A member of the annexin family that is a substrate for a tyrosine kinase, ONCOGENE PROTEIN PP60(V-SRC). Annexin A2 occurs as a 36-KDa monomer and in a 90-KDa complex containing two subunits of annexin A2 and two subunits of S100 FAMILY PROTEIN P11. The monomeric form of annexin A2 was formerly referred to as calpactin I heavy chain.
Protein of the annexin family exhibiting lipid interaction and steroid-inducibility.
A protein of the annexin family isolated from human PLACENTA and other tissues. It inhibits cytosolic PHOSPHOLIPASE A2, and displays anticoagulant activity.
Protein of the annexin family with a probable role in exocytotic and endocytotic membrane events.
Protein of the annexin family originally isolated from the electric organ of the electric ray Torpedo marmorata. It has been found in a wide range of mammalian tissue where it is localized to the apical membrane of polarized EPITHELIAL CELLS.
An annexin family member that plays a role in MEMBRANE FUSION and signaling via VOLTAGE-DEPENDENT CALCIUM CHANNELS.
A protein of the annexin family that catalyzes the conversion of 1-D-inositol 1,2-cyclic phosphate and water to 1-D-myo-inositol 1-phosphate.
Family of calcium- and phospholipid-binding proteins which are structurally related and exhibit immunological cross-reactivity. Each member contains four homologous 70-kDa repeats. The annexins are differentially distributed in vertebrate tissues (and lower eukaryotes) and appear to be involved in MEMBRANE FUSION and SIGNAL TRANSDUCTION.
A family of highly acidic calcium-binding proteins found in large concentration in the brain and believed to be glial in origin. They are also found in other organs in the body. They have in common the EF-hand motif (EF HAND MOTIFS) found on a number of calcium binding proteins. The name of this family derives from the property of being soluble in a 100% saturated ammonium sulfate solution.
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to a serine moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and serine and 2 moles of fatty acids.
One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.
Quaternary ammonium analog of ethidium; an intercalating dye with a specific affinity to certain forms of DNA and, used as diiodide, to separate them in density gradients; also forms fluorescent complexes with cholinesterase which it inhibits.
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.
Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system.
Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
A cell line derived from cultured tumor cells.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
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.
Technique using an instrument system for making, processing, and displaying one or more measurements on individual cells obtained from a cell suspension. Cells are usually stained with one or more fluorescent dyes specific to cell components of interest, e.g., DNA, and fluorescence of each cell is measured as it rapidly transverses the excitation beam (laser or mercury arc lamp). Fluorescence provides a quantitative measure of various biochemical and biophysical properties of the cell, as well as a basis for cell sorting. Other measurable optical parameters include light absorption and light scattering, the latter being applicable to the measurement of cell size, shape, density, granularity, and stain uptake.
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.
Extracellular vesicles generated by the shedding of CELL MEMBRANE blebs.
A family of G-protein-coupled receptors that was originally identified by its ability to bind N-formyl peptides such as N-FORMYLMETHIONINE LEUCYL-PHENYLALANINE. Since N-formyl peptides are found in MITOCHONDRIA and BACTERIA, this class of receptors is believed to play a role in mediating cellular responses to cellular damage and bacterial invasion. However, non-formylated peptide ligands have also been found for this receptor class.
Proteins prepared by recombinant DNA technology.
A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 9. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
Organic compounds that contain technetium as an integral part of the molecule. These compounds are often used as radionuclide imaging agents.
The span of viability of a cell characterized by the capacity to perform certain functions such as metabolism, growth, reproduction, some form of responsiveness, and adaptability.
Established cell cultures that have the potential to propagate indefinitely.
A family of intracellular CYSTEINE ENDOPEPTIDASES that play a role in regulating INFLAMMATION and APOPTOSIS. They specifically cleave peptides at a CYSTEINE amino acid that follows an ASPARTIC ACID residue. Caspases are activated by proteolytic cleavage of a precursor form to yield large and small subunits that form the enzyme. Since the cleavage site within precursors matches the specificity of caspases, sequential activation of precursors by activated caspases can occur.
Fluorescent probe capable of being conjugated to tissue and proteins. It is used as a label in fluorescent antibody staining procedures as well as protein- and amino acid-binding techniques.
An in situ method for detecting areas of DNA which are nicked during APOPTOSIS. Terminal deoxynucleotidyl transferase is used to add labeled dUTP, in a template-independent manner, to the 3 prime OH ends of either single- or double-stranded DNA. The terminal deoxynucleotidyl transferase nick end labeling, or TUNEL, assay labels apoptosis on a single-cell level, making it more sensitive than agarose gel electrophoresis for analysis of DNA FRAGMENTATION.
A product of the lysis of plasminogen (profibrinolysin) by PLASMINOGEN activators. It is composed of two polypeptide chains, light (B) and heavy (A), with a molecular weight of 75,000. It is the major proteolytic enzyme involved in blood clot retraction or the lysis of fibrin and quickly inactivated by antiplasmins.
The parts of a macromolecule that directly participate in its specific combination with another molecule.

Characterization of the Ca2+-dependent binding of annexin IV to surfactant protein A. (1/59)

We have shown previously that surfactant protein A (SP-A) binds to annexin IV in a Ca2+-dependent manner [Sohma, Matsushima, Watanabe, Hattori, Kuroki and Akino (1995) Biochem. J. 312, 175-181]. Annexin IV is a member of the annexin family having four consensus repeats of about 70 amino acids and a unique N-terminal tail. In the present study, the functional site of both annexin IV and SP-A for the Ca2+-dependent binding was investigated using mutant proteins. SP-A bound in a Ca2+-dependent manner to an annexin-IV truncation mutant consisting of the N-terminal domain and the first three domains (T(N-1-2-3)). SP-A also bound to T3-4, but this interaction was not Ca2+-dependent. SP-A bound weakly to the other truncation mutants (T(N-1-2), T(2-3) and T(2-3-4)). Each consensus repeat of annexin IV possesses a conserved acidic amino acid residue (Glu70, Asp142, Glu226 and Asp301) that putatively ligates Ca2+. Using annexin-IV DE mutants in which one, two or three residues out of the four Asp/Glu were altered to Ala by site-directed mutagenesis [Nelson and Creutz (1995) Biochemistry 34, 3121-3132], it was revealed that Ca2+ binding in the third domain is more important than in the other Ca2+-binding sites. SP-A is a member of the animal lectin group homologous with mannose-binding protein A. The substitution of Arg197 of rat SP-A with Asp or Asn eliminated binding to annexin IV, whereas the substitution of Glu195 with Gln was silent. These results suggest that the Ca2+ binding to domain 3 of annexin IV is required for the Ca2+-dependent binding by SP-A and that Arg197 of SP-A is important in this binding.  (+info)

Detection of annexins I and IV in bronchoalveolar lavage fluids from calves inoculated with bovine herpes virus-1. (2/59)

Annexins are phospholipid-binding proteins and are abundant in the lung. Annexins I and IV, but not II and VI, have been detected in bronchoalveolar lavage (BAL) fluids from calves inoculated with Pasteurella haemolytica, the pathogen for calf pneumonia. In this study, BAL fluids from calves with experimental pneumonia induced by inoculation to right lung lobes of bovine herpes virus-1 (BHV-1), the major viral pathogen for pneumonia, were examined for detection of annexins I and IV. Of 6 calves inoculated with BHV-1, annexins I and IV were coincidentally detected in BAL fluids from right lung lobes of 4 calves, but not in BAL fluids from left lung lobes of 6 inoculated calves or those from left and right lung lobes of 3 control calves. Annexin II and VI were not found in any BAL fluids examined. These results, together with previous findings on calves inoculated with Pasteurella haemolytica, suggest that the release of annexins I and IV onto the alveolar surface is an essential event occurring in response to pulmonary infections of BHIV-1 and Pasteurella haemolytica.  (+info)

Immunolocalization of annexins IV, V and VI in the failing and non-failing human heart. (3/59)

The failing human heart is characterized by changes in the expression and function of proteins involved in intracellular Ca2+ cycling, resulting in altered Ca2+ transients and impaired contractile properties of cardiac muscle. The role of the cardiac annexins in this process remains unclear. Annexins may play a role in the regulation of Ca2+ pumps and exchangers on the sarcolemma, and have been shown to be altered in some cardiac disease states. OBJECTIVE: The goal of this study was to compare the immunolocalization and expression of annexins IV, V and VI in failing and non-failing human hearts. METHODS: We used immunostaining to identify the subcellular location of annexins IV, V and VI proteins within the myocardial cell, and Western blot analysis to quantify the proteins in the same hearts. RESULTS: Annexin IV showed a cytoplasmic distribution in both failing and non-failing human heart cells. Annexin V was localized at the z-line, around lipofuscin granules, and in the cytosol in the non-failing heart cells. Annexin VI was localized at the sarcolemma and intercalated disc. Protein levels of annexins IV and V were up-regulated in failing human hearts, while the expression of annexin VI was unchanged. CONCLUSIONS: Alterations in the intracellular localization of annexins, along with up-regulation of annexins IV and V in the failing human heart cells, suggests differential regulation of these Ca2+ regulatory proteins during heart failure.  (+info)

Modulation of paclitaxel resistance by annexin IV in human cancer cell lines. (4/59)

A recurring problem with cancer therapies is the development of drug resistance. While investigating the protein profile of cells resistant to a novel antimitotic compound (A204197), we discovered an increase in annexin IV expression. When we examined the annexin IV protein expression level in a paclitaxel-resistant cell line (H460/T800), we found that annexin IV was also overexpressed. Interestingly a closely related protein, annexin II, was not overexpressed in H460/T800 cells. Immunostaining with either annexin II or IV antibody revealed that annexin IV was primarily located in the nucleus of paclitaxel-resistant H460/T800 cells. Short-term treatment of H460 cells with 10 nM paclitaxel for up to 4 days resulted in induction of annexin IV, but not annexin II expression. In addition, there was an increase in annexin IV staining in the nucleus starting at day 1. Furthermore, cells pretreated with 10 nM paclitaxel for 4 days resulted in cells becoming approximately fivefold more resistant to paclitaxel. Transfection of annexin IV cDNA into 293T cells revealed that there was a threefold increase in paclitaxel resistance. Thus our results indicate that annexin IV plays a role in paclitaxel resistance in this cell line and it is among one of the earliest proteins that is induced in cells in response to cytotoxic stress such as antimitotic drug treatment.  (+info)

Differential lipid specificities of the repeated domains of annexin IV. (5/59)

The roles of the four domains of annexin IV in binding to phospholipids and glycolipids were assessed by analyzing the binding of a group of mutant annexins IV in which one or more of the four domains was inactivated by replacing a critical amino residue(s) (Asp or Glu) with the neutral residue Ala. The data reveal that individual annexin domains may have characteristic affinities for different lipids. In particular, inactivation of the fourth domain inhibits the binding to phosphatidylserine (PS) and phosphatidylinositol (PI) but not to phosphatidylglycerol (PG), suggesting that this domain specifically can accommodate the larger head groups of PS and PI whereas the other three domains may form more restricted binding pockets. In order to block binding to PG, domain 1, or both domains 2 and 3 must be inactivated in addition to domain 4, suggesting that all four domains may be able to accommodate the headgroup of PG to some extent. Binding to acidic glycolipids (sulfatides) was also sensitive to inactivation of domain 4. However, in the case of sulfatides the nature of the binding reaction is fundamentally different compared with the binding to phospholipids since the interaction with sulfatides was highly sensitive to an increase in ionic strength. The binding to sulfatides may depend therefore on charge-charge interactions whereas the binding to phospholipid may involve a more specific interaction between the lipid headgroup and the protein surface, and/or interaction of the protein with the hydrophobic portion of a lipid bilayer.  (+info)

UDP hydrolase activity associated with the porcine liver annexin fraction. (6/59)

In the crude fraction of porcine liver annexins, we identified annexin IV (AnxIV), AnxII and AnxVI of MW (molecular weight) of 32, 36 and 68 kDa, respectively, an albumin of MW of 61.5 kDa and an UDP hydrolase (UDPase) of MW of 62 kDa, related to the human UDPase from Golgi membranes. The latter enzyme exhibits its highest specificity towards UDP and GDP but not ADP and CDP, and it is stimulated by Mg(2+) and Ca(2+). AnxVI itself, although it binds purine nucleotides, does not exhibit hydrolytic activity towards nucleotides. Taken together, these results suggest that AnxVI may interact in vivo with a nucleotide-utilizing enzyme, UDPase. This is in line with observations made by other investigators that various annexins are able to interact with nucleotide-utilizing proteins, such as protein kinases, GTPases, cytoskeletal proteins and p120(GAP). Such interactions could be of particular importance in modulating the biological activities of these proteins in vivo.  (+info)

Annexin IV (Xanx-4) has a functional role in the formation of pronephric tubules. (7/59)

Vertebrate kidney organogenesis is characterised by the successive formation of the pronephros, the mesonephros and the metanephros. The pronephros is the first to form and is the functional embryonic kidney of lower vertebrates; although it is vestigial in higher vertebrates, it is a necessary precursor for the other kidney types. The Xenopus pronephros is a simple paired organ; each nephron consists of a single large glomus, one set of tubules and a single duct. The simple organisation of the pronephros and the amenability of Xenopus laevis embryos to manipulation make the Xenopus pronephros an attractive system in which to study organogenesis. It has been shown that pronephric tubules can be induced to form in presumptive ectodermal tissue by treatment with RA and activin. We have used this system in a subtractive hybridisation screen that resulted in the cloning of Xenopus laevis annexin IV (Xanx-4). Xanx-4 transcripts are specifically located to the developing pronephric tubules, and the protein to the luminal surface of these tubules. Temporal expression shows zygotic transcription is upregulated at the time of pronephric tubule specification and persists throughout pronephric development. The temporal and spatial expression pattern of Xanx-4 suggests it may have a role in pronephric tubule development. Overexpression of Xanx-4 yields no apparent phenotype, but Xanx-4 depletion, using morpholinos, produces a shortened, enlarged tubule phenotype. The phenotype observed can be rescued by co-injection of Xanx-4 mRNA. Although the function of annexins is not yet clear, studies have suggested a role for annexins in a number of cellular processes. Annexin IV has been shown to have an inhibitory role in the regulation of epithelial calcium-activated chloride ion conductance. The enlarged pronephric tubule phenotype observed may be attributed to incorrect modulation of exocytosis, membrane plasticity or ion channels and/or water homeostasis. In this study, we demonstrate an in vivo role for annexin IV in the development of the pronephric tubules in Xenopus laevis.  (+info)

Cloning and characterization of ZAP36, an annexin-like, zymogen granule membrane associated protein, in exocrine pancreas. (8/59)

ZAP36, a zymogen granule membrane associated protein with 36 kDa, was cloned from both canine and rat pancreas. ZAP36 is found to be a novel member of annexin IV, and showed an apical localization in exocrine pancreas and an ubiquitous expression in epithelial tissues. ZAP36 may be involved in exocytosis in apical regions of polarized cells.  (+info)

Annexin A2 is a protein found in various types of cells, including those that line the inside of blood vessels. It is a member of the annexin family of proteins, which are characterized by their ability to bind to calcium ions and membranes. Annexin A2 is involved in several cellular processes, including the regulation of ion channels, the modulation of enzyme activity, and the promotion of cell adhesion and migration. It also plays a role in the coagulation of blood, and has been implicated in the development and progression of various diseases, including cancer and cardiovascular disease.

Annexin A1 is a protein that belongs to the annexin family, which are calcium-dependent phospholipid-binding proteins. This protein is found in various tissues, including the human body, and has multiple functions, such as anti-inflammatory, anti-proliferative, and pro-resolving activities. It plays a crucial role in regulating cellular processes like apoptosis (programmed cell death), membrane organization, and signal transduction.

Annexin A1 is also known to interact with other proteins and receptors, such as the formyl peptide receptor 2 (FPR2), which contributes to its immunomodulatory functions. In addition, it has been implicated in several pathophysiological conditions, including cancer, inflammation, and autoimmune diseases.

Modulating Annexin A1 levels or activity may provide therapeutic benefits for various medical conditions; however, further research is required to fully understand its potential as a drug target.

Annexin A5 is a protein that belongs to the annexin family, which are calcium-dependent phospholipid-binding proteins. Annexin A5 has high affinity for phosphatidylserine, a type of phospholipid that is usually located on the inner leaflet of the plasma membrane in healthy cells. However, when cells undergo apoptosis (programmed cell death), phosphatidylserine is exposed on the outer leaflet of the plasma membrane.

Annexin A5 can bind to exposed phosphatidylserine on the surface of apoptotic cells and is commonly used as a marker for detecting apoptosis in various experimental settings, including flow cytometry, immunohistochemistry, and imaging techniques. Annexin A5-based assays are widely used in research and clinical settings to study the mechanisms of apoptosis and to develop diagnostic tools for various diseases, such as cancer, neurodegenerative disorders, and cardiovascular diseases.

Annexin A6 is a protein that belongs to the annexin family, which are calcium-dependent phospholipid-binding proteins. Annexin A6 is involved in various cellular processes such as exocytosis, endocytosis, and membrane trafficking. It has been shown to play a role in regulating ion channels, modulating the actin cytoskeleton, and interacting with other proteins to form multimolecular complexes. Annexin A6 is expressed in various tissues, including the heart, lung, kidney, and pancreas. Mutations in the ANXA6 gene have been associated with certain diseases, such as kidney stones and cataracts.

Annexin A4 is a type of protein that belongs to the annexin family, which are characterized by their ability to bind to calcium ions and membranes. Specifically, Annexin A4 is known to play roles in various cellular processes such as exocytosis, endocytosis, and regulation of ion channels. It has also been implicated in the development and progression of certain diseases, including cancer and neurological disorders.

In the medical field, the study of Annexin A4 is important for understanding its functions and potential therapeutic applications. For example, research has suggested that targeting Annexin A4 may be a useful strategy for developing new treatments for cancer or other diseases. However, more studies are needed to fully elucidate the role of this protein in various biological processes and disease states.

Annexin A7 is a type of protein that belongs to the annexin family, which are characterized by their ability to bind to cell membranes in a calcium-dependent manner. Specifically, Annexin A7 (also known as Syntaxin-binding protein 1 or SBP1) is involved in various cellular processes such as exocytosis, endocytosis, and signal transduction. It has been shown to interact with other proteins, including syntaxins, which are important for vesicle trafficking and fusion. Additionally, Annexin A7 may have a role in regulating apoptosis (programmed cell death) and has been implicated in several diseases, including cancer and neurodegenerative disorders. However, more research is needed to fully understand the functions and regulatory mechanisms of this protein.

Annexin A3 is a type of protein that belongs to the annexin family, which are characterized by their ability to bind to calcium ions and membranes. Specifically, annexin A3 is involved in various cellular processes such as exocytosis, endocytosis, and signal transduction. It has been found to play a role in the regulation of blood clotting, inflammation, and cancer metastasis. Annexin A3 can be found on the surface of various cells, including platelets, neutrophils, and tumor cells. In addition, annexin A3 has been identified as a potential biomarker for certain types of cancer, such as ovarian and prostate cancer.

Annexins are a family of calcium-dependent phospholipid-binding proteins that are found in various organisms, including humans. They are involved in several cellular processes, such as membrane organization, signal transduction, and regulation of ion channels. Some annexins also have roles in inflammation, blood coagulation, and apoptosis (programmed cell death).

Annexins have a conserved structure, consisting of a core domain that binds to calcium ions and a variable number of domains that bind to phospholipids. This allows annexins to interact with membranes in a calcium-dependent manner, which is important for their functions.

There are several different annexin proteins, each with its own specific functions and expression patterns. For example, annexin A1 is involved in the regulation of inflammation and has been studied as a potential target for anti-inflammatory therapies. Annexin A2 is involved in the regulation of coagulation and has been studied as a potential target for anticoagulant therapies. Other annexins have roles in cell division, differentiation, and survival.

Overall, annexins are important regulators of various cellular processes and have potential as targets for therapeutic intervention in a variety of diseases.

S100 proteins are a family of calcium-binding proteins that are involved in the regulation of various cellular processes, including cell growth and differentiation, intracellular signaling, and inflammation. They are found in high concentrations in certain types of cells, such as nerve cells (neurons), glial cells (supporting cells in the nervous system), and skin cells (keratinocytes).

The S100 protein family consists of more than 20 members, which are divided into several subfamilies based on their structural similarities. Some of the well-known members of this family include S100A1, S100B, S100 calcium-binding protein A8 (S100A8), and S100 calcium-binding protein A9 (S100A9).

Abnormal expression or regulation of S100 proteins has been implicated in various pathological conditions, such as neurodegenerative diseases, cancer, and inflammatory disorders. For example, increased levels of S100B have been found in the brains of patients with Alzheimer's disease, while overexpression of S100A8 and S100A9 has been associated with the development and progression of certain types of cancer.

Therefore, understanding the functions and regulation of S100 proteins is important for developing new diagnostic and therapeutic strategies for various diseases.

Phosphatidylserines are a type of phospholipids that are essential components of the cell membrane, particularly in the brain. They play a crucial role in maintaining the fluidity and permeability of the cell membrane, and are involved in various cellular processes such as signal transduction, protein anchorage, and apoptosis (programmed cell death). Phosphatidylserines contain a polar head group made up of serine amino acids and two non-polar fatty acid tails. They are abundant in the inner layer of the cell membrane but can be externalized to the outer layer during apoptosis, where they serve as signals for recognition and removal of dying cells by the immune system. Phosphatidylserines have been studied for their potential benefits in various medical conditions, including cognitive decline, Alzheimer's disease, and depression.

Apoptosis is a programmed and controlled cell death process that occurs in multicellular organisms. It is a natural process that helps maintain tissue homeostasis by eliminating damaged, infected, or unwanted cells. During apoptosis, the cell undergoes a series of morphological changes, including cell shrinkage, chromatin condensation, and fragmentation into membrane-bound vesicles called apoptotic bodies. These bodies are then recognized and engulfed by neighboring cells or phagocytic cells, preventing an inflammatory response. Apoptosis is regulated by a complex network of intracellular signaling pathways that involve proteins such as caspases, Bcl-2 family members, and inhibitors of apoptosis (IAPs).

Propidium is not a medical condition or diagnosis, but rather it is a fluorescent dye that is used in medical and scientific research. It is often used in procedures such as flow cytometry and microscopy to stain and label cells or nucleic acids (DNA or RNA). Propidium iodide is the most commonly used form of propidium, which binds to DNA by intercalating between the bases.

Once stained with propidium iodide, cells with damaged membranes will take up the dye and can be detected and analyzed based on their fluorescence intensity. This makes it possible to identify and quantify dead or damaged cells in a population, as well as to analyze DNA content and cell cycle status.

Overall, propidium is an important tool in medical research and diagnostics, providing valuable information about cell health, viability, and genetic material.

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.

Phospholipids are a major class of lipids that consist of a hydrophilic (water-attracting) head and two hydrophobic (water-repelling) tails. The head is composed of a phosphate group, which is often bound to an organic molecule such as choline, ethanolamine, serine or inositol. The tails are made up of two fatty acid chains.

Phospholipids are a key component of cell membranes and play a crucial role in maintaining the structural integrity and function of the cell. They form a lipid bilayer, with the hydrophilic heads facing outwards and the hydrophobic tails facing inwards, creating a barrier that separates the interior of the cell from the outside environment.

Phospholipids are also involved in various cellular processes such as signal transduction, intracellular trafficking, and protein function regulation. Additionally, they serve as emulsifiers in the digestive system, helping to break down fats in the diet.

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.

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

A cell line that is derived from tumor cells and has been adapted to grow in culture. These cell lines are often used in research to study the characteristics of cancer cells, including their growth patterns, genetic changes, and responses to various treatments. They can be established from many different types of tumors, such as carcinomas, sarcomas, and leukemias. Once established, these cell lines can be grown and maintained indefinitely in the laboratory, allowing researchers to conduct experiments and studies that would not be feasible using primary tumor cells. It is important to note that tumor cell lines may not always accurately represent the behavior of the original tumor, as they can undergo genetic changes during their time in culture.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

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.

Flow cytometry is a medical and research technique used to measure physical and chemical characteristics of cells or particles, one cell at a time, as they flow in a fluid stream through a beam of light. The properties measured include:

* Cell size (light scatter)
* Cell internal complexity (granularity, also light scatter)
* Presence or absence of specific proteins or other molecules on the cell surface or inside the cell (using fluorescent antibodies or other fluorescent probes)

The technique is widely used in cell counting, cell sorting, protein engineering, biomarker discovery and monitoring disease progression, particularly in hematology, immunology, and cancer research.

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.

Cell-derived microparticles (CDMs), also known as microvesicles or microparticles, are small membrane-bound particles that are released from the cell surface upon activation or apoptosis of various cell types, including platelets, leukocytes, endothelial cells, and red blood cells. CDMs range in size from 0.1 to 1.0 micrometers in diameter and contain a variety of bioactive molecules, such as lipids, proteins, and nucleic acids, which can be transferred to neighboring or distant cells, thereby modulating their function.

CDMs have been implicated in various physiological and pathological processes, including coagulation, inflammation, immune response, angiogenesis, and cancer progression. They have also emerged as potential biomarkers for various diseases, such as cardiovascular disease, sepsis, and cancer, due to their distinct molecular signature and abundance in body fluids, such as blood, urine, and cerebrospinal fluid.

The mechanisms of CDM formation and release are complex and involve several cellular processes, including cytoskeletal rearrangement, membrane budding, and vesicle shedding. The molecular composition of CDMs reflects their cellular origin and activation state, and can be analyzed by various techniques, such as flow cytometry, proteomics, and transcriptomics, to gain insights into their biological functions and clinical relevance.

Formyl peptide receptors (FPRs) are a type of G protein-coupled receptors that play a crucial role in the innate immune system. They are expressed on various cells including neutrophils, monocytes, and macrophages. FPRs recognize and respond to formylated peptides derived from bacteria, mitochondria, and host proteins during cell damage or stress. Activation of FPRs triggers a variety of cellular responses, such as chemotaxis, phagocytosis, and release of inflammatory mediators, which help to eliminate invading pathogens and promote tissue repair. There are three subtypes of human FPRs (FPR1, FPR2, and FPR3) that have distinct ligand specificities and functions in the immune response.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Caspase-3 is a type of protease enzyme that plays a central role in the execution-phase of cell apoptosis, or programmed cell death. It's also known as CPP32 (CPP for ced-3 protease precursor) or apopain. Caspase-3 is produced as an inactive protein that is activated when cleaved by other caspases during the early stages of apoptosis. Once activated, it cleaves a variety of cellular proteins, including structural proteins, enzymes, and signal transduction proteins, leading to the characteristic morphological and biochemical changes associated with apoptotic cell death. Caspase-3 is often referred to as the "death protease" because of its crucial role in executing the cell death program.

Western blotting is a laboratory technique used in molecular biology to detect and quantify specific proteins in a mixture of many different proteins. This technique is commonly used to confirm the expression of a protein of interest, determine its size, and investigate its post-translational modifications. The name "Western" blotting distinguishes this technique from Southern blotting (for DNA) and Northern blotting (for RNA).

The Western blotting procedure involves several steps:

1. Protein extraction: The sample containing the proteins of interest is first extracted, often by breaking open cells or tissues and using a buffer to extract the proteins.
2. Separation of proteins by electrophoresis: The extracted proteins are then separated based on their size by loading them onto a polyacrylamide gel and running an electric current through the gel (a process called sodium dodecyl sulfate-polyacrylamide gel electrophoresis or SDS-PAGE). This separates the proteins according to their molecular weight, with smaller proteins migrating faster than larger ones.
3. Transfer of proteins to a membrane: After separation, the proteins are transferred from the gel onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric current in a process called blotting. This creates a replica of the protein pattern on the gel but now immobilized on the membrane for further analysis.
4. Blocking: The membrane is then blocked with a blocking agent, such as non-fat dry milk or bovine serum albumin (BSA), to prevent non-specific binding of antibodies in subsequent steps.
5. Primary antibody incubation: A primary antibody that specifically recognizes the protein of interest is added and allowed to bind to its target protein on the membrane. This step may be performed at room temperature or 4°C overnight, depending on the antibody's properties.
6. Washing: The membrane is washed with a buffer to remove unbound primary antibodies.
7. Secondary antibody incubation: A secondary antibody that recognizes the primary antibody (often coupled to an enzyme or fluorophore) is added and allowed to bind to the primary antibody. This step may involve using a horseradish peroxidase (HRP)-conjugated or alkaline phosphatase (AP)-conjugated secondary antibody, depending on the detection method used later.
8. Washing: The membrane is washed again to remove unbound secondary antibodies.
9. Detection: A detection reagent is added to visualize the protein of interest by detecting the signal generated from the enzyme-conjugated or fluorophore-conjugated secondary antibody. This can be done using chemiluminescent, colorimetric, or fluorescent methods.
10. Analysis: The resulting image is analyzed to determine the presence and quantity of the protein of interest in the sample.

Western blotting is a powerful technique for identifying and quantifying specific proteins within complex mixtures. It can be used to study protein expression, post-translational modifications, protein-protein interactions, and more. However, it requires careful optimization and validation to ensure accurate and reproducible results.

Organotechnetium compounds are chemical substances that contain carbon-technetium bonds, where technetium is an element with the symbol Tc and atomic number 43. These types of compounds are primarily used in medical imaging as radioactive tracers due to the ability of technetium-99m to emit gamma rays. The organotechnetium compounds help in localizing specific organs, tissues, or functions within the body, making them useful for diagnostic purposes in nuclear medicine.

It is important to note that most organotechnetium compounds are synthesized from technetium-99m, which is generated from the decay of molybdenum-99. The use of these compounds requires proper handling and administration by trained medical professionals due to their radioactive nature.

Cell survival refers to the ability of a cell to continue living and functioning normally, despite being exposed to potentially harmful conditions or treatments. This can include exposure to toxins, radiation, chemotherapeutic drugs, or other stressors that can damage cells or interfere with their normal processes.

In scientific research, measures of cell survival are often used to evaluate the effectiveness of various therapies or treatments. For example, researchers may expose cells to a particular drug or treatment and then measure the percentage of cells that survive to assess its potential therapeutic value. Similarly, in toxicology studies, measures of cell survival can help to determine the safety of various chemicals or substances.

It's important to note that cell survival is not the same as cell proliferation, which refers to the ability of cells to divide and multiply. While some treatments may promote cell survival, they may also inhibit cell proliferation, making them useful for treating diseases such as cancer. Conversely, other treatments may be designed to specifically target and kill cancer cells, even if it means sacrificing some healthy cells in the process.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Caspases are a family of protease enzymes that play essential roles in programmed cell death, also known as apoptosis. These enzymes are produced as inactive precursors and are activated when cells receive signals to undergo apoptosis. Once activated, caspases cleave specific protein substrates, leading to the characteristic morphological changes and DNA fragmentation associated with apoptotic cell death. Caspases also play roles in other cellular processes, including inflammation and differentiation. There are two types of caspases: initiator caspases (caspase-2, -8, -9, and -10) and effector caspases (caspase-3, -6, and -7). Initiator caspases are activated in response to various apoptotic signals and then activate the effector caspases, which carry out the proteolytic cleavage of cellular proteins. Dysregulation of caspase activity has been implicated in a variety of diseases, including neurodegenerative disorders, ischemic injury, and cancer.

Fluorescein-5-isothiocyanate (FITC) is not a medical term per se, but a chemical compound commonly used in biomedical research and clinical diagnostics. Therefore, I will provide a general definition of this term:

Fluorescein-5-isothiocyanate (FITC) is a fluorescent dye with an absorption maximum at approximately 492-495 nm and an emission maximum at around 518-525 nm. It is widely used as a labeling reagent for various biological molecules, such as antibodies, proteins, and nucleic acids, to study their structure, function, and interactions in techniques like flow cytometry, immunofluorescence microscopy, and western blotting. The isothiocyanate group (-N=C=S) in the FITC molecule reacts with primary amines (-NH2) present in biological molecules to form a stable thiourea bond, enabling specific labeling of target molecules for detection and analysis.

In situ nick-end labeling (ISEL, also known as TUNEL) is a technique used in pathology and molecular biology to detect DNA fragmentation, which is a characteristic of apoptotic cells (cells undergoing programmed cell death). The method involves labeling the 3'-hydroxyl termini of double or single stranded DNA breaks in situ (within tissue sections or individual cells) using modified nucleotides that are coupled to a detectable marker, such as a fluorophore or an enzyme. This technique allows for the direct visualization and quantification of apoptotic cells within complex tissues or cell populations.

Fibrinolysin is defined as a proteolytic enzyme that dissolves or breaks down fibrin, a protein involved in the clotting of blood. This enzyme is produced by certain cells, such as endothelial cells that line the interior surface of blood vessels, and is an important component of the body's natural mechanism for preventing excessive blood clotting and maintaining blood flow.

Fibrinolysin works by cleaving specific bonds in the fibrin molecule, converting it into soluble degradation products that can be safely removed from the body. This process is known as fibrinolysis, and it helps to maintain the balance between clotting and bleeding in the body.

In medical contexts, fibrinolysin may be used as a therapeutic agent to dissolve blood clots that have formed in the blood vessels, such as those that can occur in deep vein thrombosis or pulmonary embolism. It is often administered in combination with other medications that help to enhance its activity and specificity for fibrin.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

... is a protein that in humans is encoded by the ANXA3 gene. It is abnormally expressed in fetuses of both IVF and ICSI ... "Entrez Gene: ANXA3 annexin A3". Zhang Y, Zhang YL, Feng C, et al. (September 2008). "Comparative proteomic analysis of human ... 2005). "Annexin A3 is a potential angiogenic mediator". Biochem. Biophys. Res. Commun. 337 (4): 1283-7. doi:10.1016/j.bbrc. ... "The high-resolution crystal structure of human annexin III shows subtle differences with annexin V.". Biochemistry. 35 (6): ...
... is a protein that in humans is encoded by the ANXA4 gene. Annexin IV (ANX4) belongs to the annexin family of calcium ... "Entrez Gene: ANXA4 annexin A4". Human ANXA4 genome location and ANXA4 gene details page in the UCSC Genome Browser. Römisch J, ... Dreier R, Schmid KW, Gerke V, Riehemann K (Aug 1998). "Differential expression of annexins I, II and IV in human tissues: an ... Han EK, Tahir SK, Cherian SP, Collins N, Ng SC (Jul 2000). "Modulation of paclitaxel resistance by annexin IV in human cancer ...
... (or annexin V) is a cellular protein in the annexin group. In flow cytometry, annexin V is commonly used to detect ... Annexin A5 showed upregulation in papillary thyroid carcinoma. Annexin A5 is used as a non-quantitative probe to detect cells ... Annexin A5 forms a shield around negatively charged phospholipid molecules. The formation of an annexin A5 shield blocks the ... The annexin A5 affinity assay typically uses a conjugate of annexin V and a fluorescent or enzymatic label, biotin or other ...
This clustering of annexin A5 on the membrane greatly increases the intensity of annexin A5 when labeled with a fluorescent or ... Labeling of annexin A5 with fluorescent or radioactive molecules makes it possible to detect binding of labeled annexin A5 to ... Internalization amplifies additionally the intensity of the annexin A5 stained cell. Annexin A5 has been used to successively ... annexin A5 assembles into a trimeric cluster. This trimer consists of three annexin A5 molecules that are bound to each other ...
Annexin A5 forms a shield around negatively charged phospholipid molecules, thus reducing their availability for coagulation. ... Thus, anti-annexin A5 antibodies increase phospholipid-dependent coagulation steps. The lupus anticoagulant antibodies are ...
However some annexins (Annexin A1, Annexin A2, and Annexin A5) can be secreted from the cytoplasm to outside cellular ... Annexin, type I InterPro: IPR002388 Annexin, type II InterPro: IPR002389 Annexin, type III InterPro: IPR002390 Annexin, type IV ... In addition to annexin A-II, annexin A-XI has also been shown to organize cell membrane properties. Annexin A-XI is believed to ... The 310 amino acid annexin core has four annexin repeats, each composed of 5 alpha-helices. The exception is annexin A-VI that ...
Annexin A5-stained EVs, etc.); or c) descriptions of conditions or cell of origin (podocyte EVs, hypoxic EVs, large oncosomes, ...
Integrin, beta 5 has been shown to interact with PTK2, Annexin A5 and PAK4. ITGB5 encodes a subunit of integrin that can ... "Alpha v beta 5 integrin-dependent programmed cell death triggered by a peptide mimic of annexin V". Mol. Cell. 11 (5): 1151-62 ...
... has been shown to interact with SHC2, Annexin A5 and SHC1. Cluster of differentiation VEGF ...
... which encodes annexin A5. It is also neighbored by PP12613 located on the positive strand. The gene on chromosome 4 encoding ...
The concept for the therapy is based on the anti-inflammatory properties of Annexin A5, a body own protective protein that acts ... Annexin Pharmaceuticals is a Swedish privately held biotech company developing new therapeutic approaches for inflammatory ... The company is currently focusing on treatment of peripheral artery disease (PAD). Martz, Lauren (May 26, 2014). "Annexin: ...
... a sequence for the insulin gene Adenosine A3 receptor, a human gene Annexin A3, a human gene ATC code A03 Drugs for functional ... Look up A-3, A3, or a3 in Wiktionary, the free dictionary. A3, A03 or A.III may refer to: A3 paper, a paper size defined by ISO ... a band known as A3 in the U.S. to avoid confusion with the country group Alabama A-3, a Yamaha musical instrument product A3 ( ... a club football tournament also known as the East Asian Champions Cup Arrows A3, a 1980 racing car A3, a climbing grade A-3 ...
Annexin A5 affinity assay, a test for cells undergoing apoptosis, often uses flow cytometry Cell cycle analysis Coulter counter ...
... regulatory sequence in biochemistry A5, the abbreviation for the androgen Androstenediol Annexin A5, a human cellular ... A5 is the code for permission to use specific land or premises for takeaways A5/1, A5/2 and A5/3, ciphers used in cellular ... formerly JAC Jiayue A5 A5 road, in several countries Hall-Scott A-5, an engine powering the 1916 Standard H-2 aircraft Prussian ... ARM applications processor A5 (classification), an amputee sport classification A5 grade (climbing) A5, an aid climbing gear ...
Annexin A3 MeSH D12.776.157.125.050.080 - annexin a4 MeSH D12.776.157.125.050.100 - annexin a5 MeSH D12.776.157.125.050.110 - ... annexin a6 MeSH D12.776.157.125.050.120 - annexin a7 MeSH D12.776.157.125.412.249 - calmodulin MeSH D12.776.157.125.412.311 - ... annexin a1 MeSH D12.776.157.125.050.060 - annexin a2 MeSH D12.776.157.125.050.070 - ...
... annexin A3 MeSH D08.811.277.352.640.125 - 3',5'-cyclic-GMP phosphodiesterase MeSH D08.811.277.352.640.150 - 3',5'-cyclic- ... cytochromes a3 MeSH D08.244.187.249 - cytochromes b MeSH D08.244.187.500 - cytochromes b5 MeSH D08.244.187.600 - cytochromes b6 ...
Annexin A2 CAF-1 CDC25C CHTF18 Cyclin D1 Cyclin O Cyclin-dependent kinase 4 Cyclin-dependent kinase inhibitor 1C DNMT1 EP300 ... Chromatin remodeling factor Clamp loader Cohesin DNA ligase DNA methyltransferase DNA polymerases E2 SUMO-conjugating enzyme E3 ...
Takano T, Fiore S, Maddox JF, Brady HR, Petasis NA, Serhan CN (May 1997). "Aspirin-triggered 15-epi-lipoxin A4 (LXA4) and LXA4 ... Ernst S, Lange C, Wilbers A, Goebeler V, Gerke V, Rescher U (Jun 2004). "An annexin 1 N-terminal peptide activates leukocytes ... "The synthetic peptide Trp-Lys-Tyr-Met-Val-Met-NH2 specifically activates neutrophils through FPRL1/lipoxin A4 receptors and is ... is not affected by lipoxin A4". Scandinavian Journal of Immunology. 56 (5): 470-6. doi:10.1046/j.1365-3083.2002.01149.x. PMID ...
Annexin II, which is attracted to negatively charged phospholipids, binds to p11 at the Ca2+ binding site. In addition, Annexin ... "Induction of endogenous genes following infection of human endothelial cells with an E1(-) E4(+) adenovirus gene transfer ... Kwon M, MacLeod TJ, Zhang Y, Waisman DM (Jan 2005). "S100A10, annexin A2, and annexin a2 heterotetramer as candidate ... Complexed with the annexin II, p11 binds receptor and channel proteins and guides them to the cell surface, resulting in ...
... lipoxin A4 (LXA4). Because of its interaction with lipoxin A4, FPR2 is also commonly named the ALX/FPR2 or just ALX receptor. ... Ac2-26 and Ac9-25 of Annexin A1 (ANXA1 or lipocortin 1), which at high concentrations fully stimulate neutrophil functions but ... lipoxin A4 (LXA4), and thereafter for a related arachidonic acid metabolite, the Epi-lipoxin, aspirin-triggered lipoxin A4 (i.e ... "Lipoxin A4 stable analogs are potent mimetics that stimulate human monocytes and THP-1 cells via a G-protein-linked lipoxin A4 ...
018229 ANXA6 Annexin 6 ANXA7 Annexin 7 AP1B1 Coated vesicles CLTA Clathrin A (vesicles) CLTB Clathrin B (vesicles) CLTC MTX2 ... 021178 E3 ubiquitin-protein ligase. Modulates cyclin B levels and participates in the regulation of cell cycle progression ... 003334 Homo sapiens ubiquitin-activating enzyme E1 (A1S9T and BN75 temperature UBA2 NM_005499 UBA3 NM_003968 UBA5 NM_024818 ...
These products are now termed lipoxin A4 and B4, respectively. While initially found to have in vitro activity suggesting that ... annexin A1 (an inhibitor of formation of pro-inflammatory metabolites of polyunsaturated fatty acids, and the gaseous resolvins ...
He KL, Deora AB, Xiong H, Ling Q, Weksler BB, Niesvizky R, Hajjar KA (July 2008). "Endothelial cell annexin A2 regulates ... "Cancer related mutations in NRF2 impair its recognition by Keap1-Cul3 E3 ligase and promote malignancy". Proceedings of the ... "cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination". Molecular Cell ... "Unanchored K48-linked polyubiquitin synthesized by the E3-ubiquitin ligase TRIM6 stimulates the interferon-IKKε kinase-mediated ...
Takano T, Fiore S, Maddox JF, Brady HR, Petasis NA, Serhan CN (May 1997). "Aspirin-triggered 15-epi-lipoxin A4 (LXA4) and LXA4 ... Annexin A1 (also termed ANXA1 and lipocortin 1) and its N-terminal peptides (Ac2-26 and Ac9-25). At low concentrations, these ... FMLP and lipoxin A4. Isolated mouse Olfactory bulb neurons also respond to a range of other fpr agonists. These results suggest ... and functional characterization of a murine lipoxin A4 receptor homologue gene". Journal of Immunology. 169 (6): 3363-9. doi: ...
In addition, the tumor cells may also express adenosine A1 and A3 receptors associated with Gαi proteins, promoting both the ... Babiychuk EB, Draeger A (June 2006). "Regulation of ecto-5'-nucleotidase activity via Ca2+-dependent, annexin 2-mediated ...
The four major naturally occurring estrogens are estrone (E1), estradiol (E2), estriol (E3), and estetrol (E4). Estradiol (E2) ... Nadkarni S, Cooper D, Brancaleone V, Bena S, Perretti M (November 2011). "Activation of the annexin A1 pathway underlies the ... A4), androstenediol (A5), 3α-androstanediol, and 3β-androstanediol. Some estrogen metabolites, such as the catechol estrogens 2 ... There are three major endogenous estrogens that have estrogenic hormonal activity: estrone (E1), estradiol (E2), and estriol ( ...
Annexin A3 is a protein that in humans is encoded by the ANXA3 gene. It is abnormally expressed in fetuses of both IVF and ICSI ... "Entrez Gene: ANXA3 annexin A3". Zhang Y, Zhang YL, Feng C, et al. (September 2008). "Comparative proteomic analysis of human ... 2005). "Annexin A3 is a potential angiogenic mediator". Biochem. Biophys. Res. Commun. 337 (4): 1283-7. doi:10.1016/j.bbrc. ... "The high-resolution crystal structure of human annexin III shows subtle differences with annexin V.". Biochemistry. 35 (6): ...
"Annexin A4" by people in this website by year, and whether "Annexin A4" was a major or minor topic of these publications. ... "Annexin A4" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... Below are the most recent publications written about "Annexin A4" by people in Profiles. ... Proteomic characterization of ovarian cancers identifying annexin-A4, phosphoserine aminotransferase, cellular retinoic acid- ...
... Mark Posted on 27 March 2014. Posted in Research highlight ... Annexin A4 (AnxA4) has been implicated in diverse cellular processes, including the regulation of exocytosis and ion-transport ... Annexins, found in most eukaryotic species, are cytosolic proteins that are able to bind negatively-charged phospholipids in a ...
In this work, fluorescent protein fusions of annexin A4 were used to investigate Ca2+-induced annexin A4 translocation and self ... In this work, fluorescent protein fusions of annexin A4 were used to investigate Ca2+-induced annexin A4 translocation and self ... In this work, fluorescent protein fusions of annexin A4 were used to investigate Ca2+-induced annexin A4 translocation and self ... In this work, fluorescent protein fusions of annexin A4 were used to investigate Ca2+-induced annexin A4 translocation and self ...
Cat Number: CSB-BP339158LQA(A5). USA, UK & Europe Distribution. ... Annexin A5 Antibody , CSB-PA001846HA01EQC , CusabioAnnexin A5 ... Annexin A5 Antibody, HRP conjugated , CSB-PA001846HB01EQC , CusabioAnnexin A5 Antibody, HRP conjugated is Available at Gentaur ... Annexin A5 Antibody, FITC conjugated , CSB-PA001846HC01EQC , CusabioAnnexin A5 Antibody, FITC conjugated is Available at ... Annexin A5 Antibody, Biotin conjugated , CSB-PA001846HD01EQC , CusabioAnnexin A5 Antibody, Biotin conjugated is Available at ...
Annexin A5 Increases Survival in Murine Sepsis Model by Inhibiting HMGB1-Mediated Proinflammation and Coagulation The ... Recent studies have revealed that annexin A5, a 35 kDa Ca2+-dependent phospho... ...
Anti-CHO Annexin A5 Antibody , CNX5-65ALY , Immunology Consultatnt Laboratory Host: Chicken Format: Unconjugated AP Product ...
Shop enQuireBio™ Recombinant Human ANXA5 / Annexin 5 / Annexin A5 Protein at Fishersci.co.uk ...
annexin A5. ISO. RGD. PMID:20684318. RGD:7241850. NCBI chr19:18,419,936...18,450,088 Ensembl chr19:18,407,587...18,570,378 ... ariadne RBR E3 ubiquitin protein ligase 1. involved_in. IEA. Ensembl. GO_REF:0000107. NCBI chr30:36,058,932...36,109,206 ...
Annexin A5 regulates hepatic macrophage polarization via directly targeting PKM2 and ameliorates NASH. Xu F, Guo M, Huang W, ...
Glomerular Annexin A3 and Cathepsin C Staining in COVID-19-Associated and HIV-Associated Nephropathy (HIVAN)-Associated ... Glomerular Annexin A3 and Cathepsin C Staining in COVID-19-Associated and HIV-Associated Nephropathy (HIVAN)-Associated ...
annexin a5 (1) * apoptosis (1) * bromides (1) * ca(2+)-transporting atpase (1) ...
Annexin A5 (ANXA5); and Protein S100-A9, also known as calgranulin B that, when complexed with S100A8, forms calprotectin. ...
Annexin A2 and S100A10 are independent predictors of serous ovarian cancer outcome.. Transl Res. 2016; 171:83-95.e1-2 [PubMed] ... S100A2, A6, A8, A9, A10, and A11 mRNA was expressed at high level, while S100A1, A3, A4, A5, A6, A7, and A12 mRNA expression ... The siRNA targeting annexin II of MDA-MB-435s cells did not only decrease annexin II messenger RNA and protein levels, but also ... We then silenced the expression of annexin II in MDA-MB-435s, which was found to over express annexin II, using the chemically- ...
ANXA4 annexin A4 [ Macaca mulatta (Rhesus monkey) ]. Official Symbol :. ANXA4. Synonyms :. ANXA4; annexin A4;. ... ANXA4 can also interact with other annexin proteins or cytoskeletal proteins, potentially contributing to its diverse cellular ...
ANXA4; annexin A4; ANX4; P32.5; PP4-X; PAP-II; annexin-4; protein II; endonexin I; lipocortin IV; chromobindin-4; 35-beta ... Antigen standard for annexin A4 (ANXA4) is a lysate prepared from HEK293T cells transiently transfected with a TrueORF gene- ... ANXA4 can also interact with other annexin proteins or cytoskeletal proteins, potentially contributing to its diverse cellular ... annexin IV (placental anticoagulant protein II); PIG28; ZAP36; MGC75105; DKFZp686H02120;. ...
Annexin A3 as a Potential Target for Immunotherapy of Liver Cancer Stem-Like Cells.. Authors - Qiu-Zhong Pan. View Article ...
01010003875 Recombinant Human Annexin A5 Info genways bulk GWB-B295FB bulk Ask Ask ...
... in/on annexin A5 (A5) positive (i.e., apoptotic) THP1 cells (Fig. 1d). Additionally, we infected THP1 cells with a genetically ... number of A5+ ApoBDs/number of A5+ cells) f, and the total number of A5+ monocytes within the BAL g (control n = 18 and Halo ... and Atkin-Smith et al., using A5 and TO-PRO-3-based analysis15,49. HA staining was performed using 1:250 HA-FITC, in A5 binding ... ApoBD formation index = number of A5+ ApoBDs/number of A5+ apoptotic cells. d THP1 monocytes were infected with PR8, and the ...
Stewart, David John Ossian (2019) Investigating the metamorphic properties of annexin A5 during membrane integration. PhD ...
Stewart, David John Ossian (2019) Investigating the metamorphic properties of annexin A5 during membrane integration. PhD ... Hsia, Oliver (2020) Characterisation of the role of the NEDD8 E3 ligase DCNL5 in the apoptosis response. PhD thesis, University ... Williams, Jamie John Lewis (2012) Identification of substrates for the Epac1-inducible E3 ubiquitin ligase component SOCS3. PhD ...
Human ANXA4(Annexin A4) ELISA Kit. EH1904 FN Test 96T. 681.12 EUR ... Human ANXA11(Annexin A11) ELISA Kit. Human ANXA11(Annexin A11) ELISA Kit ... Description: A sandwich ELISA kit for detection of Annexin A11 from Human in samples from blood, serum, plasma, cell culture ... Description: A sandwich ELISA kit for detection of Annexin A10 from Human in samples from blood, serum, plasma, cell culture ...
Human Annexin A4, ANXA4 ELISA KIT. ELI-05616h Lifescience Market 96 Tests. 988.8 EUR ... Human ANXA7(Annexin A7) ELISA Kit. Human ANXA7(Annexin A7) ELISA Kit ... Description: A sandwich ELISA kit for detection of Annexin A7 from Human in samples from blood, serum, plasma, cell culture ... Description: A sandwich quantitative ELISA assay kit for detection of Human Annexin A10 (ANXA10) in samples from serum, plasma ...
Topical delivery of Avastin to the posterior segment of the eye In vivo using annexin A5-associated liposomes, Small, Vol:10, ...
Alternative names and symbols: annexin 14; ANX14. Related products: Rabbit anti Annexin A10 polyclonal antibody [AB-10007]. ... Human ANXA3 (Annexin A3) recombinant protein €69,00. - €2.170,00. SKU: PRO-50002 ... Gene name: Annexin A10. Gene symbol: ANXA10. Organism: Homo sapiens. GenBank accession: NM_007193.3. Protein accession: NP_ ...
London E1 4NS Tel: +44 (0)20 7882 5555 © Queen Mary University of London. ... Annexin-A1 restricts Th17 cells and attenuates the severity of autoimmune disease * QMRO Home ... Annexin-A1 restricts Th17 cells and attenuates the severity of autoimmune disease. ... Annexin-A1 restricts Th17 cells and attenuates the severity of autoimmune disease ...
Description: Annexin V or A5 has been proposed to play a role in the inhibition of blood coagulation by competing for ... Description: Annexin 5 belongs to the annexin family of calcium-dependent phospholipid binding proteins some of which have been ... Description: Annexin 5 belongs to the annexin family of calcium-dependent phospholipid binding proteins some of which have been ... we hypothesized that SCA-associated VOC could also be because of the presence of anti-annexin V antibodies. Anti-annexin V ...
Molecular imaging of plaque inflammation: Tahara and colleagues provide an overview of 18F-FDG and 99mTc-annexin-A5 imaging in ...
annexin A3. Molecular. skeletal muscle. Mouse. Anxa3. 23.0% Increase Gene Expression Level. Add. ...
2014In-vivo monitoring of erythropoietin treatment after myocardial infarction in mice with [(6)(8)Ga]Annexin A5 and [(1)(8)F] ... annexin A5 and [18F]fluorodeoxyglucose positron emission tomography. Mol Imaging 13: 1-8In vivo monitoring of parathyroid ... annexin A5 and [18F]fluorodeoxyglucose positron emission tomography. Mol Imaging. 13 ...
  • M2/ANXA5 haplotype, a variation at the core promoter region of Annexin A5 (ANXA5) gene, was suggested to be a predisposition factor for RPL. (usm.my)
  • Annexin A5(ANXA5), is a member of the structurally related family of?annexin?proteins some of which have been implicated in membrane-related events along exocytotic and endocytotic pathways. (bioactiva.com)
  • CusabioAnnexin A5 Antibody is Available at Gentaur Genprice with the fastest delivery.Online Order Payment is possible or send quotation to info@gentaur. (joplink.net)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Annexin A11 (ANXA11) in Tissue homogenates and other biological fluids. (jsce-ip.com)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Annexin A7 (ANXA7) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (scalegen.com)
  • Monovariate logistic regression evaluation demonstrated a optimistic dose-effect relationship for anti-annexin V IgM with VOC, with elevated VOC danger seen with elevated antibody titers. (ncbcs.org)
  • Induction of apoptosis by cross-linking antibodies certain to human B-lymphoma cells: expression of Annexin V binding websites on the antibody cap. (ncbcs.org)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Annexin A7 (ANXA7) in tissue homogenates, cell lysates and other biological fluids. (2sars.com)
  • ANXA4 can also interact with other annexin proteins or cytoskeletal proteins, potentially contributing to its diverse cellular functions. (creativebiomart.net)
  • Antigen standard for annexin A4 (ANXA4) is a lysate prepared from HEK293T cells transiently transfected with a TrueORF gene-carrying pCMV plasmid and then lysed in RIPA Buffer. (creativebiomart.net)
  • Annexin A5 was proposed to use in detection of apoptosis. (cusabio.com)
  • Flow cytometric analysis of annexin V binding/PI exclusion and DNA fragmentation disclosed that all these alkaloids could induce apoptosis in OCM-1 cells. (unideb.hu)
  • Furthermore, we conducted Annexin V-FITC/PI apoptosis assay and Western blotting to determine whether andrographolide has an impact on the death pattern of RSV-infected cells. (researchsquare.com)
  • Annexin V is a valuable tool for studying cell apoptosis. (aatbio.com)
  • Annexin V-dye conjugates are widely used to monitor cell apoptosis through measuring the translocation of phosphatidylserine (PS). (aatbio.com)
  • Cy5-Annexin V probe is one of the most popular fluorescent dye-Annexin V conjugates used for monitoring cell apoptosis. (aatbio.com)
  • Annexin A3 is a protein that in humans is encoded by the ANXA3 gene. (wikipedia.org)
  • Protein of the annexin family originally isolated from the electric organ of the electric ray Torpedo marmorata. (uchicago.edu)
  • Proteomic characterization of ovarian cancers identifying annexin-A4, phosphoserine aminotransferase, cellular retinoic acid-binding protein 2, and serpin B5 as histology-specific biomarkers. (uchicago.edu)
  • In this work, fluorescent protein fusions of annexin A4 were used to investigate Ca 2+ -induced annexin A4 translocation and self-association on membrane surfaces in living cells. (elsevierpure.com)
  • Our work provides mechanistic insight into how annexin A4 may regulate plasma membrane protein function. (elsevierpure.com)
  • Piljić, A & Schultz, C 2006, ' Annexin A4 self-association modulates general membrane protein mobility in living cells ', Molecular biology of the cell , vol. 17, no. 7, pp. 3318-3328. (elsevierpure.com)
  • We emphasize the 35 kD human protein annexin A5, that has been developed as a Molecular Imaging agent to measure cell death in vitro, and non-invasively in vivo in animal models and in patients with cardiovascular diseases and cancer. (maastrichtuniversity.nl)
  • Annexin 5 is a phospholipase A2 and protein kinase C inhibitory protein with calcium channel activity and a potential role in cellular signal transduction, inflammation, growth and differentiation. (bioactiva.com)
  • Annexin 5 has also been described as placental anticoagulant protein I, vascular anticoagulant-alpha, endonexin II, lipocortin V, placental protein 4 and anchorin CII. (bioactiva.com)
  • Description: A sandwich ELISA kit for detection of Annexin A11 from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (jsce-ip.com)
  • Description: A competitive ELISA for quantitative measurement of Canine Annexin A11(ANXA11) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (jsce-ip.com)
  • Description: A sandwich ELISA kit for detection of Annexin A7 from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (scalegen.com)
  • Description: Quantitativesandwich ELISA kit for measuring Mouse Annexin A7 (ANXA7) in samples from serum, plasma, tissue homogenates. (scalegen.com)
  • Anti-annexin V antibodies have been measured with ELISA in 177 VOC and 81 steady-state SCA sufferers. (ncbcs.org)
  • Sera of 40 scleroderma sufferers and 15 wholesome controls have been examined for IgG and IgM anti-annexin V antibodies by ELISA and anticentromere antibodies by oblique immunofluorescence. (ncbcs.org)
  • Annexins, found in most eukaryotic species, are cytosolic proteins that are able to bind negatively-charged phospholipids in a calcium-dependent manner. (lcam-fnwi.nl)
  • Annexins are Ca 2+ -regulated phospholipid-binding proteins whose function is only partially understood. (elsevierpure.com)
  • The experiments revealed the immobile nature of annexin A4 aggregates on membrane surfaces, which in turn strongly reduced the mobility of transmembrane and plasma membrane associated proteins. (elsevierpure.com)
  • Annexins are a family of proteins that bind to phospholipid membranes in the presence of calcium. (aatbio.com)
  • that is characterized by arterial, venous, or microvascular thrombosis or recurrent pregnancy loss caused by antibodies directed against one or more phospholipid-bound proteins (eg, beta-2 glycoprotein 1, prothrombin, annexin A5). (msdmanuals.com)
  • It is not common to perform Annexin V binding flow cytometric analysis on adherent cells due to the possibility of membrane damage during cell detachment or harvesting. (aatbio.com)
  • Scientific significance of serum anti- annexin V antibodies in Egyptian sufferers with scleroderma. (ncbcs.org)
  • In conclusion, measurement of serum anti-annexin V IgG antibodies in scleroderma sufferers could also be necessary for early prognosis of vascular and pulmonary issues. (ncbcs.org)
  • Serum level of annexin A5 is related to annexin A5 expression in cancer tissues. (cusabio.com)
  • Serum annexin A5 level was not altered in pre-eclampsia. (cusabio.com)
  • The fluorescent annexin V conjugates are stored in a PBS buffer solution containing 0.1% bovine serum albumin (BSA) with a pH of 7.4. (aatbio.com)
  • Annexin A2 and S100A10 as Candidate Prognostic Markers in Epithelial Ovarian Cancer. (cancerindex.org)
  • The aim of this study was to examine whether Annexin A2 and S100A10 expression can be used as prognostic markers for epithelial ovarian cancer (EOC). (cancerindex.org)
  • Add Annexin V conjugate assay solution. (aatbio.com)
  • Add 2 μL of the Annexin V conjugate to the cells. (aatbio.com)
  • This gene encodes a member of the annexin family. (wikipedia.org)
  • Tahara and colleagues provide an overview of 18 F-FDG and 99m Tc-annexin-A5 imaging in the setting of acute cardiac events and look at the advantages and clinical feasibility of molecular imaging in atherosclerosis. (snmjournals.org)
  • Prepare an Annexin V-binding assay buffer: 10 mM HEPES, 140 mM NaCl, and 2.5 mM CaCl2, pH 7.4. (aatbio.com)
  • Resuspend cells in 200 μL of the Annexin V-binding assay buffer from Step 1. (aatbio.com)
  • Add 300 μL of the Annexin V-binding assay buffer (from Step 1) to increase volume before analyzing the cells with a flow cytometer or fluorescence microscope. (aatbio.com)
  • Recently focus has shifted from diagnostic towards therapeutic applications employing annexin A5 in strategies to deliver drugs to cells that express PS at their surface. (maastrichtuniversity.nl)
  • Rational Laboratory Diagnostics of Antiphospholipid Antibodies: Anti-Cardiolipin, Anti-β2-Glycoprotein I, Anti-Prothrombin and Anti-Annexin V Antibodies. (ncbcs.org)
  • Pathogenic natural antibodies recognizing annexin IV are required to develop intestinal ischemia-reperfusion injury. (uchicago.edu)
  • A attainable co-appearance of anticardiolipin (aCL), anti-β2-glycoprotein I (anti-β2-GPI), anti-prothrombin (aPT) and anti-annexin V (aANXV) antibodies of IgG, IgM and IgA class have been studied in 58 sufferers with SLE alone and 32 sufferers APS within the view of rational laboratory diagnostics. (ncbcs.org)
  • Anti- annexin V IgG and IgM antibodies in sickle cell illness sufferers with vaso-occlusive disaster. (ncbcs.org)
  • In view of their prothrombotic nature, we hypothesized that SCA-associated VOC could also be because of the presence of anti-annexin V antibodies. (ncbcs.org)
  • After categorizing anti-annexin V antibodies, the adjusted odds ratio elevated because the percentile worth elevated. (ncbcs.org)
  • Anti-annexin V IgG antibodies correlated positively with VOC kind and negatively with HbF and age of VOC onset, whereas anti-annexin V IgM correlated positively with VOC kind, length, frequency, web site, ache severity, hospitalization, and medicine, and negatively with age of VOC onset and HbS ranges. (ncbcs.org)
  • Excessive ranges of anti-annexin V IgM antibodies represent a danger issue for VOC in SCA sufferers. (ncbcs.org)
  • We investigated the prevalence of anti-annexin V IgG and IgM antibodies in sera of scleroderma sufferers and their relation to the presence of different antibodies and improvement of illness morbidity. (ncbcs.org)
  • The high-resolution crystal structure of human annexin III shows subtle differences with annexin V.". Biochemistry. (wikipedia.org)
  • Mobility of annexin A4 on membrane surfaces was investigated by FRAP. (elsevierpure.com)
  • Univariate Cox regression analysis showed that Annexin A2 and S100A10 in stromal tissue correlated with shorter overall survival (OS). (cancerindex.org)
  • Multivariate Cox regression analysis demonstrated no independent prognostic significance of stromal Annexin A2 expression. (cancerindex.org)
  • Annexin A4 is a member of this family that is believed to be involved in exocytosis and regulation of epithelial Cl - secretion. (elsevierpure.com)
  • Quantify Annexin V conjugates binding by using a flow cytometer with appropriate filters. (aatbio.com)
  • Expression of Annexin A2 and S100A10 was evaluated in EOC tissue samples (n=303) by immunohistochemistry. (cancerindex.org)
  • In patients with colon cancer, annexin A5 expression in cancer tissues is related to lymph node metastasis and tumor grade. (cusabio.com)
  • This graph shows the total number of publications written about "Annexin A4" by people in this website by year, and whether "Annexin A4" was a major or minor topic of these publications. (uchicago.edu)