Defensins
alpha-Defensins
Blood Proteins
Antimicrobial Cationic Peptides
Neutrophils
Anti-Infective Agents
Cathelicidins
Paneth Cells
Blood Bactericidal Activity
Amino Acid Sequence
Molecular Sequence Data
Tracheobionta
Fusarium
Urogenital System
Cathepsin G
Defensins impair phagocytic killing by neutrophils in biomaterial-related infection. (1/549)
The implantation of foreign material carries a risk of infection which frequently is resistant to all treatment short of removing the implant. We have previously shown that these materials activate neutrophils by contact, leading to production of oxygen free radicals accompanied by release of granule products. Such activation further results in depletion of local host defenses, including the capacity of biomaterial-activated neutrophils to kill bacteria. Among the granule products released from neutrophils are small cationic antibacterial peptides (human neutrophil peptides [HNP]) known as defensins. Here we tested the hypothesis that defensins, released from activated neutrophils onto the surface of biomaterials, might play a role in the deactivation of subsequent neutrophil populations. Incubation of neutrophils with purified HNP resulted in a dose-related impairment of stimulus-induced oxygen radical production and of phagocytic killing. Furthermore, fresh neutrophils added to biomaterial-associated neutrophils exhibited impaired phagocytic killing. This impairment could be abrogated by antibody to HNP but not by an irrelevant antibody. Taken together, these observations support the idea that neutrophils activated at a material surface can create, by means of HNP release, an environment hostile to their microbicidal function and that of their infiltrating brethren. (+info)Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. (2/549)
Positively charged antimicrobial peptides with membrane-damaging activity are produced by animals and humans as components of their innate immunity against bacterial infections and also by many bacteria to inhibit competing microorganisms. Staphylococcus aureus and Staphylococcus xylosus, which tolerate high concentrations of several antimicrobial peptides, were mutagenized to identify genes responsible for this insensitivity. Several mutants with increased sensitivity were obtained, which exhibited an altered structure of teichoic acids, major components of the Gram-positive cell wall. The mutant teichoic acids lacked D-alanine, as a result of which the cells carried an increased negative surface charge. The mutant cells bound fewer anionic, but more positively charged proteins. They were sensitive to human defensin HNP1-3, animal-derived protegrins, tachyplesins, and magainin II, and to the bacteria-derived peptides gallidermin and nisin. The mutated genes shared sequence similarity with the dlt genes involved in the transfer of D-alanine into teichoic acids from other Gram-positive bacteria. Wild-type strains bearing additional copies of the dlt operon produced teichoic acids with higher amounts of D-alanine esters, bound cationic proteins less effectively and were less sensitive to antimicrobial peptides. We propose a role of the D-alanine-esterified teichoic acids which occur in many pathogenic bacteria in the protection against human and animal defense systems. (+info)Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity. (3/549)
Lepidoptera have been reported to produce several antibacterial peptides in response to septic injury. However, in marked contrast to other insect groups, no inducible antifungal molecules had been described so far in this insect order. Surprisingly, also cysteine-rich antimicrobial peptides, which predominate in the antimicrobial defense of other insects, had not been discovered in Lepidoptera. Here we report the isolation from the hemolymph of immune induced larvae of the lepidopteran Heliothis virescens of a cysteine-rich molecule with exclusive antifungal activity. We have fully characterized this antifungal molecule, which has significant homology with the insect defensins, a large family of antibacterial peptides directed against Gram-positive strains. Interestingly, the novel peptide shows also similarities with the antifungal peptide drosomycin from Drosophila. Thus, Lepidoptera appear to have built their humoral immune response against bacteria on cecropins and attacins. In addition, we report that Lepidoptera have conferred antifungal properties to the well conserved structure of antibacterial insect defensins through amino acid replacements. (+info)Toll receptor-mediated Drosophila immune response requires Dif, an NF-kappaB factor. (4/549)
The induction of immunity genes in Drosophila has been proposed to be dependent on Dorsal, Dif, and Relish, the NF-kappaB-related factors. Here we provide genetic evidence that Dif is required for the induction of only a subset of antimicrobial peptide genes. The results show that the presence of Dif without Dorsal is sufficient to mediate the induction of drosomycin and defensin. We also demonstrate that Dif is a downstream component of the Toll signaling pathway in activating the drosomycin expression. These results reveal that individual members of the NF-kappaB family in Drosophila have distinct roles in immunity and development. (+info)In vitro antibacterial activities of platelet microbicidal protein and neutrophil defensin against Staphylococcus aureus are influenced by antibiotics differing in mechanism of action. (5/549)
Thrombin-induced platelet microbicidal protein-1 (tPMP-1) and human neutrophil defensin-1 (HNP-1) are small, cationic antimicrobial peptides. These peptides exert potent in vitro microbicidal activity against a broad spectrum of human pathogens, including Staphylococcus aureus. Evidence suggests that tPMP-1 and HNP-1 target and disrupt the bacterial membrane. However, it is not yet clear whether membrane disruption itself is sufficient to kill the bacterium or whether subsequent, presumably intracellular, events are also involved in killing. We investigated the staphylocidal activities of tPMP-1 and HNP-1 in the presence or absence of pretreatment with antibiotics that differ in their mechanisms of action. The staphylocidal effects of tPMP-1 and HNP-1 on control cells (no antibiotic pretreatment) were rapid and concentration dependent. Pretreatment of S. aureus with either penicillin or vancomycin (bacterial cell wall synthesis inhibitors) significantly enhanced the anti-S. aureus effects of tPMP-1 compared with the effects against the respective control cells over the entire tPMP-1 concentration range tested (P < 0.05). Similarly, S. aureus cells pretreated with these antibiotics were more susceptible to HNP-1 than control cells, although the difference in the effects against cells that received penicillin pretreatment did not reach statistical significance (P < 0.05 for cells that received vancomycin pretreatment versus effects against control cells). Studies with isogenic pairs of strains with normal or deficient autolytic enzyme activities demonstrated that enhancement of S. aureus killing by cationic peptides and cell wall-active agents could not be ascribed to a predominant role of autolytic enzyme activation. Pretreatment of S. aureus cells with tetracycline, a 30S ribosomal subunit inhibitor, significantly decreased the staphylocidal effect of tPMP-1 over a wide peptide concentration range (0.16 to 1.25 microgram/ml) (P < 0.05). Furthermore, pretreatment with novobiocin (an inhibitor of bacterial DNA gyrase subunit B) and with azithromycin, quinupristin, or dalfopristin (50S ribosomal subunit protein synthesis inhibitors) essentially blocked the S. aureus killing resulting from exposure to tPMP-1 or HNP-1 at most concentrations compared with the effects against the respective control cells (P < 0.05 for a tPMP-1 concentration range of 0.31 to 1.25 microgram/ml and for an HNP-1 concentration range of 6.25 to 50 microgram/ml). These findings suggest that tPMP-1 and HNP-1 exert anti-S. aureus activities through mechanisms involving both the cell membrane and intracellular targets. (+info)Production of beta-defensin antimicrobial peptides by the oral mucosa and salivary glands. (6/549)
beta-Defensins are cationic peptides with broad-spectrum antimicrobial activity that are produced by epithelia at mucosal surfaces. Two human beta-defensins, HBD-1 and HBD-2, were discovered in 1995 and 1997, respectively. However, little is known about the expression of HBD-1 or HBD-2 in tissues of the oral cavity and whether these proteins are secreted. In this study, we characterized the expression of HBD-1 and HBD-2 mRNAs within the major salivary glands, tongue, gingiva, and buccal mucosa and detected beta-defensin peptides in salivary secretions. Defensin mRNA expression was quantitated by RNase protection assays. HBD-1 mRNA expression was detected in the gingiva, parotid gland, buccal mucosa, and tongue. Expression of HBD-2 mRNA was detected only in the gingival mucosa and was most abundant in tissues with associated inflammation. To test whether beta-defensin expression was inducible, gingival keratinocyte cell cultures were treated with interleukin-1beta (IL-1beta) or bacterial lipopolysaccharide (LPS) for 24 h. HBD-2 expression increased approximately 16-fold with IL-1beta treatment and approximately 5-fold in the presence of LPS. Western immunoblotting, liquid chromatography, and mass spectrometry were used to identify the HBD-1 and HBD-2 peptides in human saliva. Human beta-defensins are expressed in oral tissues, and the proteins are secreted in saliva; HBD-1 expression was constitutive, while HBD-2 expression was induced by IL-1beta and LPS. Human beta-defensins may play an important role in the innate defenses against oral microorganisms. (+info)Porcine epithelial beta-defensin 1 is expressed in the dorsal tongue at antimicrobial concentrations. (7/549)
Epithelial cells and phagocytes contain antimicrobial polypeptides that participate in innate host defense. A recently cloned porcine beta-defensin, PBD-1, was detected by Northern organ blots exclusively in the tongue epithelium. We generated recombinant PBD-1 peptide by using a baculovirus-insect cell expression system and obtained two forms (PBD-142 and PBD-138), which differed by N-terminal truncation. Only PBD-142 was found in scrapings of the surface of the dorsal tongue or the buccal mucosa. Immunohistochemical staining with antibody to PBD-142 revealed that PBD-1 was highly concentrated in an approximately 0.1-mm-thick layer in the cornified tips of the filiform (but not fungiform) papillae of the dorsal tongue and in the superficial squamous cell layers of the buccal mucosa. By scraping, extraction, and semiquantitative Western blotting, the concentration of PBD-1 in the dorsal tongue surface and the buccal mucosa was estimated at 20 to 100 micrograms/ml. PBD-1 had antibacterial activity against Escherichia coli, Salmonella typhimurium, Listeria monocytogenes, and Candida albicans in 10 mM sodium phosphate buffer (pH 7.4). Added NaCl progressively inhibited the activity of PBD-1 against E. coli and C. albicans. In 10 mM sodium phosphate with 125 mM NaCl, the combinations of sublethal concentrations of PBD-1 and the porcine neutrophil peptide PG-3, PR-39, or PR-26 showed synergistic activity against E. coli or the multidrug-resistant S. typhimurium DT104. At its physiologic concentration, PBD-1 has antimicrobial effects under both low- and high-salt conditions encountered in the oral cavity and may contribute to the antimicrobial barrier properties of the dorsal tongue and oral epithelium. (+info)Antimicrobial defensin peptides of the human ocular surface. (8/549)
BACKGROUND/AIMS: The antimicrobial activity of the tear film exceeds the activity of its known constituents. The authors postulate that this excess activity is the result of antimicrobial peptides called defensins, and they aimed to look for defensins in the human eye. METHODS: Evidence of defensin production was sought by reverse transcriptase polymerase chain reaction (RT-PCR). Intron spanning primers were designed for beta defensins 1 and 2, and alpha defensins 5 and 6. RT-PCR was performed on cornea, conjunctiva, and lacrimal gland samples, and reaction products were size fractionated and sequenced to confirm their identity. A monoclonal antibody was utilised for the detection of alpha defensins 1, 2, and 3 in tissue sections and in immunoblots of tears. RESULTS: RT-PCR revealed beta defensin 1 message in samples of conjunctiva, cornea, and lacrimal gland. beta Defensin 2 message was detected in the conjunctiva and cornea but was absent from the lacrimal gland. alpha Defensin 5 and 6 message was absent in these tissues but alpha defensins 1, 2, and 3 were detected in normal tears, lacrimal gland, and inflamed conjunctiva by immunochemistry. CONCLUSION: The data suggest the human eye innately produces a spectrum of antimicrobial defensin peptides. Defensins hold therapeutic potential in ocular infections as they have a broad spectrum of antimicrobial activity (bacteria fungi and viruses ) and accelerate epithelial healing. (+info)Defensins are small, cationic host defense peptides that contribute to the innate immune system's response against microbial pathogens. They are produced by various cell types, including neutrophils, epithelial cells, and some bone marrow-derived cells. Defensins have a broad spectrum of antimicrobial activity against bacteria, fungi, viruses, and enveloped lipid bilayers.
Defensins are classified into two main groups: α-defensins and β-defensins. Human α-defensins include human neutrophil peptides (HNP) 1-4 and human defensin 5, 6 (HD5, HD6). These are primarily produced by neutrophils and Paneth cells in the small intestine. β-defensins, on the other hand, are produced by various epithelial cells throughout the body.
Defensins work by disrupting the microbial membrane's integrity, leading to cell lysis and death. They also have immunomodulatory functions, such as chemotaxis of immune cells, modulation of cytokine production, and enhancement of adaptive immune responses. Dysregulation of defensin expression has been implicated in several diseases, including inflammatory bowel disease, chronic obstructive pulmonary disease, and certain skin disorders.
Alpha-defensins are a type of defensin, which are small cationic host defense peptides that contribute to the innate immune system's response to microbial invasion. They are primarily produced by neutrophils, but can also be expressed by some epithelial cells and other immune cells. Alpha-defensins have broad-spectrum antimicrobial activity against bacteria, fungi, and enveloped viruses. They also play a role in modulating the inflammatory response and wound healing. There are six human alpha-defensin genes (DEFA1 to DEFA6) that encode six different peptides: Human Neutrophil Peptides 1-4 (HNP1-4) and Human Defensin 5 and 6 (HD5 and HD6). The HNPs are stored in the azurophilic granules of neutrophils and are released upon their activation, while HD5 and HD6 are found in the Paneth cells of the small intestine.
Beta-defensins are a group of small, cationic host defense peptides that play an important role in the innate immune system. They have broad-spectrum antimicrobial activity against various pathogens, including bacteria, fungi, and viruses. Beta-defensins are produced by epithelial cells, phagocytes, and other cell types in response to infection or inflammation. They function by disrupting the membranes of microbes, leading to their death. Additionally, beta-defensins can also modulate the immune response by recruiting immune cells to the site of infection and regulating inflammation. Mutations in beta-defensin genes have been associated with increased susceptibility to infectious diseases.
Blood proteins, also known as serum proteins, are a group of complex molecules present in the blood that are essential for various physiological functions. These proteins include albumin, globulins (alpha, beta, and gamma), and fibrinogen. They play crucial roles in maintaining oncotic pressure, transporting hormones, enzymes, vitamins, and minerals, providing immune defense, and contributing to blood clotting.
Albumin is the most abundant protein in the blood, accounting for about 60% of the total protein mass. It functions as a transporter of various substances, such as hormones, fatty acids, and drugs, and helps maintain oncotic pressure, which is essential for fluid balance between the blood vessels and surrounding tissues.
Globulins are divided into three main categories: alpha, beta, and gamma globulins. Alpha and beta globulins consist of transport proteins like lipoproteins, hormone-binding proteins, and enzymes. Gamma globulins, also known as immunoglobulins or antibodies, are essential for the immune system's defense against pathogens.
Fibrinogen is a protein involved in blood clotting. When an injury occurs, fibrinogen is converted into fibrin, which forms a mesh to trap platelets and form a clot, preventing excessive bleeding.
Abnormal levels of these proteins can indicate various medical conditions, such as liver or kidney disease, malnutrition, infections, inflammation, or autoimmune disorders. Blood protein levels are typically measured through laboratory tests like serum protein electrophoresis (SPE) and immunoelectrophoresis (IEP).
Antimicrobial cationic peptides (ACPs) are a group of small, naturally occurring peptides that possess broad-spectrum antimicrobial activity against various microorganisms, including bacteria, fungi, viruses, and parasites. They are called "cationic" because they contain positively charged amino acid residues (such as lysine and arginine), which allow them to interact with and disrupt the negatively charged membranes of microbial cells.
ACPs are produced by a wide range of organisms, including humans, animals, and plants, as part of their innate immune response to infection. They play an important role in protecting the host from invading pathogens by directly killing them or inhibiting their growth.
The antimicrobial activity of ACPs is thought to be mediated by their ability to disrupt the membranes of microbial cells, leading to leakage of cellular contents and death. Some ACPs may also have intracellular targets, such as DNA or protein synthesis, that contribute to their antimicrobial activity.
ACPs are being studied for their potential use as therapeutic agents to treat infectious diseases, particularly those caused by drug-resistant bacteria. However, their clinical application is still in the early stages of development due to concerns about their potential toxicity to host cells and the emergence of resistance mechanisms in microbial pathogens.
Neutrophils are a type of white blood cell that are part of the immune system's response to infection. They are produced in the bone marrow and released into the bloodstream where they circulate and are able to move quickly to sites of infection or inflammation in the body. Neutrophils are capable of engulfing and destroying bacteria, viruses, and other foreign substances through a process called phagocytosis. They are also involved in the release of inflammatory mediators, which can contribute to tissue damage in some cases. Neutrophils are characterized by the presence of granules in their cytoplasm, which contain enzymes and other proteins that help them carry out their immune functions.
Anti-infective agents are a class of medications that are used to treat infections caused by various microorganisms such as bacteria, viruses, fungi, and parasites. These agents work by either killing the microorganism or inhibiting its growth, thereby helping to control the infection and alleviate symptoms.
There are several types of anti-infective agents, including:
1. Antibiotics: These are medications that are used to treat bacterial infections. They work by either killing bacteria (bactericidal) or inhibiting their growth (bacteriostatic).
2. Antivirals: These are medications that are used to treat viral infections. They work by interfering with the replication of the virus, preventing it from spreading and causing further damage.
3. Antifungals: These are medications that are used to treat fungal infections. They work by disrupting the cell membrane of the fungus, killing it or inhibiting its growth.
4. Antiparasitics: These are medications that are used to treat parasitic infections. They work by either killing the parasite or inhibiting its growth and reproduction.
It is important to note that anti-infective agents are not effective against all types of infections, and it is essential to use them appropriately to avoid the development of drug-resistant strains of microorganisms.
Cathelicidins are a family of antimicrobial peptides that are widely distributed in nature and play an important role in the innate immune system. They are expressed in various tissues, including the epithelia of the respiratory, gastrointestinal, and urogenital tracts, as well as in immune cells such as neutrophils and macrophages.
The human cathelicidin gene is called CAMP (camp gene) and encodes a precursor protein called hCAP-18 (human cationic antimicrobial protein of 18 kDa). After cleavage by proteolytic enzymes, the active peptide LL-37 is generated.
LL-37 has broad-spectrum antimicrobial activity against bacteria, viruses, fungi, and parasites. It also has immunomodulatory functions, such as chemotaxis of immune cells, modulation of cytokine production, and promotion of wound healing. Dysregulation of cathelicidins has been implicated in various inflammatory diseases, including chronic obstructive pulmonary disease (COPD), psoriasis, and rosacea.
Paneth cells are specialized epithelial cells located in the small intestine, specifically in the crypts of Lieberkühn. They play an essential role in the immune function and maintenance of the intestinal environment. Paneth cells are characterized by their large, granulated secretory vesicles that contain antimicrobial peptides and proteins, such as defensins and lysozyme. These substances help to control the growth of bacteria in the small intestine and maintain a balanced microbiota. Additionally, Paneth cells secrete other factors that support the function and survival of stem cells located in the crypts. They are also involved in the inflammatory response by producing cytokines and chemokines, which help to recruit immune cells to the site of infection or injury.
Blood bactericidal activity refers to the ability of an individual's blood to kill or inhibit the growth of bacteria. This is an important aspect of the body's immune system, as it helps to prevent infection and maintain overall health. The bactericidal activity of blood can be influenced by various factors, including the presence of antibodies, white blood cells (such as neutrophils), and complement proteins.
In medical terms, the term "bactericidal" specifically refers to an agent or substance that is capable of killing bacteria. Therefore, when we talk about blood bactericidal activity, we are referring to the collective ability of various components in the blood to kill or inhibit the growth of bacteria. This is often measured in laboratory tests as a way to assess a person's immune function and their susceptibility to infection.
It's worth noting that not all substances in the blood are bactericidal; some may simply inhibit the growth of bacteria without killing them. These substances are referred to as bacteriostatic. Both bactericidal and bacteriostatic agents play important roles in maintaining the body's defense against infection.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
"Tracheobionta" is not a standard medical term. However, in the field of biology, it is used to refer to a group of organisms that possess a respiratory system with a true trachea or its equivalent, such as insects, spiders, and other arthropods.
In a broader context, Tracheobionta is sometimes used interchangeably with the term "Tracheata," which refers to a taxonomic category that includes all organisms with a true tracheal system for respiration, including various invertebrate groups such as arthropods and nematodes.
However, it's important to note that these terms are not commonly used in medical contexts, but rather in the fields of biology, zoology, and taxonomy.
"Fusarium" is a genus of fungi that are widely distributed in the environment, particularly in soil, water, and on plants. They are known to cause a variety of diseases in animals, including humans, as well as in plants. In humans, Fusarium species can cause localized and systemic infections, particularly in immunocompromised individuals. These infections often manifest as keratitis (eye infection), onychomycosis (nail infection), and invasive fusariosis, which can affect various organs such as the lungs, brain, and bloodstream. Fusarium species produce a variety of toxins that can contaminate crops and pose a threat to food safety and human health.
The urogenital system is a part of the human body that includes the urinary and genital systems. The urinary system consists of the kidneys, ureters, bladder, and urethra, which work together to produce, store, and eliminate urine. On the other hand, the genital system, also known as the reproductive system, is responsible for the production, development, and reproduction of offspring. In males, this includes the testes, epididymis, vas deferens, seminal vesicles, prostate gland, bulbourethral glands, and penis. In females, it includes the ovaries, fallopian tubes, uterus, vagina, mammary glands, and external genitalia.
The urogenital system is closely related anatomically and functionally. For example, in males, the urethra serves as a shared conduit for both urine and semen, while in females, the urethra and vagina are separate but adjacent structures. Additionally, some organs, such as the prostate gland in males and the Skene's glands in females, have functions that overlap between the urinary and genital systems.
Disorders of the urogenital system can affect both the urinary and reproductive functions, leading to a range of symptoms such as pain, discomfort, infection, and difficulty with urination or sexual activity. Proper care and maintenance of the urogenital system are essential for overall health and well-being.
I'm sorry for any confusion, but "Petunia" is not a medical term. It's the name of a genus of plants in the family Solanaceae, commonly known as petunias. They are popular ornamental plants due to their vibrant and diverse flowers. If you have any questions about botany or gardening, I'd be happy to try to help with those!
Cathepsin G is a serine protease, which is a type of enzyme that breaks down other proteins. It is produced and released by neutrophils, a type of white blood cell that plays an important role in the body's immune response to infection. Cathepsin G helps to digest and kill microorganisms that have invaded the body. It can also contribute to tissue damage and inflammation in certain diseases, such as rheumatoid arthritis and cystic fibrosis.
Uridine Diphosphate N-Acetylmuramic Acid (UDP-MurNAc) is not a medical term per se, but rather a biochemical term. It is an important intermediate in the biosynthesis of peptidoglycan, a major component of bacterial cell walls.
To define it more accurately:
UDP-MurNAc is a nucleotide sugar that consists of N-acetylmuramic acid (MurNAc) linked to uridine diphosphate (UDP). MurNAc is a derivative of N-acetylglucosamine (GlcNAc), where a lactic acid is attached to the hydroxyl group at the C3 position.
This molecule plays a crucial role in the biosynthesis of peptidoglycan, which is essential for maintaining bacterial cell shape and integrity. The process begins with UDP-MurNAc, which undergoes several enzymatic modifications, including the addition of pentapeptide side chains, to form lipid II. Lipid II is then transported across the cytoplasmic membrane and incorporated into the existing peptidoglycan layer during cell wall synthesis.
While not a medical term itself, understanding UDP-MurNAc and its role in bacterial cell wall biosynthesis can be relevant to medical fields such as microbiology, infectious diseases, and antibiotic development.
Defensin - Wikipedia
Frontiers | Antifungal defensins and their role in plant defense
Defa41 MGI Mouse Gene Detail - MGI:3705230 - defensin, alpha, 41
β-defensin-1 regulates influenza virus infection in human bronchial epithelial cells through the STAT3 signaling pathway
beta-Defensin 2 Products: R&D Systems
Defensin peptides | Antimicrobial peptides | Eurogentec
Cardiac Defensins--Natural Antibiotics of the Heart - WSAVA2005 - VIN
Defensin beta 3 Antikörper, ELISA Kits
Beta defensin 129 DEFB129) - Gentaur.com
Defensins - NBS Biologicals
Live-cell Imaging of Fungal Cells to Investigate Modes of Entry and Subcellular Localization of Antifungal Plant Defensins |...
Mouse DEFa5 (Defensin Alpha 5, Paneth Cell Specific) ELISA Kit | G-EC-04309 | Gentaur Elisa Kits
defensin-beta-3 (Cytokines & Cells Encyclopedia - COPE)
Beta-Defensin Expression in the Canine Nasal Cavity
The Role of Defensins in Hidradenitis Suppurativa - University of Edinburgh Research Explorer
European Crohn´s and Colitis Organisation - ECCO - P169 Copy number variation of alpha defensin 1-3 is a predictive marker of...
Defensin - Chemwatch
ΔNp63 isoform-mediated β-defensin family up-regulation is associated with (lymph)angiogenesis and poor prognosis in patients...
Beta defensins. Medical search
Tissue-specific human beta-defensins (HBD)1, HBD2, and HBD3 secretion from human extra-placental membranes stimulated with...
MyBioSource - Beta defensin
Beta-Defensin-4 (Human) › PeptaNova
β-Defensin 3 - Cell Guidance Systems
Avian beta-defensin 1 (AvBD1) - Genepep
Gingival crevicular fluid levels of human beta-defensin 1 in individuals with and without chronic periodontitis
How Do Defensins Work as Anti-Aging Ingredients? - Dr. Leslie Baumann
Defensive effects of human antimicrobial peptide α-defensins against Enterococcus faecalis<...
beta Defensin-2 ELISA Assay | BD-2 ELISA | Eagle Biosciences
Synovasure® Alpha Defensin Lateral Flow Test Kit - Health Technology Wales
Peptides38
- Characteristic disulphide linkages The name 'defensin' was coined in the mid-1980s, though the proteins have been called 'Cationic Antimicrobial Proteins,' 'Neutrophil peptides,' 'Gamma thionins' amongst others. (wikipedia.org)
- In addition to the defensins involved in host defence, there are a number of related Defensin-Like Peptides (DLPs) that have evolved to have other activities. (wikipedia.org)
- only coined the term "plant defensin," after comparison of a new class of plant antifungal peptides with known insect defensins. (frontiersin.org)
- From there, many plant defensins have been reported and studies on this class of peptides encompass its activity toward microorganisms and molecular features of the mechanism of action against bacteria and fungi. (frontiersin.org)
- Defensins are small cationic peptides of 45-54 amino acid residues with a conserved signature of cysteines, which can form three to four disulfide bridges. (frontiersin.org)
- renamed these peptides as "plant defensins," after comparing their structural and functional resemblance to previously characterized AMPs found in insects and mammals. (frontiersin.org)
- Defensins are members of a family of microbicidal and cytotoxic peptides produced by neutrophils. (rndsystems.com)
- The defensins are a large family of small, cationic, cysteine- and arginine-rich antimicrobial peptides. (eurogentec.com)
- Human neutrophil peptides (HNP) 1-3 are microbicidal and cytotoxic defensins derived from a 94-amino acid prepro HNP1-94, co-translationally proteolyzed to proHNP20-94, then converted by removal of the anionic propiece to mature HNP65-94 (HNP-1 and -3) and HNP66-94 (HNP-2). (eurogentec.com)
- Defensins and cathelicidins constitute the two major groups of antimicrobial peptides in most mammalian species. (vin.com)
- The most abundant group of antimicrobial peptides is comprised by the α-, β- and θ-defensins. (vin.com)
- β-defensins are small (3.5-4.5 kDa) highly basic cationic peptides. (vin.com)
- Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. (antikoerper-online.de)
- GENTAUR supplies anti-defensins, monclonals, polyclonals antisera and recombinant DEFs or peptides of defensin. (gentaur.com)
- Constitutively produced or induced in inflammatory conditions, human beta-defensins (HβDs) are cationic peptides involved in host defenses against bacteria, viruses and fungi. (oncotarget.com)
- Production of beta-defensin antimicrobial peptides by the oral mucosa and salivary glands. (lookformedical.com)
- beta-Defensins are cationic peptides with broad-spectrum antimicrobial activity that are produced by epithelia at mucosal surfaces. (lookformedical.com)
- In this study, we characterized the expression of HBD-1 and HBD-2 mRNAs within the major salivary glands, tongue, gingiva, and buccal mucosa and detected beta-defensin peptides in salivary secretions. (lookformedical.com)
- beta-Defensins are cationic peptides with broad-spectrum antimicrobial activity that may play a role in mucosal defenses of several organs. (lookformedical.com)
- Three human beta-Defensin peptides, with the conserved disulfide connectivity between Cys 1 - Cys 5 , Cys 2 - Cys 4 , and Cys 3 - Cys 6 , have been isolated thus far, yet 28 β-Defensins were predicted in five gene clusters. (peptanova.de)
- These isolated peptides were actually human alpha-defensin-1 (hBD-1, Code 4337-s), human beta-defensin-2 (hBD-2, Code 4338-s) and human beta-defensin-3 (hBD-3, Code 4382-s). (peptanova.de)
- β-defensin 3 is a member of the defensin class of antimicrobial peptides. (mayflowerbio.com)
- One of the latest anti-aging strategies utilizes peptides called defensins to "turn on" the stem cells in the skin that are responsible for healing wounds. (lesliebaumannmd.com)
- The 8 in 1 Bioserum is my favorite) DefenAge uses a large, stable protein called albumin to stabilize, transport, and increase the efficacy of defensin peptides when applied topically. (lesliebaumannmd.com)
- Cationic and amphiphilic antimicrobial peptides (AMPs) such as α-defensins and cathelicidins are factors related to innate immunity. (elsevierpure.com)
- Defensins are 2-6 kDa, cationic, microbicidal peptides active against many Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses, containing three pairs of intramolecular disulphide bonds. (eaglebio.com)
- IntroductionThe antimicrobial peptides (AMPs) human -defensins and cathelicidin (LL-37) are key factors in innate and adaptive immune responses of the respiratory tract and play an important role in many respiratory diseases. (bezmialem.edu.tr)
- Defensins represent an evolutionary ancient family of antimicrobial peptides that play diverse roles in human health and disease. (le.ac.uk)
- Defensins are cationic cysteine-containing multifunctional peptides predominantly expressed by epithelial cells or neutrophils. (le.ac.uk)
- Defensins play a key role in host innate immune responses to infection and, in addition to their classically described role as antimicrobial peptides, have also been implicated in immune modulation, fertility, development, and wound healing. (le.ac.uk)
- β-defensins are important components of the vertebrate innate immune system responsible for encoding a variety of anti-microbial peptides. (uea.ac.uk)
- To investigate the structure and activity relationship, amino acid substitutions that alter charge were introduced into synthetic defensin peptides by adding 2-2 Arg (RR) and Asp (DD) at both the terminal and tested their effects on HIV-1, E. coli, S. aureus, and P. aeruginosa. (sciencecentral.in)
- In the present study, we have chemically synthesized native defensin peptides and their variants with Arg (RR) and Asp (DD) amino acid residues at N- and C-termini. (sciencecentral.in)
- The enhanced microbicidal activity observed for defensin peptides with Arg (RR) residues could be due to optimization of amphiphilicity of the structure, which could facilitate specific interactions with the microbial membranes. (sciencecentral.in)
- Human β-defensins 2 and 3 are small cationic peptides with antimicrobial activity against the fungal pathogen Candida albicans. (nebraska.edu)
- We found that hog1 and pbs2 mutants were hypersensitive to treatment with these peptides, pointing to a role of the high-osmolarity glycerol (HOG) pathway in the response to defensin-induced cell injury. (nebraska.edu)
- Big defensins are antimicrobial peptides (AMPs) that are proposed as important effectors of the immune response in mollusks, chelicerates and chordates. (pucv.cl)
- This review summarizes some immunological factors involved in the development and control of this oral disease, such as: the participation of inflammatory cells in local inflammation, the synthesis of chemotaxis proteins with activation of the complement system and a range of antimicrobial peptides, such as defensins, cathelicidin and saposins. (bvsalud.org)
Proteins8
- Defensins are small cysteine-rich cationic proteins across cellular life, including vertebrate and invertebrate animals, plants, and fungi. (wikipedia.org)
- Proteins called 'defensins' are not all evolutionarily related to one another. (wikipedia.org)
- Mature defensins are cationic proteins with three intramolecular disulfides and a characteristic triple-stranded beta-sheet. (rndsystems.com)
- At the amino acid sequence level, human beta-Defensin 2 shares 98% and 51% homology with the proteins from rhesus monkey and rat, respectively. (rndsystems.com)
- α-defensins are proteins found in neutrophils and intestinal epithelia . (eurogentec.com)
- Alpha- and beta-defensins are natural immune proteins that have been shown in in vitro studies to activate stem cells in the hair follicle, which typically helps with wound healing of the skin," says Yunyoung Claire Chang, M.D. , a board-certified cosmetic dermatologist. (hellogiggles.com)
- A further theory suggests that NOD2 mutations lead to a reduction in the production of alpha-defensins (small antibacterial proteins) by Paneth cells located in the small bowel. (medscape.com)
- Neutrophils from these individuals have abnormalities in nuclear morphology and lack primary, specific, and tertiary granule proteins including lactoferrin, collagenase, and defensins. (lu.se)
Neutrophils4
- human, mouse or other beta β- and alpha α- defensins are expressed by neutrophils ( α- ), lymphocytes and epithelial cells. (gentaur.com)
- Alpha-defensin 1-3 (DEFA1A3) is an antimicrobial peptide found in phagocytic cells such as neutrophils, functioning as an effector factor in innate immunity. (ecco-ibd.eu)
- DEFENSINS found in azurophilic granules of neutrophils and in the secretory granules of intestinal PANETH CELLS. (lookformedical.com)
- In cows, as many as 13 beta-defensins exist in neutrophils. (eaglebio.com)
Epithelial6
- Human beta-Defensin 2 expression is induced by inflammatory signals in multiple tissues, including airway epithelial cells and keratinocytes. (rndsystems.com)
- alpha, beta, theta (circle w/horizontal line)] Mammalian defensins are endogenous cysteine-rich peptide antibiotics classically produced either by epithelial cells of the respiratory, urogenital and digestive tracts, or by circulating cells including granulocytes and macrophages. (vin.com)
- Epithelial β-defensins constitute a rapidly mobilized local defense against microbial intruders at the epithelial and mucosal surfaces, and different studies have reported induction of epithelial β-defensins at sites of inflammation, injury, infection as well as other disease processes. (vin.com)
- This gene encodes defensin, beta 103B, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense. (antikoerper-online.de)
- DEFENSINS found mainly in epithelial cells. (lookformedical.com)
- Because beta-defensins are salt-sensitive epithelial products, we looked for pulmonary beta-defensin expression. (lookformedical.com)
Plant defensins6
- Plant defensins were discovered in 1990 and have subsequently been found in most plant tissues with antimicrobial activities, with both antifungal and antibacterial examples. (wikipedia.org)
- Plant defensins also have been tested as biotechnological tools to improve crop production through fungi resistance generation in organisms genetically modified (OGM). (frontiersin.org)
- Herein, is a review of the history of plant defensins since their discovery at the beginning of 90s, following the advances on its structure conformation and mechanism of action towards microorganisms is reported. (frontiersin.org)
- Plant defensins exhibit a conserved tertiary structure that consists of a triple-stranded antiparallel β-sheet and one α-helix that are stabilized into a compact shape by the disulfide bridges. (frontiersin.org)
- Despite the low level of amino acid sequence identity between defensins, their three dimensional structures are remarkably similar between different plant defensins ( Pelegrini and Franco, 2005 ). (frontiersin.org)
- Improving the Digestibility of Plant Defensins to Meet Regulatory Requirements for Transgene Products in Crop Protection. (edu.au)
Genes8
- In all families, the underlying genes responsible for defensin production are highly polymorphic. (wikipedia.org)
- In general, both α- and β-defensins are encoded by two-exon genes, where the first exon encodes for a hydrophobic leader sequence (removed after translation) and the cysteine-rich sequence (the mature peptide). (wikipedia.org)
- The activation of the TLRs and the NF- κ B pathway is responsible for the induction of the expression of antimicrobial peptide genes, including beta-defensins. (vin.com)
- Molecular cloning and characterization of rat genes encoding homologues of human beta-defensins. (lookformedical.com)
- Here, we report the identification of two genes encoding beta-defensin homologues in the rat. (lookformedical.com)
- The beta-defensin genes mapped closely on rat chromosome 16 and were closely linked to the alpha-defensins genes, suggesting that they are part of a gene cluster, similar to the organization reported for humans. (lookformedical.com)
- Defensin genes reside in complex genomic regions that are prone to structural variations and some defensin family members exhibit copy number variation (CNV). (le.ac.uk)
- We genotyped avian β-defensin (AvBD) genes in contemporary (2000-2008) and museum samples (1876-1940) of the Seychelles warbler to investigate whether immunogenetic variation was lost through this bottleneck, and examined AvBD variation across four other Acrocephalus species with varying demographic histories. (uea.ac.uk)
Beta-Defensin Expression1
- To test whether beta-defensin expression was inducible, gingival keratinocyte cell cultures were treated with interleukin-1beta (IL-1beta) or bacterial lipopolysaccharide (LPS) for 24 h. (lookformedical.com)
HBD23
- Human beta defensins (HBD)1, HBD2, and HBD3 are key elements of innate immunity that are secreted to neutralize/control the progression of infection. (biomedcentral.com)
- This study aimed to determine human -defensin 2 (hBD2) and LL-37 levels and compare between post-infectious BO patients and the control group. (bezmialem.edu.tr)
- We found that HBD3 binds to immobilized rHagB and produces a significantly higher resonance unit signal in surface plasmon resonance spectroscopic analysis, than HBD2 and HBD1 that are used as control defensins. (elsevierpure.com)
Role of defensins1
- The role of defensins in the preformed defense of plants is well reported. (frontiersin.org)
Pattern of disulphide1
- On the basis of their size and pattern of disulphide bonding, mammalian defensins are classified into alpha, beta and theta categories. (eaglebio.com)
Enzyme-linke2
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Defensin Beta 1 (DEFb1) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids. (jsce-ip.com)
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Defensin Beta 1 (DEFb1) in samples from Serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids with no significant corss-reactivity with analogues from other species. (jsce-ip.com)
Secretion1
- In the present work, we evaluated the secretion of human β-defensin-2 (hBD-2) by enterocytes after infection with P. fluorescens (a species previously suggested to be involved in inflammatory bowel disease) and investigated the effect of this host-defense peptide on the bacterial virulence. (pasteur.fr)
Cathelicidin1
- An investigation of human beta-defensins and cathelicidin expression in patients with pterygium. (antikoerper-online.de)
Human13
- Human papillomavirus oncogenic E6 protein regulates human β-defensin 3 (hBD3) expression via the tumor suppressor protein p53. (antikoerper-online.de)
- The human gene has been cloned by Jia et al (2001) who referred to it as HBD-3 and reported induction of defensin-beta-3 in fetal lung tissue by IL1-beta . (copewithcytokines.org)
- Two human beta-defensins, HBD-1 and HBD-2, were discovered in 1995 and 1997, respectively. (lookformedical.com)
- Human beta-defensins may play an important role in the innate defenses against oral microorganisms. (lookformedical.com)
- One gene was highly similar to the human beta-defensin-1 (HBD-1) gene and mouse beta-defensin-1 gene at both the nucleic acid and amino acid levels and was termed rat beta-defensin-1 (RBD-1). (lookformedical.com)
- Now, human beta-defensin-4, hBD-4 , was recently proposed based on the cDNA sequence analysis and the precursor sequence of which is composed of 72 amino acid residues. (peptanova.de)
- Background and Objective: Human beta-defensins (hBDs) contribute to innate immunity antimicrobial activity. (unesp.br)
- In the present study, we examined the protective effects of two AMPs, human neutrophil peptide-3 and α-defensin-5, against the opportunistic pathogen Enterococcus faecalis (E. faecalis). (elsevierpure.com)
- The Eagle Biosciences beta Defensin-2 ELISA assay kit is intended for the quantification of Human BD-2 / beta Defensin-2 in serum, plasma, cell culture supernatants The beta Defensin-2 ELISA assay kit is for research use only and should not be used for diagnostic procedures. (eaglebio.com)
- Description: A sandwich quantitative ELISA assay kit for detection of Human Defensin Beta 1 (DEFb1) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids. (jsce-ip.com)
- Structure Determination of Human and Murine Beta-Defensins Reveals Structural Conservation in the Absence of Significant Sequence Similarity. (expasy.org)
- Background: Yogic stretching (asana) has been proven to have an effect on salivary human beta-defensin-2 (HBD-2) concentration, which is an antimicrobial peptide and is an inflammatory marker in periodontal disease. (virginia.edu)
- Here, we asked whether human β-defensin 3 (HBD3) serves as an upstream suppressor of cytokine signaling that binds and attenuates pro-inflammatory cytokine responses to recombinant hemagglutinin B (rHagB), a non-fimbrial adhesin from Porphyromonas gingivalis strain 381. (elsevierpure.com)
Peptide3
- The antimicrobial peptide, β-defensin-1, has antiviral activity against both enveloped and non-enveloped viruses. (cdc.gov)
- Defensins are a type of peptide. (lesliebaumannmd.com)
- This patented formula also helps to improve the shelf life of defensins - another common problem among other topical peptide formulations. (lesliebaumannmd.com)
MRNA expression2
- β-defensin-1 mRNA expression has been identified in the heart of mice (murine beta-defensin-1, mBD1), pig (porcine beta-defensin-1, pBD1), and horse (equine beta-defensin-1, eBD1). (vin.com)
- Defensin mRNA expression was quantitated by RNase protection assays. (lookformedical.com)
Mammalian2
- Every mammalian species explored thus far has beta-defensins. (eaglebio.com)
- Mammalian defensins are small molecules (18-45 residues) that are cysteine, arginine rich compounds. (sciencecentral.in)
Disulfide1
- They are classified into alpha-, beta-, and theta-defensins based on their sizes and intramolecular disulfide bond patterns. (rndsystems.com)
Cysteine-rich1
- β-defensins are structurally defined by the conserved cysteine-rich motif forming three disulphide bonds, which stabilize a β-sheet formation. (vin.com)
Theta2
- Theta defensins form a single beta-hairpin structure and represent a distinct group. (wikipedia.org)
- According to their structural differences, defensins are classified in three major groups: alpha (α), beta (β), and theta (θ). (biomedcentral.com)
DEFB12
- In addition, Ingenuity Pathway Analysis (IPA) integrated with PCR array data showed that the JAK1/STAT3 pathway was significantly altered by cells overexpressing DEFB1 , suggesting that this may be one of the pathways by which defensin regulates IAV replication in HBEpCs. (cdc.gov)
- In conclusion, the reduction in IAV copy number in DEFB1 overexpressing cells suggests that β-defensin-1 plays a key role in regulating IAV survival through STAT3 and is a potential target for antiviral drug development. (cdc.gov)
Found in mammals1
- Defensins found in mammals belong to mainly two subfamilies α- and β-defensins. (sciencecentral.in)
Antimicrobial activities1
- We reported that anti-HIV and antimicrobial activities of native defensins is increased significantly by adding Arg (RR) residues at both the termini while the substitution of Arg (RR) with Asp (DD), eliminate anti-HIV and antimicrobial activity against all bacterial species tested. (sciencecentral.in)
Adaptive immunity1
- β-defensin 3 expression is stimulated by IFN-γ and is an important molecule during adaptive immunity. (mayflowerbio.com)
Mucosal1
- Defensins are a family of endogenous antibiotics that are important in mucosal innate immunity, but little is currently known about defensin expression in the nasal cavity. (auburn.edu)
Characteristic2
- The predicted prepropeptides were strongly cationic, were 69 and 63 residues in length for RBD-1 and RBD-2, respectively, and contained the six-cysteine motif characteristic of beta-defensins. (lookformedical.com)
- The deduced protein sequence contains 124 amino acids with a molecular weight of 13.5 kDa, showing characteristic motifs of the big defensin family and presenting 76% identity with the big defensin from the scallop A. irradians. (pucv.cl)
Protein4
- Other invertebrates known to produce defensins from this protein superfamily include molluscs, annelids and cnidaria. (wikipedia.org)
- aa 24 - 64) also known as defensin beta 2 (DEFB-2), is a secreted, 41 amino acid residue anti-microbial protein belonging to the defensin family. (rndsystems.com)
- Members of the defensin family are highly similar in protein sequence. (antikoerper-online.de)
- This is the first time that a big defensin is detected and located at the protein level in a mollusk. (pucv.cl)
AMPs1
- Although AMPs often neutralize bacterial bioactive products, neither α-defensin reduced the proteolytic activity of GelE, a toxic protease from E. faecalis. (elsevierpure.com)
Fungal1
- Fungal defensins were first identified in 2005. (wikipedia.org)
Cytokines1
- Defensins are produced constitutively and/or in response to microbial products or proinflammatory cytokines. (eaglebio.com)
Infection3
- Synovasure® Alpha Defensin Lateral Flow Test Kit for the assessment of periprosthetic joint infection. (healthtechnology.wales)
- The use of Synovasure® alpha defensin testing shows promise in the diagnosis of peri-prosthetic hip and knee infection but the evidence does not currently support routine adoption. (healthtechnology.wales)
- HTW assessed the Synovasure ® Alpha Defensin Test to help decide whether it should be made available to NHS Wales for diagnosing Periprosthetic Joint Infection. (healthtechnology.wales)
Species4
- More recently, however, β-defensins have also been identified in the heart of different species. (vin.com)
- Both beta-defensins and their signaling molecules, Toll-Like Receptors, have been identified in the heart of various species. (vin.com)
- They have been isolated in several species, and in humans, two beta-defensins have been identified. (lookformedical.com)
- In parallel with their role in immunity, in other species, defensins have evolved alternative functions, including the control of coat color in dogs. (le.ac.uk)
Vertebrate1
- citation needed] Vertebrate defensins are primarily α-defensins and β-defensins. (wikipedia.org)
Neutrophil1
- An organism usually produces many different defensins, some of which are stored inside the cells (e.g. in neutrophil granulocytes to kill phagocytosed bacteria), and others are secreted into the extracellular medium. (wikipedia.org)
Family3
- Although the most well-studied defensins are from vertebrates, a family of trans-defensins called 'big defensins' are found in molluscs, arthropods and lancelets. (wikipedia.org)
- Structural variations have mediated, and continue to influence, the diversification and expression of defensin family members. (le.ac.uk)
- At present, only two members of the big defensin family have been identified in scallop. (pucv.cl)
Defense2
- How Can Defensins have a Role in Plant Defense? (frontiersin.org)
- β-defensins exert host defense responses against viruses, bacteria, and fungi through the binding and permeabilizing of microbial membranes. (mayflowerbio.com)
Products4
- and (iv) a brief discussion about the absence of products in the market containing plant antifungal defensins. (frontiersin.org)
- beta-Defensin 2 " has 2 results in Products. (rndsystems.com)
- Learn more about what defensins are, how they work, and which products currently contain these novel anti-aging ingredients. (lesliebaumannmd.com)
- Which Products Contain Defensins? (lesliebaumannmd.com)
Pathway1
- To our knowledge, this is the only pathway which has been described as a route for β-defensin production. (vin.com)
Alpha3
- Only alpha and beta-defensins are expressed in humans. (wikipedia.org)
- This topic was referred to HTW by the manufacturer of the Synovasure® alpha defensin test (Zimmer Biomet). (healthtechnology.wales)
- PJI is difficult to diagnose and the use of the Synovasure® alpha defensin test may improve detection rates and ultimately result in more appropriate patient management. (healthtechnology.wales)
Immune3
- In vertebrates, some α- and β-defensins are involved in signalling between the innate immune and adaptive immune systems. (wikipedia.org)
- Several reports show that defensins are an integral part of the plant innate immune system. (frontiersin.org)
- Aberrant expression of defensins is important in a number of inflammatory diseases as well as modulating host immune responses to bacteria, unicellular pathogens, and viruses. (le.ac.uk)
Insect1
- Indeed, an insect defensin has been experimentally converted into a toxin by deletion of a small loop that otherwise sterically hindered interactions with the ion channels. (wikipedia.org)
Murine1
- Murine β-defensin 14 expression mirrors that of cBD103 in the dog, with high expression in the nares and tongue, but has little to no expression in the RE, OE or OB. (auburn.edu)
Bacterial1
- Bacterial defensins have also been identified, but are by far the least studied. (wikipedia.org)
Cysteines1
- They include variants with only four cysteines, whereas defensins from eukaryote defensins almost all have six or eight. (wikipedia.org)
Nasal1
- Exploring Pleiotropic Functions of Canine β-Defensin 103: Nasal Cavity Expression, Antimicrobial Activity, and Melanocortin Receptor Activity. (antikoerper-online.de)
Sequence1
- In the present work, a cDNA sequence encoding a new big defensin homologue was characterized from the scallop Argopecten purpuratus, namely ApBD1. (pucv.cl)
Locus1
- This review highlights the work currently being done to better understand the genomic architecture of the β-defensin locus. (le.ac.uk)
Expression1
- Herein expression of canine β-defensin (cBD)1, cBD103, cBD108 and cBD123 RNA in the respiratory epithelium (RE), cBD1 and 108 RNA in the olfactory epithelium (OE), and cBD1, cBD108, cBD119 and cBD123 RNA in the olfactory bulb (OB) is reported. (auburn.edu)
