Collectins
Pulmonary Surfactant-Associated Protein D
Pulmonary Surfactant-Associated Protein A
Serum Globulins
Pulmonary Surfactant-Associated Proteins
Pulmonary Surfactants
Mannose-Binding Lectin
Proteolipids
Lectins
Complement C1q
Opsonin Proteins
Hemagglutination
Macrophages, Alveolar
Influenza A virus
Hemagglutination Inhibition Tests
Glycoproteins
Monosaccharides
Carbohydrates
Phagocytosis
Lung
Mycobacterium avium
Carrier Proteins
Immunity, Innate
Surface Plasmon Resonance
Respiratory Mucosa
Glycosylation
Two constituents of the initiation complex of the mannan-binding lectin activation pathway of complement are encoded by a single structural gene. (1/252)
Mannan-binding lectin (MBL) forms a multimolecular complex with at least two MBL-associated serine proteases, MASP-1 and MASP-2. This complex initiates the MBL pathway of complement activation by binding to carbohydrate structures present on bacteria, yeast, and viruses. MASP-1 and MASP-2 are composed of modular structural motifs similar to those of the C1q-associated serine proteases C1r and C1s. Another protein of 19 kDa with the same N-terminal sequence as the 76-kDa MASP-2 protein is consistently detected as part of the MBL/MASP complex. In this study, we present the primary structure of this novel MBL-associated plasma protein of 19 kDa, MAp19, and demonstrate that MAp19 and MASP-2 are encoded by two different mRNA species generated by alternative splicing/polyadenylation from one structural gene. (+info)C1qRP is a heavily O-glycosylated cell surface protein involved in the regulation of phagocytic activity. (2/252)
C1q, mannose-binding lectin (MBL), and pulmonary surfactant protein A (SPA) interact with human monocytes and macrophages, resulting in the enhancement of phagocytosis of suboptimally opsonized targets. mAbs that recognize a cell surface molecule of 126,000 Mr, designated C1qRP, have been shown to inhibit C1q- and MBL-mediated enhancement of phagocytosis. Similar inhibition of the SPA-mediated enhancement of phagocytosis by these mAbs now suggests that C1qRP is a common component of a receptor for these macromolecules. Ligation of human monocytes with immobilized R3, a IgM mAb recognizing C1qRP, also triggers enhanced phagocytic capacity of these cells in the absence of ligand, verifying the direct involvement of this polypeptide in the regulation of phagocytosis. While the cDNA for C1qRP encodes a 631 amino acid membrane protein, Chinese hamster ovary cells transfected with the cDNA of the C1qRP coding region express a surface glycoprotein with the identical 126,000 Mr in SDS-PAGE as the native C1qRP. Use of glycosylation inhibitors, cleavage of the mature C1qRP with specific glycosidases, and in vitro translation of C1qRP cDNA demonstrated that both posttranslational glycosylation and the nature of the amino acid sequence of the protein contribute to the difference between its predicted m.w. and its migration on SDS-PAGE. These results verify that the cDNA cloned codes for the mature C1qRP, that C1qRP contains a relatively high degree of O-linked glycoslyation, and that C1qRP cross-linked directly by monoclonal anti-C1qRP or engaged as a result of cell surface ligation of SPA, as well as C1q and MBL, enhances phagocytosis. (+info)KM+, a mannose-binding lectin from Artocarpus integrifolia: amino acid sequence, predicted tertiary structure, carbohydrate recognition, and analysis of the beta-prism fold. (3/252)
The complete amino acid sequence of the lectin KM+ from Artocarpus integrifolia (jackfruit), which contains 149 residues/mol, is reported and compared to those of other members of the Moraceae family, particularly that of jacalin, also from jackfruit, with which it shares 52% sequence identity. KM+ presents an acetyl-blocked N-terminus and is not posttranslationally modified by proteolytic cleavage as is the case for jacalin. Rather, it possesses a short, glycine-rich linker that unites the regions homologous to the alpha- and beta-chains of jacalin. The results of homology modeling implicate the linker sequence in sterically impeding rotation of the side chain of Asp141 within the binding site pocket. As a consequence, the aspartic acid is locked into a conformation adequate only for the recognition of equatorial hydroxyl groups on the C4 epimeric center (alpha-D-mannose, alpha-D-glucose, and their derivatives). In contrast, the internal cleavage of the jacalin chain permits free rotation of the homologous aspartic acid, rendering it capable of accepting hydrogen bonds from both possible hydroxyl configurations on C4. We suggest that, together with direct recognition of epimeric hydroxyls and the steric exclusion of disfavored ligands, conformational restriction of the lectin should be considered to be a new mechanism by which selectivity may be built into carbohydrate binding sites. Jacalin and KM+ adopt the beta-prism fold already observed in two unrelated protein families. Despite presenting little or no sequence similarity, an analysis of the beta-prism reveals a canonical feature repeatedly present in all such structures, which is based on six largely hydrophobic residues within a beta-hairpin containing two classic-type beta-bulges. We suggest the term beta-prism motif to describe this feature. (+info)Molecular cloning of a novel human collectin from liver (CL-L1). (4/252)
Collectins are a C-lectin family with collagen-like sequences and carbohydrate recognition domains. These proteins can bind to carbohydrate antigens of microorganisms and inhibit their infection by direct neutralization and agglutination, the activation of complement through the lectin pathway, and opsonization by collectin receptors. Here we report the cloning of a cDNA encoding human collectin from liver (CL-L1 (collectin liver 1)) that has typical collectin structural characteristics, consisting of an N-terminal cysteine-rich domain, a collagen-like domain, a neck domain, and a carbohydrate recognition domain. The cDNA has an insert of 831 base pairs coding for a protein of 277 amino acid residues. The deduced amino acid sequence shows that this collectin has a unique repeat of four lysine residues in its C-terminal area. Northern blot, Western blot, and reverse transcription-polymerase chain reaction analyses showed that CL-L1 is present mainly in liver as a cytosolic protein and at low levels in placenta. More sensitive analyses by reverse transcription-polymerase chain reactions showed that most tissues (except skeletal muscle) have CL-L1 mRNA. Zoo-blot analysis indicated that CL-L1 is limited to mammals and birds. A chromosomal localization study indicated that the CL-L1 gene localizes to chromosome 8q23-q24.1, different from chromosome 10 of other human collectin genes. Expression studies of fusion proteins lacking the collagen and N-terminal domains produced in Escherichia coli affirmed that CL-L1 binds mannose weakly. CL-L1 and recombinant CL-L1 fusion proteins do not bind to mannan columns. Analysis of the phylogenetic tree of CL-L1 and other collectins indicated that CL-L1 belongs to a fourth subfamily of collectins following the mannan-binding protein, surfactant protein A, and surfactant protein D subfamilies including bovine conglutinin and collectin-43 (CL-43). These findings indicate that CL-L1 may be involved in different biological functions. (+info)Isolation, characterization, molecular cloning and molecular modelling of two lectins of different specificities from bluebell (Scilla campanulata) bulbs. (5/252)
Two lectins have been isolated from bluebell (Scilla campanulata) bulbs. From their isolation by affinity chromatography, they are characterized as a mannose-binding lectin (SCAman) and a fetuin-binding lectin (SCAfet). SCAman preferentially binds oligosaccharides with alpha(1,3)- and alpha(1,6)-linked mannopyranosides. It is a tetramer of four identical protomers of approx. 13 kDa containing 119 amino acid residues; it is not glycosylated. The fetuin-binding lectin (SCAfet), which is not inhibited by any simple sugars, is also unglycosylated. It is a tetramer of four identical subunits of approx. 28 kDa containing 244 residues. Each 28 kDa subunit is composed of two 14 kDa domains. Both lectins have been cloned from a cDNA library and sequenced. X-ray crystallographic analysis and molecular modelling studies have demonstrated close relationships in sequence and structure between these lectins and other monocot mannose-binding lectins. A refined model of the molecular evolution of the monocot mannose-binding lectins is proposed. (+info)Glomerular deposition of mannose-binding lectin in human glomerulonephritis. (6/252)
BACKGROUND: Mannose-binding lectin (MBL), a member of the collectin family, binds to various oligosaccharides and activates the classical pathway of complement independent from C1q. At present it is unknown whether this so-called lectin pathway of complement activation plays a role in the pathogenesis of human glomerulonephritis. METHODS: Direct immunofluorescence of 84 renal biopsies using an MBL-specific monoclonal antibody and antibodies directed against IgG, IgA, IgM, C1q, C3, and terminal complement complex (TCC) was performed. Serum MBL levels of 50 patients were determined by enzyme-linked immunosorbent assay. RESULTS: MBL was detected in the glomeruli of patients with lupus nephropathy (15 of 16), membranous nephropathy (10/15), membranoproliferative glomerulonephritis type I (5/6) and anti-GBM nephritis (2/4). MBL deposition paralleled that of immunoglobulins, C1q, C3, and TCC but was less intense as compared to C1q. Focal segmental deposits of MBL were present in focal segmental glomerulosclerosis (4/6), IgA nephropathy (3/11), amyloidosis AL (1/4), and advanced renal fibrosis (2/2). Here MBL staining was identical to IgM and C3 and considered an unspecific entrapment of MBL in sclerotic lesions in these cases. No significant difference in MBL serum levels was observed between normal controls and patients with lupus nephritis, membranous nephropathy, membranoproliferative glomerulonephritis, focal segmental sclerosis, minimal change disease or IgA nephropathy. In patients suffering from membranous nephropathy with (n=10) or without (n=5) glomerular MBL deposits serum creatinine, C3, C4, serum protein, and proteinuria were not statistically different. CONCLUSION: MBL is present in the glomeruli of patients with glomerulonephritis involving deposition of IgG and activation of the classical pathway of complement. We propose that MBL binds to agalactosyl oligosaccharides of IgG that terminate in N-acetylglucosamine. The extent to which the lectin pathway of complement contributes to overall complement activation in the glomeruli remains unknown, but is likely to be marginal. (+info)The significance of IgG subclasses and mannan-binding lectin (MBL) for susceptibility to infection in apparently healthy adults with IgA deficiency. (7/252)
The aim of this study was to investigate the significance of IgG subclasses and MBL for susceptibility to infection in association with IgA deficiency. The study population consisted of 139 apparently healthy adult blood donors with IgA deficiency and normal serum levels of IgG and IgM, and an increased susceptibility to infection demonstrated at a population level. Additionally, 216 controls matched for age and sex were investigated. IgG4 deficiency was more common and the mean level of IgG4 lower in persons with IgA deficiency than in the controls. No significant associations could be demonstrated between overt IgG subclass deficiencies and increased susceptibility to infection. However, when the mean concentrations of IgG subclasses were analysed with regard to medical history, that of IgG1 was lower in persons who reported recurrent viral respiratory infections, that of IgG3 in persons who had episodes of severe infection in their history, and that of IgG4 in persons who had recurrent mild respiratory infections, compared with those who had no particular history of infections. In contrast, MBL deficiency-alone or combined with that of the IgG subclass-was not associated with increased susceptibility to infection in persons with IgA deficiency. The results indicate that the proneness to infections observed in a population of otherwise healthy persons with IgA deficiency can only for a small part be accounted for by concomitant deficiencies of IgG subclasses. Contrary to expectations, no synergism between the deficiencies of IgA and MBL could be demonstrated. (+info)Antibody-independent classical complement pathway activation and homologous C3 deposition in xeroderma pigmentosum cell lines. (8/252)
Of human malignantly transformed cell lines, xeroderma pigmentosum (XP) cell lines were found to be highly susceptible to homologous complement (C): cells were opsonized by C3 fragments on incubation with diluted normal human serum. C3 fragment deposition on XP cells was Ca2+-dependent and occurred on live cells but not UV-irradiated apoptotic cells. (Ca2+ is required for activation of the classical C pathway via C1q and the lactin pathway via mannose binding lectin (MBL), and the surface of apoptotic cells usually activates the alternative C pathway.) In this study we tested which of the pathways participates in XP cell C3 deposition. In seven cell lines that allowed C3 deposition (i), Clq was shown to be essential but MBL played no role in C activation, (ii) Cls but not MASP bound XP cells for activation, (iii) no antibodies recognizing XP cells were required for homologous C3 deposition, and (iv) the alternative pathway barely participated in C3 deposition. Furthermore, the levels of C-regulatory proteins for host cell protection against C, decay-accelerating factor (DAF, CD55) and membrane cofactor protein (MCP, CD46), were found to be relatively low in almost all XP cell lines compared with normal cells. These results indicate that XP cells activate the classical C pathway in an antibody-independent manner through the expression of a molecule which directly attracts C1q in a C-activating form, and that relatively low levels of DAF and MCP on XP cells facilitate effective C3 deposition. The possible relationship between the pathogenesis of XP and our findings is discussed. (+info)Collectins are a family of proteins that are part of the innate immune system. They are found in the extracellular fluid, including the blood, and are involved in the recognition and clearance of pathogens, such as bacteria and viruses. Collectins are characterized by their ability to bind to carbohydrates on the surface of microorganisms, which helps to aggregate them and facilitate their clearance by immune cells. There are several different types of collectins, including mannose-binding lectin (MBL), surfactant protein D (SP-D), and collectin-11 (CL-11). Collectins play an important role in the body's defense against infection and are also involved in the regulation of inflammation.
Pulmonary Surfactant-Associated Protein D (SP-D) is a protein that plays a crucial role in the function of the lungs. It is a member of the collectin family of proteins, which are involved in the immune system's response to pathogens and the regulation of inflammation. SP-D is synthesized and secreted by type II alveolar cells in the lungs, and it is present in high concentrations in the surfactant layer that covers the surface of the alveoli. This layer helps to reduce surface tension and prevent the alveoli from collapsing during exhalation. SP-D has several functions in the lungs. One of its main roles is to recognize and bind to pathogens, such as bacteria and viruses, and to promote their clearance from the lungs. It also plays a role in regulating the immune response to these pathogens by modulating the activity of immune cells. In addition to its immune functions, SP-D has been shown to have anti-inflammatory effects in the lungs. It can help to reduce the production of pro-inflammatory molecules and to promote the resolution of inflammation. SP-D deficiency has been associated with several lung diseases, including chronic obstructive pulmonary disease (COPD), asthma, and idiopathic pulmonary fibrosis. It is also a potential biomarker for these conditions, as levels of SP-D in the blood or airways can be used to diagnose and monitor the progression of these diseases.
Pulmonary Surfactant-Associated Protein A (SP-A) is a protein that plays a crucial role in the function of the lungs. It is a member of the collectin family of proteins, which are involved in the innate immune system and the clearance of pathogens and debris from the lungs. SP-A is synthesized and secreted by type II alveolar cells, which are specialized cells in the lungs that produce and secrete pulmonary surfactant. Pulmonary surfactant is a complex mixture of lipids and proteins that helps to reduce surface tension in the alveoli, allowing them to expand and contract properly during breathing. SP-A functions by binding to and aggregating phospholipids and other molecules in the airways and alveoli, forming a protective layer that helps to prevent the accumulation of excess fluid and debris. It also plays a role in the clearance of pathogens and other foreign substances from the lungs. Abnormalities in SP-A levels or function have been associated with a number of lung diseases, including acute respiratory distress syndrome (ARDS), chronic obstructive pulmonary disease (COPD), and idiopathic pulmonary fibrosis (IPF).
Serum globulins are a group of proteins found in the blood plasma that are responsible for various functions in the body. They are classified into four main categories: albumin, alpha globulins, beta globulins, and gamma globulins. Albumin is the most abundant serum protein, accounting for about 50-60% of total serum protein. It plays a crucial role in maintaining the osmotic pressure of the blood, transporting hormones and fatty acids, and serving as a reservoir for various substances. Alpha globulins are a diverse group of proteins that include haptoglobin, alpha-1 acid glycoprotein, and alpha-2 macroglobulin. They play a role in the immune system, as well as in the transport and metabolism of various substances. Beta globulins include transferrin, which transports iron in the blood, and haptoglobin, which binds to free hemoglobin and helps to remove it from the bloodstream. Gamma globulins, also known as immunoglobulins, are the most diverse group of serum proteins and are responsible for the immune response. They are produced by B cells in response to foreign substances and are involved in the destruction of pathogens and the production of antibodies. Abnormal levels of serum globulins can indicate various medical conditions, such as liver disease, kidney disease, or certain types of cancer.
Pulmonary surfactant-associated proteins (PSAPs) are a group of proteins that are synthesized and secreted by type II alveolar cells in the lungs. These proteins play a crucial role in maintaining the surface tension of the alveoli, which helps to keep the lungs inflated and prevent them from collapsing. PSAPs are composed of two main types of proteins: surfactant protein A (SP-A) and surfactant protein D (SP-D). SP-A is a small, globular protein that binds to a variety of pathogens and helps to clear them from the lungs. SP-D is a larger, multi-domain protein that binds to lipids and carbohydrates, and has been shown to have antiviral and anti-inflammatory properties. In addition to SP-A and SP-D, PSAPs also include surfactant protein B (SP-B) and surfactant protein C (SP-C). SP-B is a small, hydrophobic protein that helps to stabilize the structure of the surfactant film, while SP-C is a hydrophobic protein that helps to regulate the surface tension of the alveoli. Disruptions in the production or function of PSAPs can lead to a variety of lung diseases, including respiratory distress syndrome (RDS), chronic obstructive pulmonary disease (COPD), and idiopathic pulmonary fibrosis (IPF).
Mannose-binding lectin (MBL) is a protein that plays a role in the innate immune system. It is produced by the liver and circulates in the blood, where it binds to specific carbohydrate structures on the surface of microorganisms, such as bacteria and viruses. This binding triggers a series of immune responses, including the activation of complement proteins and the recruitment of immune cells to the site of infection. MBL is also involved in the clearance of damaged or apoptotic cells from the body. Deficiencies in MBL can increase the risk of infections and autoimmune diseases.
Proteolipids are a type of lipid-protein complex that are found in the cell membrane of many organisms, including animals, plants, and bacteria. They are composed of a hydrophobic lipid tail and a hydrophilic protein head, which allows them to interact with both the interior and exterior of the cell membrane. In the medical field, proteolipids are of particular interest because they play important roles in the function of the nervous system. For example, proteolipids are a major component of the myelin sheath, which is a layer of fatty substance that surrounds and insulates nerve fibers. The myelin sheath helps to speed up the transmission of nerve impulses and is essential for normal brain function. Proteolipids are also involved in the development and maintenance of the blood-brain barrier, which is a barrier that separates the circulating blood from the brain and spinal cord. This barrier helps to protect the brain from harmful substances in the blood and maintain a stable environment for nerve cells. In addition to their roles in the nervous system, proteolipids have also been implicated in a number of other medical conditions, including multiple sclerosis, Alzheimer's disease, and Parkinson's disease.
Mannans are a type of polysaccharide, which are complex carbohydrates made up of long chains of sugar molecules. In the medical field, mannans are often used as a dietary supplement or as an ingredient in certain medications. Mannans are found in many foods, including fruits, vegetables, and grains, but they are also produced by certain types of fungi and bacteria. Some studies have suggested that mannans may have immune-boosting properties and may be beneficial for people with certain health conditions, such as allergies, autoimmune disorders, and cancer. In the medical field, mannans are sometimes used as an ingredient in dietary supplements or as an active ingredient in certain medications. For example, some dietary supplements contain mannan-chitosan complexes, which are believed to help reduce cholesterol levels and improve digestion. Mannans are also used in some medications to treat certain types of infections, such as fungal infections of the skin and nails. It's important to note that while mannans may have potential health benefits, more research is needed to fully understand their effects on the body. As with any dietary supplement or medication, it's important to talk to a healthcare provider before starting to take mannans or any other supplement or medication.
Lectins are a class of proteins that are found in many plants, animals, and microorganisms. They are characterized by their ability to bind to specific carbohydrates, such as sugars and starches, on the surface of cells. In the medical field, lectins have been studied for their potential therapeutic applications. For example, some lectins have been shown to have antiviral, antibacterial, and antifungal properties, and may be useful in the development of new drugs to treat infections. Lectins have also been used as research tools to study cell-cell interactions and to identify specific cell surface markers. In addition, some lectins have been used in diagnostic tests to detect specific diseases or conditions, such as cancer or diabetes. However, it is important to note that not all lectins are safe or effective for medical use, and some may even be toxic. Therefore, the use of lectins in medicine requires careful consideration and testing to ensure their safety and efficacy.
Complement C1q is a protein that plays a central role in the complement system, which is a part of the immune system that helps to defend the body against infections and other harmful substances. C1q is a component of the C1 complex, which is the first step in the activation of the complement system. When C1q binds to a pathogen or damaged cell, it triggers a cascade of events that leads to the destruction of the pathogen or cell by the immune system. C1q is also involved in the regulation of the complement system, helping to prevent overactivation and damage to healthy cells.
Opsonin proteins are a type of immune system protein that play a role in the process of phagocytosis, which is the process by which immune cells called phagocytes engulf and destroy foreign particles, such as bacteria or viruses. Opsonins bind to the surface of these foreign particles, marking them for destruction by phagocytes. This process is known as opsonization. There are several different types of opsonin proteins, including antibodies, complement proteins, and mannose-binding lectin (MBL). Antibodies are proteins produced by the immune system in response to the presence of a foreign substance, such as a virus or bacteria. They bind to specific molecules on the surface of these foreign particles, marking them for destruction by phagocytes. Complement proteins are a group of proteins that are part of the innate immune system. They are produced by the liver and other organs and circulate in the blood. Complement proteins can bind to foreign particles and mark them for destruction by phagocytes. MBL is a protein that is produced by the liver and circulates in the blood. It binds to specific molecules on the surface of foreign particles, marking them for destruction by phagocytes. Opsonin proteins play an important role in the immune system by helping to identify and destroy foreign particles. They are an important part of the body's defense against infection and disease.
Glycoproteins are a type of protein that contains one or more carbohydrate chains covalently attached to the protein molecule. These carbohydrate chains are made up of sugars and are often referred to as glycans. Glycoproteins play important roles in many biological processes, including cell signaling, cell adhesion, and immune response. They are found in many different types of cells and tissues throughout the body, and are often used as markers for various diseases and conditions. In the medical field, glycoproteins are often studied as potential targets for the development of new drugs and therapies.
Monosaccharides are the simplest form of carbohydrates, consisting of a single sugar unit. They are the building blocks of more complex carbohydrates, such as disaccharides and polysaccharides. In the medical field, monosaccharides are important sources of energy for the body. They are broken down during cellular respiration to produce ATP, which is the primary source of energy for the body's cells. Monosaccharides are also used in the production of glycogen, which is a storage form of glucose in the liver and muscles. When blood glucose levels are low, glycogen can be broken down to release glucose into the bloodstream to maintain normal blood sugar levels. In addition, monosaccharides are used in the production of various types of carbohydrates, such as starches, fibers, and glycoproteins. They are also important components of many types of food, including fruits, vegetables, and dairy products. Overall, monosaccharides play a crucial role in maintaining normal bodily functions and are an important part of a healthy diet.
In the medical field, carbohydrates are one of the three macronutrients that provide energy to the body. They are made up of carbon, hydrogen, and oxygen atoms and are found in foods such as grains, fruits, vegetables, and dairy products. Carbohydrates are broken down into glucose (a simple sugar) during digestion and are then transported to cells throughout the body to be used as energy. The body can store excess glucose as glycogen in the liver and muscles for later use. There are two main types of carbohydrates: simple and complex. Simple carbohydrates, also known as sugars, are made up of one or two sugar molecules and are quickly digested and absorbed by the body. Complex carbohydrates, on the other hand, are made up of many sugar molecules and take longer to digest and absorb. In the medical field, carbohydrates are often discussed in the context of nutrition and diabetes management. People with diabetes need to carefully monitor their carbohydrate intake to help manage their blood sugar levels.
In the medical field, carrier proteins are proteins that transport molecules across cell membranes or within cells. These proteins bind to specific molecules, such as hormones, nutrients, or waste products, and facilitate their movement across the membrane or within the cell. Carrier proteins play a crucial role in maintaining the proper balance of molecules within cells and between cells. They are involved in a wide range of physiological processes, including nutrient absorption, hormone regulation, and waste elimination. There are several types of carrier proteins, including facilitated diffusion carriers, active transport carriers, and ion channels. Each type of carrier protein has a specific function and mechanism of action. Understanding the role of carrier proteins in the body is important for diagnosing and treating various medical conditions, such as genetic disorders, metabolic disorders, and neurological disorders.
Recombinant proteins are proteins that are produced by genetically engineering bacteria, yeast, or other organisms to express a specific gene. These proteins are typically used in medical research and drug development because they can be produced in large quantities and are often more pure and consistent than proteins that are extracted from natural sources. Recombinant proteins can be used for a variety of purposes in medicine, including as diagnostic tools, therapeutic agents, and research tools. For example, recombinant versions of human proteins such as insulin, growth hormones, and clotting factors are used to treat a variety of medical conditions. Recombinant proteins can also be used to study the function of specific genes and proteins, which can help researchers understand the underlying causes of diseases and develop new treatments.
Collectin
Collectin-12
Collectin-10
Collectin of 46 kDa
Collectin of 43 kDa
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Pulmonary collectins3
- It is currently discussed that adult and infant patients suffering from diseases associated with lung infection may benefit from the anti-inflammatory and antimicrobial properties of the pulmonary collectins. (fz-borstel.de)
- Our group is investigating the functions and mechanisms of immune cells that are involved in the specific ability of pulmonary collectins to carry out immunomodulations that are important for preventing infection and inflammation. (fz-borstel.de)
- A better understanding of collectin-mediated lung immunity will contribute to the identification of disease states in which the therapeutic administration of pulmonary collectins may be beneficial. (fz-borstel.de)
Mannan-bindin1
- Nine types of collectins have been defined: MBL = mannan-binding lectin (mannose-binding lectin) SP-A = surfactant protein A SP-D = surfactant protein D CL-L1 = collectin liver 1 CL-P1 = collectin placenta 1 CL-43 = Collectin of 43 kDa CL-46 = collectin of 46 kDa CL-K1 = collectin kidney 1 Conglutinin CL-43, CL-46 and conglutinin are found in bovine. (wikipedia.org)
Microbial2
- Binding of collectins to microorganisms may trigger elimination of microorganisms by aggregation, complement activation, opsonization, activation of phagocytosis, or inhibition of microbial growth. (wikipedia.org)
- SP-A-deficient mice have an enhanced susceptibility to infection to pulmonary infection with bacterial and fungal pathogens and collectin replacement in these animals corrects defects in dysregulated cellular functions and microbial clearance. (fz-borstel.de)
Phagocytosis1
- Articles on Collectins, Defensins, Phagocytosis. (bvsalud.org)
Lectin3
- Collectins are linked with activation of lectin pathway of complement activation. (wikipedia.org)
- Collectin MBL is involved in activation of the lectin complement pathway. (wikipedia.org)
- Collectin subfamily member 10 (C-type lectin). (cdc.gov)
Inflammation1
- Collectins SP-A and SP-D have anti-allergic effects: they inhibit IgE binding to allergens, decrease histamine release from basophils, and inhibit T-lymphocyte production in the late phase of the inflammation. (wikipedia.org)
Lung1
- The data on the role of lung collectins in immunomodulation are compelling, but the intracellular events by which they exert anti-inflammatory effects on activated immune cells are only partially understood. (fz-borstel.de)
Immune3
- Collectins (collagen-containing C-type lectins) are a part of the innate immune system. (wikipedia.org)
- Other functions of collectins are modulation of inflammatory, allergic responses, adaptive immune system and clearance of apoptotic cells. (wikipedia.org)
- The immune surfactant or collectin surfactant protein D (SP-D) is a crucial multifunctional innate immune receptor. (cdc.gov)
Ability1
- The Give A Little App comes pre-installed on the CollecTin More and gives donors the ability to choose from up to six donation amounts and also the option to choose their own amount. (collectin.com)
Specific1
- There is a specific interaction between collectins and receptors on phagocytic cells which can lead to increased clearance of microorganisms. (wikipedia.org)
Effect2
- Collectins have effect on microorganism survival. (wikipedia.org)
- Little work to date has examined the effect of such collectins in response to organic dusts. (cdc.gov)
Price1
- The kapaa collectin offers contemporary shag rugs at an affordable price. (thingzcontemporary.com)
Clearance1
- Collectins SP-A and SP-D enhance clearance of apoptotic cells by macrophages. (wikipedia.org)
Surfactant proteins2
- The pulmonary collectins, surfactant proteins A (SP-A) and D (SP-D), have been reported to bind lipopolysaccharide (LPS), opsonize microorganisms, and enhance the clearance of lung pathogens. (nih.gov)
- SP-A and SP-D are hydrophilic surfactant proteins and are members of the collectin family. (novusbio.com)
Subfamily member2
- Collectin subfamily member 10 (C-type lectin). (cdc.gov)
- collectin subfamily member. (gsea-msigdb.org)
Trimers3
- Functionally collectins are trimers. (wikipedia.org)
- In general, collectins form higher-order multimers through disulfide bonding between trimers at the N-terminus. (medscape.com)
- Collectins form trimers that may assemble into larger oligomers. (bvsalud.org)
Lectins1
- Collectins (collagen-containing C-type lectins) are a part of the innate immune system. (wikipedia.org)
Placenta1
- These "novel collectins" consist of collectin liver 1 (CL-L1), collectin kidney 1 (CL-K1), and collectin placenta 1 (CL-P1) and are encoded by three separate genes. (nih.gov)
Immunity2
- Experimental findings on human and animal collectins have shown that both novel collectins and classical collectins play an important role in innate immunity. (nih.gov)
- The first evidence of the role of collectins in immunity against influenza virus was the observation that mammalian serum β-inhibitors of the virus are collectins. (medscape.com)
Microorganisms3
- Collectins can bind to the surface of microorganisms and between carbohydrate ligands. (wikipedia.org)
- There is a specific interaction between collectins and receptors on phagocytic cells which can lead to increased clearance of microorganisms. (wikipedia.org)
- Binding of collectins to microorganisms results in their agglutination and enhanced clearance. (bvsalud.org)
Gene1
- Deletion of the E. coli OmpA gene from a collectin-resistant smooth E. coli strain enhanced SP-A and SP-D-mediated growth inhibition. (nih.gov)
Influenza4
- [ 10 ] Our laboratory has studied the interactions of collectins with influenza virus extensively so we will provide a fairly comprehensive discussion of their antiviral activities. (medscape.com)
- Collectins bind to and directly neutralize influenza virus. (medscape.com)
- [ 13 ] The collectins appear to play important roles in restricting influenza replication in the early phase of infection and in preventing excessive inflammation. (medscape.com)
- 16. Inhibition of influenza viral neuraminidase activity by collectins. (nih.gov)
Inflammatory2
- Other functions of collectins are modulation of inflammatory, allergic responses, adaptive immune system and clearance of apoptotic cells. (wikipedia.org)
- Collectins also bind to inflammatory cells and can modulate activation of these cells, resulting in either an increase or decrease in activation. (medscape.com)
Complement1
- The Role of Complement Activating Collectins and Associated Serine Proteases in Patients With Hematological Malignancies, Receiving High-Dose Chemotherapy, and Autologous Hematopoietic Stem Cell Transplantations (Auto-HSCT). (cdc.gov)
Binding3
- At the beginning, there is a binding of collectin to PAMPs or DAMPs. (wikipedia.org)
- Each collectin polypeptide chain consists of four regions: a relatively short N-terminal region, a collagen-like region, an alpha-helical coiled-coil region, and carbohydrate-binding region. (bvsalud.org)
- Circulating glycoproteins such as alpha-fetoprotein, alpha-2-macroglobulin, galectin-3-binding protein, and collectin-10 show association to failing heart and CRT treatment model. (nih.gov)
Inhibition1
- In general, rough E. coli strains were more susceptible than smooth strains, and collectin-mediated growth inhibition was partially blocked by coincubation with rough LPS vesicles. (nih.gov)
Innate1
- The immune surfactant or collectin surfactant protein D (SP-D) is a crucial multifunctional innate immune receptor. (cdc.gov)
Molecular1
- C1q is a glycoprotein that belongs to the collectin family, having a molecular weight of about 410-462 kDa. (prospecbio.com)
Role1
- In addition to learning about how the virus infects lung cells, this PA specifically encourages in vitro research on the role of lung collectins and other extracellular lung host factors. (nih.gov)
Cells1
- Collectins SP-A and SP-D enhance clearance of apoptotic cells by macrophages. (wikipedia.org)
Functions1
- Based on our recent results and those of others, in this paper, we summarize the new biological functions of these novel collectins in embryonic morphogenesis and development. (nih.gov)
Important1
- [ 11 , 12 ] The basic structural unit of collectins is a trimer composed of a disulfide containing a N-terminus, a structurally important collagen domain, a trimerizing neck domain and a carbohydrate-recognition domain (CRD) that mediates attachment to carbohydrates. (medscape.com)