tissue distribution, target specificity, and functions as an endogenous inhibitor of lysosomal cysteine proteases.
A cytastin subtype found at high levels in the SKIN and in BLOOD CELLS. Cystatin A incorporates into the cornified cell envelope of stratified squamous epithelial cells and may play a role in bacteriostatic properties of skin.
A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
An extracellular cystatin subtype that is abundantly expressed in bodily fluids. It may play a role in the inhibition of interstitial CYSTEINE PROTEASES.
A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.
Proteins and peptides found in SALIVA and the SALIVARY GLANDS. Some salivary proteins such as ALPHA-AMYLASES are enzymes, but their composition varies in different individuals.
A sulfhydryl proteinase with cysteine at the active site from ficus latex. Preferential cleavage is at tyrosine and phenylalanine residues. EC 3.4.22.3.
Endogenous peptides present in most body fluids. Certain enzymes convert them to active KININS which are involved in inflammation, blood clotting, complement reactions, etc. Kininogens belong to the cystatin superfamily. They are cysteine proteinase inhibitors. HIGH-MOLECULAR-WEIGHT KININOGEN; (HMWK); is split by plasma kallikrein to produce BRADYKININ. LOW-MOLECULAR-WEIGHT KININOGEN; (LMWK); is split by tissue kallikrein to produce KALLIDIN.
ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.
A lipocalin that was orignally characterized from human TEARS. It is expressed primarily in the LACRIMAL GLAND and the VON EBNER GLANDS. Lipocalin 1 may play a role in olfactory transduction by concentrating and delivering odorants to the ODORANT RECEPTORS.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
The clear, viscous fluid secreted by the SALIVARY GLANDS and mucous glands of the mouth. It contains MUCINS, water, organic salts, and ptylin.
A plant genus of the family POACEAE. The EDIBLE GRAIN, barley, is widely used as food.
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)

Cathepsin B immunohistochemical staining in tumor and endothelial cells is a new prognostic factor for survival in patients with brain tumors. (1/642)

The cysteine endopeptidase, cathepsin (Cat) B, and its endogenous inhibitor, stefin A, were found relevant for cancer progression of many neoplasms, including human brain tumors. Histological sections of 100 primary brain tumors, 27 benign and 73 malignant, were stained immunohistochemically for Cat B and stefin A. The immunohistochemical staining of Cat B in tumor cells, endothelial cells, and macrophages was scored separately from 0-12. The score in tumor and endothelial cells was significantly higher in malignant tumors compared with benign tumors (P<0.000). A significant correlation between immunostaining of Cat B (scored together for tumor and endothelial cells) and clinical parameters, such as duration of symptoms, Karnofsky score, psycho-organic symptoms, and histological score was demonstrated. Univariate survival analysis indicated that total Cat B score above 8 was a significant predictor for shorter overall survival (P = 0.003). In glioblastoma multiforme, intense Cat B staining of endothelial cells was a significant predictor for shorter survival (P = 0.003). Stefin A immunostaining was weak and detected only in a few benign and some malignant tumors, suggesting that this inhibitor alone is not sufficient in balancing proteolytic activity of Cat B. We conclude that specific immunostaining of Cat B in tumor and endothelial cells can be used to predict the risk of death in patients with primary tumors of the central nervous system.  (+info)

Intracellular accumulation of the amyloidogenic L68Q variant of human cystatin C in NIH/3T3 cells. (2/642)

AIM: To study the cellular transport of L68Q cystatin C, the cystatin variant causing amyloidosis and brain haemorrhage in patients suffering from hereditary cystatin C amyloid angiopathy (HCCAA). METHODS: Expression vectors for wild-type and L68Q cystatin C were constructed and used to transfect mouse NIH/3T3 cells. Stable cell clones were isolated after cotransfection with pSV2neo. Clones expressing human wild-type and L68Q cystatin C were compared with respect to secreted cystatin C by enzyme linked immunosorbent assay (ELISA), and for intracellular cystatin C by western blotting and immunofluorescence cytochemistry. Colocalisation studies in cells were performed by double staining with antibodies against human cystatin C and marker proteins for lysosomes, the Golgi apparatus, or the endoplasmic reticulum, and evaluated by confocal microscopy. RESULTS: Concentrations of human cystatin C secreted from transfected NIH/3T3 cells were similar to those secreted from human cells in culture. In general, clones expressing the gene encoding L68Q cystatin C secreted slightly lower amounts of the protein than clones expressing wild-type human cystatin C. Both immunofluorescence cytochemistry and western blotting experiments showed an increased accumulation of cystatin C in cells expressing the gene encoding L68Q cystatin C compared with cells expressing the gene for the wild-type protein. The intracellularly accumulating L68Q cystatin C was insoluble and located mainly in the endoplasmic reticulum. CONCLUSIONS: The cellular transport of human cystatin C is impeded by the pathogenic amino acid substitution Leu68-->Gln. The resulting intracellular accumulation and increased localised concentration of L68Q cystatin C might be an important event in the molecular pathophysiology of amyloid formation and brain haemorrhage in patients with HCCAA.  (+info)

Hydrophobic sequences can substitute for the wild-type N-terminal sequence of cystatin A (stefin A) in tight binding to cysteine proteinases selection of high-affinity N-terminal region variants by phage display. (3/642)

A phage-display library of the cysteine-proteinase inhibitor, cystatin A, was constructed in which variants with the four N-terminal amino acids randomly mutated were expressed on the surface of filamenteous phage. Screening of this library for binding to papain gave predominantly variants with a glycine residue in position 4. This finding is in agreement with previous conclusions that glycine in this position is essential for tight binding of cystatin A to cysteine proteinases by allowing optimal interaction of the N-terminal region of the inhibitor with the enzyme. In contrast, the first three residues of the variants obtained by the screening were more variable. Two variants were identified with similar affinities for papain as the wild-type inhibitor, but with these residues, Val-Phe-Thr- or Ile-Leu-Leu, differing appreciably from those of the wild-type, Met-Ile-Pro. Other sequences of the N-terminal region, presumably mainly hydrophobic, can thus substitute for the wild-type sequence and contribute similar energy to the inhibitor-proteinase interaction. The two variants binding tightly to papain differed in their affinity for cathepsin B, demonstrating that cystatin variants with increased selectivity for a particular target cysteine proteinase can be obtained by phage-display technology.  (+info)

Structure, alternative splicing and chromosomal localization of the cystatin-related epididymal spermatogenic gene. (4/642)

The cystatin superfamily of cysteine protease inhibitors consists of three major families, including the stefins, cystatins and kininogens. However, the recent identification of several genes that possess sequence similarity with the cystatins but have different gene or protein structures indicates that several new cystatin families or subgroups of families might exist. We previously identified the cystatin-related epididymal spermatogenic (Cres) gene, which is related to the family 2 cystatins but exhibits highly tissue-specific expression in the reproductive tract. In the studies presented here, an analysis of gene structure as well as chromosomal mapping studies suggest that the Cres gene might represent a new subgroup within the family 2 cystatins. Although the Cres gene possesses an additional exon encoding 5' untranslated sequences, its coding exons are similar in size to the three coding exons of the cystatin family 2 genes, and the Cres exon/intron splice junctions occur in identical locations as in the cystatin C gene. Furthermore, chromosomal mapping studies show that the Cres gene co-segregates with the cystatin C gene on mouse chromosome 2. Similar to the cystatin family 2 proteins, the Cres protein possesses the type A and B disulphide loops that are necessary for cystatin folding. Interestingly, Cres protein also possesses half of a type C disulphide loop. Although probably related to the cystatin genes, the Cres gene is distinct in that its promoter contains consensus motifs typical of regulated genes. Finally, reverse transcriptase-mediated PCR studies and the identification of new Cres cDNA clones indicate that the Cres mRNA is alternatively spliced, resulting in two Cres mRNAs that might be involved in the regulation of Cres function.  (+info)

Immunolocalization of CRES (Cystatin-related epididymal spermatogenic) protein in the acrosomes of mouse spermatozoa. (5/642)

The CRES (cystatin-related epididymal spermatogenic) protein is a member of the cystatin superfamily of cysteine protease inhibitors and exhibits highly restricted expression in the reproductive tract. We have previously shown that CRES protein is present in elongating spermatids in the testis and is synthesized and secreted by the proximal caput epididymal epithelium. The presence of CRES protein in developing germ cells and in the luminal fluid surrounding maturing spermatozoa prompted us to examine whether CRES protein is associated with spermatozoa. In the studies presented, indirect immunofluorescence, immunogold electron microscopy, and Western blot analysis demonstrated that CRES protein is localized in sperm acrosomes and is released during the acrosome reaction. Interestingly, while the 19- and 14-kDa CRES proteins were present in testicular and proximal caput epididymal spermatozoa, the 14-kDa CRES protein was the predominant form present in mid-caput to cauda epididymal spermatozoa. Furthermore, following the ionophore-induced acrosome reaction, CRES protein localization was similar to that of proacrosin/acrosin in that it was detected in the soluble fraction as well as associated with the acrosome-reacted spermatozoa. The presence of CRES protein in the sperm acrosome, a site of high hydrolytic and proteolytic activity, suggests that CRES may play a role in the regulation of intraacrosomal protein processing or may be involved in fertilization.  (+info)

The affinity and kinetics of inhibition of cysteine proteinases by intact recombinant bovine cystatin C. (6/642)

Recent studies have shown that the bovine cysteine proteinase inhibitor, cystatin C, is synthesized as a preprotein containing a 118-residue mature protein. However, the forms of the inhibitor isolated previously from bovine tissues had shorter N-terminal regions than expected from these results, and also lower affinity for proteinases than human cystatin C. In this work, we report the properties of recombinant, full-length bovine cystatin C having a complete N-terminal region. The general characteristics of this form of the inhibitor, as reflected by the isoelectric point, the far-ultraviolet circular dichroism spectrum, the thermal stability and the changes of tryptophan fluorescence on interaction with papain, resembled those of human cystatin C. The affinity and kinetics of inhibition of papain and cathepsins B, H and L by the bovine inhibitor were also comparable with those of the human inhibitor, although certain differences were apparent. Notably, the affinity of bovine cystatin C for cathepsin H was somewhat weaker than that of human cystatin C, and bovine cystatin C bound to cathepsin L with about a four-fold higher association rate constant than the human inhibitor. This rate constant is comparable with the highest values reported previously for cystatin-cysteine proteinase reactions. The full-length, recombinant bovine cystatin C bound appreciably more tightly to proteinases than the shorter form characterized previously. Digestion of the recombinant inhibitor with neutrophil elastase resulted in forms with truncated N-terminal regions and appreciably decreased affinity for papain, consistent with the forms of bovine cystatin C isolated previously having arisen by proteolytic cleavage of a mature, full-length inhibitor.  (+info)

Inhibition of mammalian legumain by some cystatins is due to a novel second reactive site. (7/642)

We have investigated the inhibition of the recently identified family C13 cysteine peptidase, pig legumain, by human cystatin C. The cystatin was seen to inhibit enzyme activity by stoichiometric 1:1 binding in competition with substrate. The Ki value for the interaction was 0.20 nM, i.e. cystatin C had an affinity for legumain similar to that for the papain-like family C1 cysteine peptidase, cathepsin B. However, cystatin C variants with alterations in the N-terminal region and the "second hairpin loop" that rendered the cystatin inactive against cathepsin B, still inhibited legumain with Ki values 0.2-0.3 nM. Complexes between cystatin C and papain inhibited legumain activity against benzoyl-Asn-NHPhNO2 as efficiently as did cystatin C alone. Conversely, cystatin C inhibited papain activity against benzoyl-Arg-NHPhNO2 whether or not the cystatin had been incubated with legumain, strongly indicating that the cystatin inhibited the two enzymes with non-overlapping sites. A ternary complex between legumain, cystatin C, and papain was demonstrated by gel filtration supported by immunoblotting. Screening of a panel of cystatin superfamily members showed that type 1 inhibitors (cystatins A and B) and low Mr kininogen (type 3) did not inhibit pig legumain. Of human type 2 cystatins, cystatin D was non-inhibitory, whereas cystatin E/M and cystatin F displayed strong (Ki 0.0016 nM) and relatively weak (Ki 10 nM) affinity for legumain, respectively. Sequence alignments and molecular modeling led to the suggestion that a loop located on the opposite side to the papain-binding surface, between the alpha-helix and the first strand of the main beta-pleated sheet of the cystatin structure, could be involved in legumain binding. This was corroborated by analysis of a cystatin C variant with substitution of the Asn39 residue in this loop (N39K-cystatin C); this variant showed a slight reduction in affinity for cathepsin B (Ki 1.5 nM) but >>5,000-fold lower affinity for legumain (Ki >>1,000 nM) than wild-type cystatin C.  (+info)

Cathepsin L is capable of truncating cystatin C of 11 N-terminal amino acids. (8/642)

Cystatin C with the 11 N-terminal amino acids truncated shows a much lower affinity for cysteine proteinases than the intact inhibitor. Such truncation of cystatin C is recorded after action of glycyl endopeptidase and cathepsin L. Incubation of cystatin C with papain, cathepsin B or cathepsin H led to no changes in the cystatin C molecule. Isoelectric focusing of the cathepsin L and cystatin C mixture showed the formation of two new bands. One of them appeared whether E-64 or PMSF was added or not, evidently representing a cystatin C/cathepsin L complex. The other band is the truncated cystatin C molecule. N-terminal sequencing after separation by HPLC showed that cystatin C is cleaved by cathepsin L at the Gly11-Gly12 bond. The action of cathepsin L on cystatin C may be explained by the cleavage of the scissile bond in an inappropriate complex.  (+info)

Cystatins are a group of proteins that inhibit cysteine proteases, which are enzymes that break down other proteins. Cystatins are found in various biological fluids and tissues, including tears, saliva, seminal plasma, and urine. They play an important role in regulating protein catabolism and protecting cells from excessive protease activity. There are three main types of cystatins: type 1 (cystatin C), type 2 (cystatin M, cystatin N, and fetuin), and type 3 (kininogens). Abnormal levels of cystatins have been associated with various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders.

Salivary cystatins are a group of proteins that belong to the cystatin superfamily and are found in saliva. They function as inhibitors of cysteine proteases, which are enzymes that break down other proteins. Specifically, salivary cystatins help regulate the activity of these proteases in the oral cavity and protect the soft tissues of the mouth from degradation. There are several types of salivary cystatins, including cystatin A, B, C, D, SN, S, SA, and SB, each with different properties and functions. Some salivary cystatins have been studied for their potential role in oral health and disease, such as caries prevention and protection against oral cancer.

Cystatin B is a type of protease inhibitor that belongs to the cystatin superfamily. It is primarily produced in the central nervous system and is found in various body fluids, including cerebrospinal fluid and urine. Cystatin B plays a crucial role in regulating protein catabolism by inhibiting lysosomal cysteine proteases, which are enzymes that break down proteins.

Defects or mutations in the gene that encodes for cystatin B have been associated with a rare inherited neurodegenerative disorder known as Uner Tan Syndrome (UTS). UTS is characterized by language impairment, mental retardation, and distinctive facial features. The exact mechanism by which cystatin B deficiency leads to this disorder is not fully understood, but it is thought to involve the dysregulation of protein catabolism in neurons, leading to neurotoxicity and neurodegeneration.

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.

Papain is defined as a proteolytic enzyme that is derived from the latex of the papaya tree (Carica papaya). It has the ability to break down other proteins into smaller peptides or individual amino acids. Papain is widely used in various industries, including the food industry for tenderizing meat and brewing beer, as well as in the medical field for its digestive and anti-inflammatory properties.

In medicine, papain is sometimes used topically to help heal burns, wounds, and skin ulcers. It can also be taken orally to treat indigestion, parasitic infections, and other gastrointestinal disorders. However, its use as a medical treatment is not widely accepted and more research is needed to establish its safety and efficacy.

Cathepsin H is a lysosomal cysteine protease that plays a role in intracellular protein degradation and turnover. It is expressed in various tissues, including the spleen, thymus, lungs, and immune cells. Cathepsin H has been implicated in several physiological processes, such as antigen presentation, bone resorption, and extracellular matrix remodeling. Additionally, its dysregulation has been associated with various pathological conditions, including cancer, neurodegenerative disorders, and infectious diseases.

The enzyme's active site contains a catalytic triad composed of cysteine, histidine, and aspartic acid residues, which facilitates the proteolytic activity. Cathepsin H exhibits specificity for peptide bonds containing hydrophobic or aromatic amino acids, making it an important player in processing and degrading various cellular proteins.

In summary, Cathepsin H is a lysosomal cysteine protease involved in protein turnover and degradation with potential implications in several pathological conditions when dysregulated.

Cystatin M is a type of cysteine protease inhibitor that is primarily expressed in the epididymis, a tube-like structure in the male reproductive system where sperm maturation occurs. It belongs to the cystatin superfamily, which are proteins that regulate protein catabolism by inhibiting the activity of cysteine proteases.

Cystatin M is encoded by the CST6 gene and has been shown to play a role in sperm maturation and fertility. It is secreted into the lumen of the epididymis, where it interacts with sperm and other proteins to regulate their function. Mutations in the CST6 gene have been associated with male infertility, suggesting that cystatin M plays an important role in reproductive health.

In addition to its role in the male reproductive system, cystatin M has also been found in other tissues and may have additional functions beyond regulating cysteine proteases. However, further research is needed to fully understand the physiological roles of this protein.

Cystatin A is a type of cysteine protease inhibitor that is primarily produced by cells of the immune system. It is a small protein consisting of 120 amino acids and is encoded by the CSTA gene in humans. Cystatin A functions to regulate the activity of cathepsins, which are enzymes that break down proteins in the body.

Cystatin A is mainly found inside cells, where it helps to maintain the balance of cathepsins and prevent excessive protein degradation. However, it can also be released into extracellular spaces under certain conditions, such as inflammation or cell damage. In the extracellular space, cystatin A may help to regulate the activity of cathepsins in the surrounding tissue and contribute to the regulation of immune responses.

Abnormal levels of cystatin A have been associated with various diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. However, more research is needed to fully understand the role of cystatin A in these conditions and its potential as a therapeutic target.

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.

Cathepsins are a type of proteolytic enzymes, which are found in lysosomes and are responsible for breaking down proteins inside the cell. They are classified as papain-like cysteine proteases and play important roles in various physiological processes, including tissue remodeling, antigen presentation, and apoptosis (programmed cell death). There are several different types of cathepsins, including cathepsin B, C, D, F, H, K, L, S, V, and X/Z, each with distinct substrate specificities and functions.

Dysregulation of cathepsins has been implicated in various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders. For example, overexpression or hyperactivation of certain cathepsins has been shown to contribute to tumor invasion and metastasis, while their inhibition has been explored as a potential therapeutic strategy in cancer treatment. Similarly, abnormal levels of cathepsins have been linked to the progression of neurodegenerative diseases like Alzheimer's and Parkinson's, making them attractive targets for drug development.

Cystatin C is a protein produced by many cells in the body, including all types of nucleated cells. It is a member of the cysteine protease inhibitor family and functions as an endogenous inhibitor of cathepsins, which are proteases involved in various physiological and pathological processes such as extracellular matrix degradation, antigen presentation, and cell death.

Cystatin C is freely filtered by the glomeruli in the kidneys and almost completely reabsorbed and catabolized by the proximal tubules. Therefore, its serum concentration is a reliable marker of glomerular filtration rate (GFR) and can be used to estimate kidney function.

Increased levels of cystatin C in the blood may indicate impaired kidney function or kidney disease, while decreased levels are less common and may be associated with hyperfiltration or overproduction of cystatin C. Measuring cystatin C levels can complement or supplement traditional methods for assessing kidney function, such as estimating GFR based on serum creatinine levels.

Cathepsin B is a lysosomal cysteine protease that plays a role in various physiological processes, including intracellular protein degradation, antigen presentation, and extracellular matrix remodeling. It is produced as an inactive precursor (procathepsin B) and activated upon cleavage of the propeptide by other proteases or autocatalytically. Cathepsin B has a wide range of substrates, including collagen, elastin, and various intracellular proteins. Its dysregulation has been implicated in several pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders.

Salivary proteins and peptides refer to the diverse group of molecules that are present in saliva, which is the clear, slightly alkaline fluid produced by the salivary glands in the mouth. These proteins and peptides play a crucial role in maintaining oral health and contributing to various physiological functions.

Some common types of salivary proteins and peptides include:

1. **Mucins**: These are large, heavily glycosylated proteins that give saliva its viscous quality. They help to lubricate the oral cavity, protect the mucosal surfaces, and aid in food bolus formation.
2. **Amylases**: These enzymes break down carbohydrates into simpler sugars, initiating the digestive process even before food reaches the stomach.
3. **Proline-rich proteins (PRPs)**: PRPs contribute to the buffering capacity of saliva and help protect against tooth erosion by forming a protective layer on tooth enamel.
4. **Histatins**: These are small cationic peptides with antimicrobial properties, playing a significant role in maintaining oral microbial homeostasis and preventing dental caries.
5. **Lactoferrin**: An iron-binding protein that exhibits antibacterial, antifungal, and anti-inflammatory activities, contributing to the overall oral health.
6. **Statherin and Cystatins**: These proteins regulate calcium phosphate precipitation, preventing dental calculus formation and maintaining tooth mineral homeostasis.

Salivary proteins and peptides have attracted significant interest in recent years due to their potential diagnostic and therapeutic applications. Alterations in the composition of these molecules can provide valuable insights into various oral and systemic diseases, making them promising biomarkers for disease detection and monitoring.

Ficain is not typically defined in the context of human medicine, but it is a term used in biochemistry and molecular biology. Ficain is a proteolytic enzyme, also known as ficin, that is isolated from the latex of the fig tree (Ficus species). It has the ability to break down other proteins into smaller peptides or individual amino acids by cleaving specific peptide bonds. Ficain is often used in research and industrial applications, such as protein degradation, digestion studies, and biochemical assays.

Kininogens are a group of proteins found in the blood plasma that play a crucial role in the inflammatory response and blood coagulation. They are precursors to bradykinin, a potent vasodilator and inflammatory mediator. There are two types of kininogens: high molecular weight kininogen (HMWK) and low molecular weight kininogen (LMWK). HMWK is involved in the intrinsic pathway of blood coagulation, while LMWK is responsible for the release of bradykinin. Both kininogens are important targets in the regulation of inflammation and hemostasis.

Cysteine endopeptidases are a type of enzymes that cleave peptide bonds within proteins. They are also known as cysteine proteases or cysteine proteinases. These enzymes contain a catalytic triad consisting of three amino acids: cysteine, histidine, and aspartate. The thiol group (-SH) of the cysteine residue acts as a nucleophile and attacks the carbonyl carbon of the peptide bond, leading to its cleavage.

Cysteine endopeptidases play important roles in various biological processes, including protein degradation, cell signaling, and inflammation. They are involved in many physiological and pathological conditions, such as apoptosis, immune response, and cancer. Some examples of cysteine endopeptidases include cathepsins, caspases, and calpains.

It is important to note that these enzymes require a reducing environment to maintain the reduced state of their active site cysteine residue. Therefore, they are sensitive to oxidizing agents and inhibitors that target the thiol group. Understanding the structure and function of cysteine endopeptidases is crucial for developing therapeutic strategies that target these enzymes in various diseases.

Cathepsin L is a lysosomal cysteine protease that plays a role in various physiological processes, including protein degradation, antigen presentation, and extracellular matrix remodeling. It is produced as an inactive precursor and activated by cleavage of its propeptide domain. Cathepsin L has a broad specificity for peptide bonds and can cleave both intracellular and extracellular proteins, making it an important player in various pathological conditions such as cancer, neurodegenerative diseases, and infectious diseases. Inhibition of cathepsin L has been explored as a potential therapeutic strategy for these conditions.

Lipocalin 1, also known as neutrophil gelatinase-associated lipocalin (NGAL), is a protein that belongs to the lipocalin family. It is a small secreted protein with a molecular weight of approximately 25 kDa and is composed of a single polypeptide chain.

Lipocalin 1 is primarily produced by neutrophils, but can also be expressed in other tissues such as the kidney, liver, and lungs. It plays a role in the innate immune response by binding to bacterial siderophores, preventing bacterial growth by limiting their access to iron.

In addition, Lipocalin 1 has been identified as a biomarker for early detection of acute kidney injury (AKI). Its expression is rapidly upregulated in the kidney in response to injury, and its levels can be measured in urine and blood. Increased urinary Lipocalin 1 levels have been shown to predict AKI with high sensitivity and specificity, making it a promising diagnostic tool for this condition.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Cathepsin F is a lysosomal cysteine protease that belongs to the papain family. It is primarily expressed in hematopoietic cells, including monocytes, macrophages, and dendritic cells. Cathepsin F plays a role in various physiological processes, such as antigen presentation, bone remodeling, and extracellular matrix degradation. It is also implicated in several pathological conditions, such as cancer, neurodegenerative disorders, and infectious diseases.

Cathepsin F has a broad substrate specificity and can cleave various proteins, including collagen, elastin, and casein. Its activity is tightly regulated by endogenous inhibitors, such as cystatins and stefins, to prevent excessive protein degradation and tissue damage.

In summary, Cathepsin F is a lysosomal enzyme involved in various physiological and pathological processes, with a broad substrate specificity and regulatory mechanisms.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Protease inhibitors are a class of antiviral drugs that are used to treat infections caused by retroviruses, such as the human immunodeficiency virus (HIV), which is responsible for causing AIDS. These drugs work by blocking the activity of protease enzymes, which are necessary for the replication and multiplication of the virus within infected cells.

Protease enzymes play a crucial role in the life cycle of retroviruses by cleaving viral polyproteins into functional units that are required for the assembly of new viral particles. By inhibiting the activity of these enzymes, protease inhibitors prevent the virus from replicating and spreading to other cells, thereby slowing down the progression of the infection.

Protease inhibitors are often used in combination with other antiretroviral drugs as part of highly active antiretroviral therapy (HAART) for the treatment of HIV/AIDS. Common examples of protease inhibitors include saquinavir, ritonavir, indinavir, and atazanavir. While these drugs have been successful in improving the outcomes of people living with HIV/AIDS, they can also cause side effects such as nausea, diarrhea, headaches, and lipodystrophy (changes in body fat distribution).

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Saliva is a complex mixture of primarily water, but also electrolytes, enzymes, antibacterial compounds, and various other substances. It is produced by the salivary glands located in the mouth. Saliva plays an essential role in maintaining oral health by moistening the mouth, helping to digest food, and protecting the teeth from decay by neutralizing acids produced by bacteria.

The medical definition of saliva can be stated as:

"A clear, watery, slightly alkaline fluid secreted by the salivary glands, consisting mainly of water, with small amounts of electrolytes, enzymes (such as amylase), mucus, and antibacterial compounds. Saliva aids in digestion, lubrication of oral tissues, and provides an oral barrier against microorganisms."

I'm sorry for any confusion, but "Hordeum" is not a medical term. It is actually the genus name for barley in botany. If you have any medical terms or concepts that you would like me to explain, please let me know!

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.

Type 1 cystatins are also known as Stefins (after the Stefan Institute where they were first discovered ) The Type 2 cystatins ... Cystatins show similarity to fetuins, kininogens, histidine-rich glycoproteins and cystatin-related proteins. Cystatins mainly ... The cystatins are a family of cysteine protease inhibitors which share a sequence homology and a common tertiary structure of ... Cystatins at the U.S. National Library of Medicine Medical Subject Headings (MeSH) This article incorporates text from the ...
Magister, Špela; Kos, Janko (2012-12-20). "Cystatins in Immune System". Journal of Cancer. 4 (1): 45-56. doi:10.7150/jca.5044. ...
Cystatins are proteins that inhibit cysteine proteases. Research are ongoing to evaluate the potential of using cystatins in ... Tremblay J, Goulet MC, Michaud D (November 2019). "Recombinant cystatins in plants". Biochimie. 166: 184-193. doi:10.1016/j. ... Homology with animal cystatins and transient expression in the ripening process of rice seeds". The Journal of Biological ...
There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the ... Barka T, Asbell PA, van der Noen H, Prasad A (1991). "Cystatins in human tear fluid". Curr. Eye Res. 10 (1): 25-34. doi:10.3109 ... "Cystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatins". J Biol Chem. 272 ...
There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the ... Cystatin-S is a protein that in humans is encoded by the CST4 gene. The cystatin superfamily encompasses proteins that contain ... Determination of cystatins, albumin, amylase and IgA". Journal of Periodontal Research. 31 (1): 57-65. doi:10.1111/j.1600- ... Dickinson DP, Zhao Y, Thiesse M, Siciliano MJ (1995). "Direct mapping of seven genes encoding human type 2 cystatins to a ...
There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and ... "Entrez Gene: CSTB cystatin B (stefin B)". Pavlova, Alona; Björk Ingemar (Sep 2003). "Grafting of features of cystatins C or B ... Järvinen M, Rinne A, Hopsu-Havu VK (1988). "Human cystatins in normal and diseased tissues--a review". Acta Histochem. 82 (1): ... Turk V, Bode W (1991). "The cystatins: protein inhibitors of cysteine proteinases". FEBS Lett. 285 (2): 213-9. doi:10.1016/0014 ...
... cystatins". Biochemical and Biophysical Research Communications. 154 (2): 765-72. doi:10.1016/0006-291X(88)90206-9. PMID ...
Turk V, Stoka V, Turk D (May 2008). "Cystatins: biochemical and structural properties, and medical relevance". Frontiers in ... Turk V, Bode W (July 1991). "The cystatins: protein inhibitors of cysteine proteinases". FEBS Letters. 285 (2): 213-9. doi: ... Derived from the cysteine protease inhibitor family of cystatins, which function in nature as cysteine protease inhibitors, ... is closely related to that of oryzacystatin-I but different from those of animal cystatins". FEBS Letters. 278 (1): 87-90. doi: ...
There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins, and ... "Entrez Gene: CSTA cystatin A (stefin A)". Pavlova, Alona; Björk Ingemar (Sep 2003). "Grafting of features of cystatins C or B ... Järvinen M, Rinne A, Hopsu-Havu VK (1988). "Human cystatins in normal and diseased tissues--a review". Acta Histochem. 82 (1): ... Davies ME, Barrett AJ (1984). "Immunolocalization of human cystatins in neutrophils and lymphocytes". Histochemistry. 80 (4): ...
... s are related to cystatins through their similar glycosylated regions. During the contact activation system (CAS), ...
Similarity to the disulfide bridge structures of cystatins and kininogens". J. Biol. Chem. 264 (24): 14121-8. doi:10.1016/S0021 ...
There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the ... Like other type 2 cystatins, it has two disulfide bonds. Around 50% of the molecules carry a hydroxylated proline. Cystatin C ...
There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the ... Dickinson DP, Zhao Y, Thiesse M, Siciliano MJ (1995). "Direct mapping of seven genes encoding human type 2 cystatins to a ... Isemura S, Saitoh E, Sanada K, Minakata K (1992). "Identification of full-sized forms of salivary (S-type) cystatins (cystatin ... Takahashi M, Honda Y, Ogawa K, Barka T (1993). "Immunofluorescence localization of cystatins in human lacrimal gland and in the ...
Johnsson M, Richardson CF, Bergey EJ, Levine MJ, Nancollas GH (1992). "The effects of human salivary cystatins and statherin on ... Sabatini LM, Warner TF, Saitoh E, Azen EA (1990). "Tissue distribution of RNAs for cystatins, histatins, statherin, and proline ...
Pavlova A, Björk I (September 2003). "Grafting of features of cystatins C or B into the N-terminal region or second binding ... Sloane BF (April 1990). "Cathepsin B and cystatins: evidence for a role in cancer progression". Seminars in Cancer Biology. 1 ( ...
These will inhibit the breakdown of the proteins in group 3. Cystatins are not a gene product previously found in viruses to ...
The toxins that have been confirmed to be within the venom are cystatins, peroxiredoxin and galectin. Galectin induces cell ... death in its victims and cystatins inhibit defense enzymes. In humans, these toxins lead to increased blood flow in the ...
The enzymes lysozyme and peroxidase, defensins, cystatins and an antibody, IgA, are all antibacterial. Thrombospondin and some ...
The Affimer protein scaffold is derived from the cysteine protease inhibitor family of cystatins. Within the protein scaffold ...
There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the ... Dickinson DP, Zhao Y, Thiesse M, Siciliano MJ (1995). "Direct mapping of seven genes encoding human type 2 cystatins to a ...
There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the ... This gene is located in the cystatin locus and encodes a protein similar to type 2 cystatins. The protein exhibits highly ... Dickinson DP, Zhao Y, Thiesse M, Siciliano MJ (1995). "Direct mapping of seven genes encoding human type 2 cystatins to a ...
There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the ... Dickinson DP, Zhao Y, Thiesse M, Siciliano MJ (1995). "Direct mapping of seven genes encoding human type 2 cystatins to a ... Isemura S, Saitoh E, Sanada K, Minakata K (1992). "Identification of full-sized forms of salivary (S-type) cystatins (cystatin ... Takahashi M, Honda Y, Ogawa K, Barka T (1993). "Immunofluorescence localization of cystatins in human lacrimal gland and in the ...
There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the ... Dickinson DP, Zhao Y, Thiesse M, Siciliano MJ (1995). "Direct mapping of seven genes encoding human type 2 cystatins to a ...
There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the ... Dickinson DP, Zhao Y, Thiesse M, Siciliano MJ (1995). "Direct mapping of seven genes encoding human type 2 cystatins to a ...
There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the ... Dickinson DP, Zhao Y, Thiesse M, Siciliano MJ (1995). "Direct mapping of seven genes encoding human type 2 cystatins to a ...
... relationship to cystatins and the tumor suppressor TIG1." Structure 13(2), 309-317, 2005. Cho et al.: "Hypermethylation of CpG ...
There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the ...
LCN1 shares three sequence motifs with cystatins which enables LCN1 to act in a similar manner to cystatins as a cysteine ...
... is inactivated by E-64, making the inhibitor a convenient active-site titrant, and it is inhibited by cystatins, Ki ...
... often by the presence of endogenous protease inhibitors such as cystatins. In many RNA viruses, including significant human ...
... ... in an attempt to study novel Canecystatins, we identified two ORFs encoding cystatins (referred as CaneCPI-2 and CaneCPI-3) ... These findings contribute to a better understanding of the activity of sugarcane cystatins and encourage future activity and ...
beta 2-Strand of salivary S cystatins: A "chemeleon sequence". Vitali, A;Carelli Alinovi, Cristiana;De Rosa, Mc;Petruzzelli, R. ... Secondary structure prediction of salivary cystatins S, SA, and SN carried out by several methods label the 39-58 sequence (β2- ... The results obtained indicate that the β2-strand of salivary S cystatins has high helical propensity when isolated from native ... Secondary structure prediction of salivary cystatins S, SA, and SN carried out by several methods label the 39-58 sequence (β2- ...
Type 1 cystatins are also known as Stefins (after the Stefan Institute where they were first discovered ) The Type 2 cystatins ... Cystatins show similarity to fetuins, kininogens, histidine-rich glycoproteins and cystatin-related proteins. Cystatins mainly ... The cystatins are a family of cysteine protease inhibitors which share a sequence homology and a common tertiary structure of ... Cystatins at the U.S. National Library of Medicine Medical Subject Headings (MeSH) This article incorporates text from the ...
Cystatins / physiology * Cysteine Proteinase Inhibitors / physiology* * Evolution, Molecular * Eye Infections / prevention & ...
These enzymes can be inactivated by specific proteins found in plants called cystatins. Because cystatins interact specifically ... compared to plants without the cystatins. Some plants with cystatins had increased resistance to spring blackstem and leaf spot ... The genes fo two cystatins from rice seeds and the gene for a marker enzyme were fused to a promoting DNA sequence so that the ... Production of cystatins in roots reduced the populations of the root-lesion nematode 71-79% ...
The cDNAs of two novel cystatins .... * Genomic changes associated with somaclonal variation in banana (Musa spp.)  ...
Due to the presence of histatins (proline-rich proteins including cystatins and statherin), calcium and phosphate are ...
Cystatins Medicine & Life Sciences 34% * Fluorescein-5-isothiocyanate Medicine & Life Sciences 28% ...
Level 0 data-placement=right src=/Images/empty.png /> PFR18973: Cystatin-S *Home ...
Klotz C, Ziegler T, Danilowicz-Luebert E, Hartmann S: Cystatins of parasitic organisms. Adv Exp Med Biol. 2011, 712: 208-221. ... Hartmann S, Lucius R: Modulation of host immune responses by nematode cystatins. Int J Parasitol. 2003, 33: 1291-1302. ... cystatins) [19], as well as in the inhibition of host molecules responsible for the initiation of blood coagulation (serpins) [ ... cystatins and serpins, respectively; MEROPS family I25 and I04, respectively) are known to participate in the cascades of ...
This may constitute a mechanism for clearing inappropriately localized cystatins. A pH-dependent conformational variability in ...
Salivary Acidic Protein 1 use Salivary Cystatins Salivary Acquired Pellicle use Dental Pellicle ...
I have a keen interest in methodological issues in epidemiological research and how the Swedish register infrastructure can be used to improve validity. How can we trust results from observational studies, which often get substantial publicity in media? How can we improve risk predictions and our understanding of causes and effects by smarter study designs and novel analytic approaches? One such novel analytic approach is machine learning, i.e. methods where computer programs learn to complete a task, perform classifications or to foresee outcomes based on extensive input data. In an on-going interdisciplinary project called AIR Lund (see www.lupop.lu.se/airlund), partly financed by VINNOVA, we investigate how machine learning methods applied on the Swedish register infrastructure can contribute to improved prevention, diagnosis and prognosis of cardiometabolic diseases. We will critically assess the added value of these methods compared to more simplistic risk scoring schemes and statistical ...
Salivary Acidic Protein 1 use Salivary Cystatins Salivary Acquired Pellicle use Dental Pellicle ...
Salivary Acidic Protein 1 use Salivary Cystatins Salivary Acquired Pellicle use Dental Pellicle ...
Salivary Acidic Protein 1 use Salivary Cystatins Salivary Acquired Pellicle use Dental Pellicle ...
Salivary Acidic Protein 1 use Salivary Cystatins Salivary Acquired Pellicle use Dental Pellicle ...
Shi, J., Shiraishi, K., Choi, J., Matsuo, K., Chen, T. Y., Dai, J., Hung, R. J., Chen, K., Shu, X. O., Kim, Y. T., Landi, M. T., Lin, D., Zheng, W., Yin, Z., Zhou, B., Song, B., Wang, J., Seow, W. J., Song, L., Chang, I. S., 及其他202Hu, W., Chien, L. H., Cai, Q., Hong, Y. C., Kim, H. N., Wu, Y. L., Wong, M. P., Richardson, B. D., Funderburk, K. M., Li, S., Zhang, T., Breeze, C., Wang, Z., Blechter, B., Bassig, B. A., Kim, J. H., Albanes, D., Wong, J. Y. Y., Shin, M. H., Chung, L. P., Yang, Y., An, S. J., Zheng, H., Yatabe, Y., Zhang, X. C., Kim, Y. C., Caporaso, N. E., Chang, J., Ho, J. C. M., Kubo, M., Daigo, Y., Song, M., Momozawa, Y., Kamatani, Y., Kobayashi, M., Okubo, K., Honda, T., Hosgood, D. H., Kunitoh, H., Patel, H., Watanabe, S. I., Miyagi, Y., Nakayama, H., Matsumoto, S., Horinouchi, H., Tsuboi, M., Hamamoto, R., Goto, K., Ohe, Y., Takahashi, A., Goto, A., Minamiya, Y., Hara, M., Nishida, Y., Takeuchi, K., Wakai, K., Matsuda, K., Murakami, Y., Shimizu, K., Suzuki, H., Saito, M., ...
Lu, Y., Van Zandt, M., Liu, Y., Li, J., Wang, X., Chen, Y., Chen, Z., Cho, J., Dorajoo, S. R., Feng, M., Hsu, M. H., Hsu, J. C., Iqbal, U., Jonnagaddala, J., Li, Y. C., Liaw, S. T., Lim, H. S., Ngiam, K. Y., Nguyen, P. A., Park, R. W., & 11 othersPratt, N., Reich, C., Rhee, S. Y., Sathappan, S. M. K., Shin, S. J., Tan, H. X., You, S. C., Zhang, X., Krumholz, H. M., Suchard, M. A. & Xu, H., Mar 24 2022, In: JAMA network open. 5, 3, p. E223877. Research output: Contribution to journal › Article › peer-review ...
Dive into the research topics of Plasma Levels of Middle Molecules to Estimate Residual Kidney Function in Haemodialysis without Urine Collection. Together they form a unique fingerprint. ...
Bobek LA and Levine MJ (1992). Cystatins-inhibitors of cysteine proteinases. Crit. Rev. Oral Biol. Med. 3: 307-332. PMid: ...
Cystatins encode a high functional variability not only because of their ability to inhibit different classes of proteases but ... Mammalian cystatins can form amyloid fibrils; however, the potential for amyloid fibril formation of phytocystatins remains ...
Salivary Cystatins Medicine & Life Sciences 33% * Proteins Medicine & Life Sciences 31% * Protein Databases Medicine & Life ...
... type I cystatins are up-regulated in tumor tissue while type II cystatins are generally down-regulated in tumors [50]. ... Dickinson DP: Salivary (SD-type) cystatins: over one billion years in the making-but to what purpose?. Crit Rev Oral Biol Med. ... Magister S, Kos J: Cystatins in immune system. J Cancer. 2013, 4: 45-56. 10.7150/jca.5044. ... Salivary cystatins are likely to exert certain antiviral effect as they can interfere with events in viral replication [47-52 ...
Cystatins. *Cystine-Knot Miniproteins. *Cytoskeletal Proteins. *Dental Enamel Proteins. *Dietary Proteins. *DNA-Binding ...
Safety assessment of cystatins used to control pests in transgenic bananas in Uganda. [1]. ...
Maquiberry Cystatins: Recombinant Expression, Characterization, and Use to Protect Tooth Dentin and Enamel ...
Octreotide may improve pharyngocutaneous fistula healing through downregulation of cystatins: A pilot study ...
Benchabane M, Schluter U, Vorster J, Goulet M, Michaud D. (2010) Plant cystatins. Biochimie 92(11):1657-1666. 10.1016/j.biochi. ... Tremblay J, Goulet M-C, Vorster J, Goulet C, Michaud M. (2021) Harnessing the functional diversity of plant cystatins to design ... We have been particularly interested in how cysteine proteases and cysteine protease inhibitors (cystatins) regulate natural as ... Deleterious effects of plant cystatins against the Banana weevil Cosmopolites sordidus. Archives of Insect Biochemistry and ...
  • Secondary structure prediction of salivary cystatins S, SA, and SN carried out by several methods label the 39-58 sequence (β2-strand) as predominantly α-helical. (unicatt.it)
  • One is the presence of a N-terminal alpha-helix, present only in plant cystatins. (wikipedia.org)
  • Tremblay J, Goulet M-C, Vorster J , Goulet C, Michaud M. (2021) Harnessing the functional diversity of plant cystatins to design inhibitor variants highly active against herbivorous arthropod digestive proteases . (up.ac.za)
  • found some 19 different cystatins similar to oryzacystatin-I in the soybean along with related cysteine proteases. (wikipedia.org)
  • We have been particularly interested in how cysteine proteases and cysteine protease inhibitors (cystatins) regulate natural as well as stress-induced senescence. (up.ac.za)
  • Reverse transcription was carried out in a 20 l reaction volume with 1 g RNA, 0.five g Oligo(dT)18 primer (100 M) and 1 l of RevertAidTM M-MuVL Reverse Transcriptase (200 U/l).Full-length protein sequences for every single in the cystatins and cysteine proteases had been aligned and phylogenetic trees generated with the CLC Most important Workbench v6.7.1. (icbinhibitor.com)
  • Due to the presence of histatins (proline-rich proteins including cystatins and statherin), calcium and phosphate are maintained in supersaturation and are available for remineralization of tooth structure. (dentistrytoday.com)
  • The results showed that low-molecular-weight mucin, alpha-amylase, secretory IgA, acidic proline-rich proteins, and cystatins adhered to all kinds of brackets, though the amino acid composition of pellicles differed between bracket types. (snu.ac.kr)
  • Cystatins mainly inhibit peptidase enzymes (another term for proteases) belonging to peptidase families C1 (papain family) and C13 (legumain family). (wikipedia.org)
  • Type 1 cystatins are also known as Stefins (after the Stefan Institute where they were first discovered ) The Type 2 cystatins, which are mainly extracellular secreted polypeptides are largely acidic, contain four conserved cysteine residues known to form two disulfide bonds, may be glycosylated and/or phosphorylated. (wikipedia.org)
  • There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. (utsouthwestern.edu)
  • Cystatins show similarity to fetuins, kininogens, histidine-rich glycoproteins and cystatin-related proteins. (wikipedia.org)
  • These are cystatin-like proteins found in a range of organisms: plant phytocystatins, fetuin in mammals, insect cystatins, and a puff adder venom cystatin, which inhibits metalloproteases of the MEROPS peptidase family M12 (astacin/adamalysin). (wikipedia.org)
  • These enzymes can be inactivated by specific proteins found in plants called cystatins. (usda.gov)
  • Because cystatins interact specifically with insect and nematode edigestive enzymes, they are attractive for controlling pests. (usda.gov)
  • Safety assessment of cystatins used to control pests in transgenic bananas in Uganda. (mak.ac.ug)
  • May involve the interaction of phosphate groups with calcium ions in saliva to form "bridges" Protective functions of early enamel pellicle: protection , lubrication by decreasing frictional forces, may selectively concentrate antimicrobial substances such as immunoglobulins, lysozyme, and cystatins at different oral surfaces. (medicpresents.com)
  • Production of cystatins in roots reduced the populations of the root-lesion nematode 71-79% compared to plants without the cystatins. (usda.gov)
  • We have therefore investigated cuticle disruption by CPs of a well-annotated free-living nematode, and a murine GI nematode, culture The genome contains two cystatins, the functions of which include the inhibition of papain-like CPs [29]. (physiciansontherise.org)
  • The helical propensity of a peptide corresponding to β2-strand of salivary SA cystatin analyzed by CD display high helical propensity in aqueous solution, whereas peptides matching the β2-strand amino acid sequence of cystatins S and SN, display random coil conformation in aqueous solution but acquire α-helical conformation in the presence of trifluoroethanol (TFE). (unicatt.it)
  • The cystatins are a family of cysteine protease inhibitors which share a sequence homology and a common tertiary structure of an alpha helix lying on top of an anti-parallel beta sheet. (wikipedia.org)
  • The genes fo two cystatins from rice seeds and the gene for a marker enzyme were fused to a promoting DNA sequence so that the cystatins and the marker would be produced only in wounded cells, then the genes were introduced into alfalfa plants. (usda.gov)
  • citation needed] The cystatin family includes: The Type 1 cystatins, which are intracellular and are present in the cytosol of many cell types, but can also appear in body fluids at significant concentrations. (wikipedia.org)
  • 7: Cornwall GA, Hsia N. A new subgroup of the family 2 cystatins Mol Cell Endocrinol. (moleculardepot.com)
  • 10: Hsia N, Cornwall GA. Cres2 and Cres3: new members of the cystatin-related epididymal spermatogenic subgroup of family 2 cystatins Endocrinology. (moleculardepot.com)
  • These results show that cystatins have the potential to confer resistance to multiple diseases of alfalfa. (usda.gov)
  • citation needed] The Type 3 cystatins, which are multidomain proteins. (wikipedia.org)
  • The cystatins are a family of cysteine protease inhibitors which share a sequence homology and a common tertiary structure of an alpha helix lying on top of an anti-parallel beta sheet. (wikipedia.org)
  • found some 19 different cystatins similar to oryzacystatin-I in the soybean along with related cysteine proteases. (wikipedia.org)
  • The main aim of this review is to discuss the structure-activity relationships of cysteine proteases and cystatins, as well as of some synthetic inhibitors of cysteine proteases structurally based on the binding fragments of cystatins. (lu.se)
  • 13. The regulation of cysteine cathepsins and cystatins in human gliomas. (nih.gov)
  • The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN , and other peptidases which have a sulfhydryl group at the active site. (bvsalud.org)
  • Cystatins show similarity to fetuins, kininogens, histidine-rich glycoproteins and cystatin-related proteins. (wikipedia.org)
  • citation needed] The Type 3 cystatins, which are multidomain proteins. (wikipedia.org)
  • These are cystatin-like proteins found in a range of organisms: plant phytocystatins, fetuin in mammals, insect cystatins, and a puff adder venom cystatin, which inhibits metalloproteases of the MEROPS peptidase family M12 (astacin/adamalysin). (wikipedia.org)
  • Cystatins that occur as plasma proteins. (bvsalud.org)
  • The expression of various genes of interest identified in the sequencing shall be studied in the functional genome, such as regulatory protein genes (for example, homeobox), proteases related to the protein metabolism, and cystatins, which are anti-fungal and anti-parasites proteins. (ufscar.br)
  • citation needed] The cystatin family includes: The Type 1 cystatins, which are intracellular and are present in the cytosol of many cell types, but can also appear in body fluids at significant concentrations. (wikipedia.org)