Complement System Proteins
Phosphatidylethanolamine Binding Protein
Complement Membrane Attack Complex
Complement Inactivator Proteins
Complement C3-C5 Convertases
Complement Factor B
Complement Pathway, Alternative
Complement Pathway, Classical
Complement C1 Inactivator Proteins
Receptors, Complement 3b
Complement Factor H
Receptor, Anaphylatoxin C5a
Complement Activating Enzymes
Complement Inactivating Agents
Complement Hemolytic Activity Assay
Molecular Sequence Data
Receptors, Complement 3d
Amino Acid Sequence
Complement Fixation Tests
Complement Factor D
Complement C1 Inhibitor Protein
Complement Factor I
Complement C4b-Binding Protein
Complement C3b Inactivator Proteins
Complement C3-C5 Convertases, Classical Pathway
Electrophoresis, Polyacrylamide Gel
Complement C3-C5 Convertases, Alternative Pathway
Complement C3 Convertase, Alternative Pathway
Complement C5 Convertase, Classical Pathway
Sequence Homology, Amino Acid
Complement C3 Convertase, Classical Pathway
I-kappa B Proteins
Lupus Erythematosus, Systemic
Complement C5 Convertase, Alternative Pathway
Protein Structure, Tertiary
Complement Pathway, Mannose-Binding Lectin
Mitochondrial Proton-Translocating ATPases
Complement C5a, des-Arginine
Intracellular Signaling Peptides and Proteins
Cholesterol Ester Transfer Proteins
Gene Expression Regulation
Protein Phosphatase 1
Genetic Complementation Test
Enzyme-Linked Immunosorbent Assay
Cyclin-Dependent Kinase Inhibitor p21
Polymerase Chain Reaction
Major Histocompatibility Complex
Proto-Oncogene Proteins c-raf
Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone
Inhibitor of Apoptosis Proteins
Reverse Transcriptase Polymerase Chain Reaction
Recombinant Fusion Proteins
Disease Models, Animal
Blood Bactericidal Activity
Complement C3 Nephritic Factor
Cyclin-Dependent Kinase Inhibitor p27
Dose-Response Relationship, Drug
C1-Esterase inhibitor: an anti-inflammatory agent and its potential use in the treatment of diseases other than hereditary angioedema. (1/83)C1-esterase inhibitor (C1-Inh) therapy was introduced in clinical medicine about 25 years ago as a replacement therapy for patients with hereditary angioedema caused by a deficiency of C1-Inh. There is now accumulating evidence, obtained from studies in animals and observations in patients, that administration of C1-Inh may have a beneficial effect as well in other clinical conditions such as sepsis, cytokine-induced vascular leak syndrome, acute myocardial infarction, or other diseases. Activation of the complement system, the contact activation system, and the coagulation system has been observed in these diseases. A typical feature of the contact and complement system is that on activation they give rise to vasoactive peptides such as bradykinin or the anaphylatoxins, which in part explains the proinflammatory effects of either system. C1-Inh, belonging to the superfamily of serine proteinase inhibitors (serpins), is a major inhibitor of the classical complement pathway, the contact activation system, and the intrinsic pathway of coagulation, respectively. It is, therefore, endowed with anti-inflammatory properties. However, inactivation of C1-Inh occurs locally in inflamed tissues by proteolytic enzymes (e.g., elastase) released from activated neutrophils or bacteria thereby leading to increased local activation of the various host defense systems. Here we will give an overview on the biochemistry and biology of C1-Inh. We will discuss studies addressing therapeutic administration of C1-Inh in experimental and clinical conditions. Finally, we will provide an explanation for the therapeutic benefit of C1-Inh in so many different diseases. (+info)
C1 inhibitor cross-linking by tissue transglutaminase. (2/83)C1 inhibitor, a plasma proteinase inhibitor of the serpin superfamily involved in the regulation of complement classical pathway and intrinsic blood coagulation, has been shown to bind to several components of the extracellular matrix. These reactions may be responsible for C1 inhibitor localization in the perivascular space. In the study reported here, we have examined whether C1 inhibitor could function as a substrate for plasma (factor XIIIa) or tissue transglutaminase. We made the following observations: 1) SDS-polyacrylamide gel electrophoresis and autoradiography showed that C1 inhibitor exposed to tissue transglutaminase (but not to factor XIIIa) incorporated the radioactive amine donor substrate [(3)H]putrescine in a calcium-dependent manner; 2) the maximum stoichiometry for the uptake of [(3)H]putrescine by C1 inhibitor was 1:1; 3) proteolytic cleavage and peptide sequencing of reduced and carboxymethylated [(3)H]putrescine-C1 inhibitor identified Gln(453) (P'9) as the single amine acceptor residue; 4) studies with (125)I-labeled C1 inhibitor showed that tissue transglutaminase was also able to cross-link C1 inhibitor to immobilized fibrin; and 5) C1 inhibitor cross-linked by tissue transglutaminase to immobilized fibrin had inhibitory activity against its target enzymes. Thus, tissue transglutaminase-mediated cross-linking of C1 inhibitor to fibrin or other extracellular matrix components may serve as a mechanism for covalent serpin binding and influence local regulation of the proteolytic pathways inhibited by C1 inhibitor. (+info)
SERPIN regulation of factor XIa. The novel observation that protease nexin 1 in the presence of heparin is a more potent inhibitor of factor XIa than C1 inhibitor. (3/83)In the present studies we have made the novel observation that protease nexin 1 (PN1), a member of the serine protease inhibitor (SERPIN) superfamily, is a potent inhibitor of the blood coagulation Factor XIa (FXIa). The inhibitory complexes formed between PN1 and FXIa are stable when subjected to reducing agents, SDS, and boiling, a characteristic of the acyl linkage formed between SERPINs and their cognate proteases. Using a sensitive fluorescence-quenched peptide substrate, the K(assoc) of PN1 for FXIa was determined to be 7.9 x 10(4) m(-)(1) s(-)(1) in the absence of heparin. In the presence of heparin, this rate was accelerated to 1.7 x 10(6), M(-)(1) s(-)(1), making PN1 a far better inhibitor of FXIa than C1 inhibitor, which is the only other SERPIN known to significantly inhibit FXIa. FXIa-PN1 complexes are shown to be internalized and degraded by human fibroblasts, most likely via the low density lipoprotein receptor-related protein (LRP), since degradation was strongly inhibited by the LRP agonist, receptor-associated protein. Since FXIa proteolytically modifies the amyloid precursor protein, this observation may suggest an accessory role for PN1 in the pathobiogenesis of Alzheimer's disease. (+info)
The native metastable fold of C1-inhibitor is stabilized by disulfide bonds. (4/83)C1-inhibitor is a member of the serpin family of proteinase inhibitors and is an important inhibitor of complement and contact system proteinases. The native protein has the characteristic serpin feature of being in a kinetically trapped metastable state rather than in the most stable state it could adopt. A consequence of this is that it readily forms loop-sheet dimers and polymers, by a mechanism believed to be the same as observed with other serpins. An unusual feature of C1-inhibitor is that it has a unique amino-terminal domain, of unknown function, held to the serpin domain by two disulfide bonds not found in other serpins. We report here that reduction of these bonds by DTT, causes a conformational change such that the reactive center loop inserts into beta-sheet A. This form of C1-inhibitor is less stable to heat and urea than the native protein, and is more susceptible to extensive degradation by trypsin. These data show that the disulfide bonds in C1-inhibitor are required for the protein to be stabilized in the metastable state with the reactive center loop expelled from beta-sheet A. (+info)
Hereditary angioedema with a de novo mutation of exon 8 in the C1 inhibitor gene showing recurrent edema of the hands around the peripheral joints: importance for the differential diagnosis of joint swelling. (5/83)We describe a patient with hereditary angioedema (HAE), showing recurrent edema around the peripheral joints. Her symptoms began at the age of 18 with hand swelling distal to the wrist joints. Until she was referred to our hospital 3 years after her initial symptoms, she was still undiagnosed, although she was suspected of having rheumatoid arthritis. Laboratory examination showed reduced levels of CH50 and C4 with normal C3 levels. The C1 inhibitor (C1-INH) was decreased to 5 mg/ml, with remarkably reduced activity. Although these findings were compatible with a diagnosis of HAE, there were no episodes of skin edema in her family. To establish the diagnosis, we carried out DNA analysis of the C1-INH gene, which revealed a newly identified de novo mutation of G to A at nucleotide 16869 in exon 8. As described in this patient, localized edema around the peripheral joints may be the only manifestation of HAE. HAE should therefore be taken into consideration for the differential diagnosis of joint swelling. (+info)
Complement components, but not complement inhibitors, are upregulated in atherosclerotic plaques. (6/83)Complement activation occurs in atherosclerotic plaques. The capacity of arterial tissue to inhibit this activation through generation of the complement regulators C1 inhibitor, decay accelerating factor, membrane cofactor protein (CD46), C4 binding protein (C4BP), and protectin (CD59) was evaluated in pairs of aortic atherosclerotic plaques and nearby normal artery from 11 human postmortem specimens. All 22 samples produced mRNAs for each of these proteins. The ratios of plaque versus normal artery pairs was not significantly different from unity for any of these inhibitors. However, in plaques, the mRNAs for C1r and C1s, the substrates for the C1 inhibitor, were increased 2.35- and 4.96-fold, respectively, compared with normal artery; mRNA for C4, the target for C4BP, was elevated l.34-fold; and mRNAs for C7 and C8, the targets for CD59, were elevated 2.61- and 3.25-fold, respectively. By Western blotting and immunohistochemistry, fraction Bb of factor B, a marker of alternative pathway activation, was barely detectable in plaque and normal arterial tissue. These data indicate that it is primarily the classical, not the alternative pathway, that is activated in plaques and that key inhibitors are not upregulated to defend against this activation. (+info)
A new type of acquired C1 inhibitor deficiency associated with systemic lupus erythematosus. (7/83)Acquired C1 inhibitor (C1-INH) deficiency with consequent angioedema is a rare condition that may indicate an underlying lymphoproliferative disorder. The defect is caused by increased catabolism, which is often associated with the presence of serum autoantibodies to C1-INH. The present report describes 3 patients with systemic lupus erythematosus who developed typical symptoms of acquired angioedema, characterized by recurrent swelling of subcutaneous and mucous tissues. The 3 patients demonstrated a major classical pathway-mediated complement consumption, with very low levels of C3 antigen and decreased levels of C1-INH antigen. Neither antibodies to C1-INH nor associated lymphoproliferative disease was found. No patient had clinical and biologic signs of lupus activity at the time the angioedema occurred. All patients were treated with steroids and exhibited a good response, without relapse of angioedema and with normalization of plasma levels of C1-INH. In lupus patients who present with an angioedema syndrome, acquired or hereditary angioedema must be sought by examining parameters of the classical pathway and levels of C1-INH. Our observations suggest the existence of a new form of acquired C1-INH deficiency associated with a major classical pathway-mediated complement consumption and systemic autoimmunity. (+info)
In vivo biosynthesis of endogenous and of human C1 inhibitor in transgenic mice: tissue distribution and colocalization of their expression. (8/83)We have produced transgenic mice expressing human C1 inhibitor mRNA and protein under the control of the human promoter and regulatory elements. The transgene was generated using a minigene construct in which most of the human C1 inhibitor gene (C1NH) was replaced by C1 inhibitor cDNA. The construct retained the promoter region extending 1.18 kb upstream of the transcription start site, introns 1 and 2 as well as a stretch of 2.5 kb downstream of the polyadenylation site, and therefore carried all known elements involved in transcriptional regulation of the C1NH gene. Mice with high serum levels of human C1 inhibitor, resulting from multiple tandem integrations of the C1 inhibitor transgene, were selected. Immunohistochemistry in combination with in situ hybridization was applied to localize the sites of C1 inhibitor biosynthesis and to demonstrate its local production in brain, spleen, liver, heart, kidney, and lung. The distribution of human C1 inhibitor-expressing cells was qualitatively indistinguishable from that of its mouse counterpart, but expression levels of the transgene were significantly higher. In the spleen, production of C1 inhibitor was colocalized with that of a specific marker for white pulp follicular dendritic cells. This study demonstrates a stringently regulated expression of both the endogenous and the transgenic human C1 inhibitor gene and reveals local biosynthesis of C1 inhibitor at multiple sites in which the components of the macromolecular C1 complex are also produced. (+info)
Acute angioedema is usually triggered by an allergic reaction or exposure to certain medications, such as nonsteroidal anti-inflammatory drugs (NSAIDs), blood pressure medications, or antibiotics. It can also be caused by infections, insect bites, and other environmental triggers.
Chronic angioedema, on the other hand, is a more persistent form of the condition that can last for weeks, months, or even years. It is often associated with conditions such as hereditary angioedema (HAE), which is caused by a genetic defect that affects the production of a protein called C1 esterase inhibitor.
The symptoms of angioedema can vary depending on the location and severity of the swelling, but they typically include:
* Swelling in the face, hands, feet, or other parts of the body
* Redness and warmth of the affected area
* Pain or discomfort
* Difficulty breathing or swallowing (in severe cases)
There is no cure for angioedema, but there are several treatments available to help manage the symptoms. These may include:
* Antihistamines or corticosteroids to reduce inflammation and relieve itching
* Ice packs or cool compresses to reduce swelling
* Compression stockings or bandages to prevent fluid buildup
* Pain relief medications, such as ibuprofen or acetaminophen, to manage discomfort
In severe cases of angioedema, hospitalization may be necessary to provide more intensive treatment and monitoring. In some cases, injectable medications such as epinephrine or corticosteroids may be administered to help reduce swelling and prevent complications.
Overall, angioedema is a serious condition that requires prompt medical attention to manage symptoms and prevent complications. If you suspect you or someone else may have angioedema, it is important to seek medical help right away.
There are two main types of hemolysis:
1. Intravascular hemolysis: This type occurs within the blood vessels and is caused by factors such as mechanical injury, oxidative stress, and certain infections.
2. Extravascular hemolysis: This type occurs outside the blood vessels and is caused by factors such as bone marrow disorders, splenic rupture, and certain medications.
Hemolytic anemia is a condition that occurs when there is excessive hemolysis of RBCs, leading to a decrease in the number of healthy red blood cells in the body. This can cause symptoms such as fatigue, weakness, pale skin, and shortness of breath.
Some common causes of hemolysis include:
1. Genetic disorders such as sickle cell anemia and thalassemia.
2. Autoimmune disorders such as autoimmune hemolytic anemia (AIHA).
3. Infections such as malaria, babesiosis, and toxoplasmosis.
4. Medications such as antibiotics, nonsteroidal anti-inflammatory drugs (NSAIDs), and blood thinners.
5. Bone marrow disorders such as aplastic anemia and myelofibrosis.
6. Splenic rupture or surgical removal of the spleen.
7. Mechanical injury to the blood vessels.
Diagnosis of hemolysis is based on a combination of physical examination, medical history, and laboratory tests such as complete blood count (CBC), blood smear examination, and direct Coombs test. Treatment depends on the underlying cause and may include supportive care, blood transfusions, and medications to suppress the immune system or prevent infection.
The term "systemic" refers to the fact that the disease affects multiple organ systems, including the skin, joints, kidneys, lungs, and nervous system. LES is a complex condition, and its symptoms can vary widely depending on which organs are affected. Common symptoms include fatigue, fever, joint pain, rashes, and swelling in the extremities.
There are several subtypes of LES, including:
1. Systemic lupus erythematosus (SLE): This is the most common form of the disease, and it can affect anyone, regardless of age or gender.
2. Discoid lupus erythematosus (DLE): This subtype typically affects the skin, causing a red, scaly rash that does not go away.
3. Drug-induced lupus erythematosus: This form of the disease is caused by certain medications, and it usually resolves once the medication is stopped.
4. Neonatal lupus erythematosus: This rare condition affects newborn babies of mothers with SLE, and it can cause liver and heart problems.
There is no cure for LES, but treatment options are available to manage the symptoms and prevent flares. Treatment may include nonsteroidal anti-inflammatory drugs (NSAIDs), corticosteroids, immunosuppressive medications, and antimalarial drugs. In severe cases, hospitalization may be necessary to monitor and treat the disease.
It is important for people with LES to work closely with their healthcare providers to manage their condition and prevent complications. With proper treatment and self-care, many people with LES can lead active and fulfilling lives.
Idiopathic membranous nephropathy (IMN) is an autoimmune disorder that causes GNM without any identifiable cause. Secondary membranous nephropathy, on the other hand, is caused by systemic diseases such as lupus or cancer.
The symptoms of GNM can vary depending on the severity of the disease and may include blood in the urine, proteinuria, edema, high blood pressure, and decreased kidney function. The diagnosis of GNM is based on a combination of clinical findings, laboratory tests, and renal biopsy.
Treatment for GNM is aimed at slowing the progression of the disease and managing symptoms. Medications such as corticosteroids, immunosuppressive drugs, and blood pressure-lowering drugs may be used to treat GNM. In some cases, kidney transplantation may be necessary.
The prognosis for GNM varies depending on the severity of the disease and the underlying cause. In general, the prognosis for IMN is better than for secondary membranous nephropathy. With proper treatment, some patients with GNM can experience a slowing or stabilization of the disease, while others may progress to end-stage renal disease (ESRD).
The cause of GNM is not fully understood, but it is believed to be an autoimmune disorder that leads to inflammation and damage to the glomerular membrane. Genetic factors and environmental triggers may also play a role in the development of GNM.
There are several risk factors for developing GNM, including family history, age (GMN is more common in adults), and certain medical conditions such as hypertension and diabetes.
The main complications of GNM include:
1. ESRD: Progression to ESRD is a common outcome of untreated GNM.
2. High blood pressure: GNM can lead to high blood pressure, which can further damage the kidneys.
3. Infections: GNM increases the risk of infections due to impaired immune function.
4. Kidney failure: GNM can cause chronic kidney failure, leading to the need for dialysis or a kidney transplant.
5. Cardiovascular disease: GNM is associated with an increased risk of cardiovascular disease, including heart attack and stroke.
6. Malnutrition: GNM can lead to malnutrition due to decreased appetite, nausea, and vomiting.
7. Bone disease: GNM can cause bone disease, including osteoporosis and bone pain.
8. Anemia: GNM can cause anemia, which can lead to fatigue, weakness, and shortness of breath.
9. Increased risk of infections: GNM increases the risk of infections due to impaired immune function.
10. Decreased quality of life: GNM can significantly decrease a person's quality of life, leading to decreased mobility, pain, and discomfort.
It is important for individuals with GNM to receive early diagnosis and appropriate treatment to prevent or delay the progression of these complications.
The symptoms of glomerulonephritis can vary depending on the underlying cause of the disease, but may include:
* Blood in the urine (hematuria)
* Proteinuria (excess protein in the urine)
* Reduced kidney function
* Swelling in the legs and ankles (edema)
* High blood pressure
Glomerulonephritis can be caused by a variety of factors, including:
* Infections such as staphylococcal or streptococcal infections
* Autoimmune disorders such as lupus or rheumatoid arthritis
* Allergic reactions to certain medications
* Genetic defects
* Certain diseases such as diabetes, high blood pressure, and sickle cell anemia
The diagnosis of glomerulonephritis typically involves a physical examination, medical history, and laboratory tests such as urinalysis, blood tests, and kidney biopsy.
Treatment for glomerulonephritis depends on the underlying cause of the disease and may include:
* Antibiotics to treat infections
* Medications to reduce inflammation and swelling
* Diuretics to reduce fluid buildup in the body
* Immunosuppressive medications to suppress the immune system in cases of autoimmune disorders
* Dialysis in severe cases
The prognosis for glomerulonephritis depends on the underlying cause of the disease and the severity of the inflammation. In some cases, the disease may progress to end-stage renal disease, which requires dialysis or a kidney transplant. With proper treatment, however, many people with glomerulonephritis can experience a good outcome and maintain their kidney function over time.
Arteriolosclerosis is often associated with conditions such as hypertension, diabetes, and atherosclerosis, which is the buildup of plaque in the arteries. It can also be caused by other factors such as smoking, high cholesterol levels, and inflammation.
The symptoms of arteriolosclerosis can vary depending on the location and severity of the condition, but may include:
* Decreased blood flow to organs or tissues
* Shortness of breath
* Dizziness or lightheadedness
* Pain in the affected limbs or organs
Arteriolosclerosis is typically diagnosed through a combination of physical examination, medical history, and diagnostic tests such as ultrasound, angiography, or blood tests. Treatment for the condition may include lifestyle changes such as exercise and dietary modifications, medications to control risk factors such as hypertension and high cholesterol, and in some cases, surgical intervention to open or bypass blocked arterioles.
In summary, arteriolosclerosis is a condition where the arterioles become narrowed or obstructed, leading to decreased blood flow to organs and tissues and potentially causing a range of health problems. It is often associated with other conditions such as hypertension and atherosclerosis, and can be diagnosed through a combination of physical examination, medical history, and diagnostic tests. Treatment may include lifestyle changes and medications to control risk factors, as well as surgical intervention in some cases.
1) They share similarities with humans: Many animal species share similar biological and physiological characteristics with humans, making them useful for studying human diseases. For example, mice and rats are often used to study diseases such as diabetes, heart disease, and cancer because they have similar metabolic and cardiovascular systems to humans.
2) They can be genetically manipulated: Animal disease models can be genetically engineered to develop specific diseases or to model human genetic disorders. This allows researchers to study the progression of the disease and test potential treatments in a controlled environment.
3) They can be used to test drugs and therapies: Before new drugs or therapies are tested in humans, they are often first tested in animal models of disease. This allows researchers to assess the safety and efficacy of the treatment before moving on to human clinical trials.
4) They can provide insights into disease mechanisms: Studying disease models in animals can provide valuable insights into the underlying mechanisms of a particular disease. This information can then be used to develop new treatments or improve existing ones.
5) Reduces the need for human testing: Using animal disease models reduces the need for human testing, which can be time-consuming, expensive, and ethically challenging. However, it is important to note that animal models are not perfect substitutes for human subjects, and results obtained from animal studies may not always translate to humans.
6) They can be used to study infectious diseases: Animal disease models can be used to study infectious diseases such as HIV, TB, and malaria. These models allow researchers to understand how the disease is transmitted, how it progresses, and how it responds to treatment.
7) They can be used to study complex diseases: Animal disease models can be used to study complex diseases such as cancer, diabetes, and heart disease. These models allow researchers to understand the underlying mechanisms of the disease and test potential treatments.
8) They are cost-effective: Animal disease models are often less expensive than human clinical trials, making them a cost-effective way to conduct research.
9) They can be used to study drug delivery: Animal disease models can be used to study drug delivery and pharmacokinetics, which is important for developing new drugs and drug delivery systems.
10) They can be used to study aging: Animal disease models can be used to study the aging process and age-related diseases such as Alzheimer's and Parkinson's. This allows researchers to understand how aging contributes to disease and develop potential treatments.
There are several types of lupus nephritis, each with its own unique characteristics and symptoms. The most common forms include:
* Class I (mesangial proliferative glomerulonephritis): This type is characterized by the growth of abnormal cells in the glomeruli (blood-filtering units of the kidneys).
* Class II (active lupus nephritis): This type is characterized by widespread inflammation and damage to the kidneys, with or without the presence of antibodies.
* Class III (focal lupus nephritis): This type is characterized by localized inflammation in certain areas of the kidneys.
* Class IV (lupus nephritis with crescentic glomerulonephritis): This type is characterized by widespread inflammation and damage to the kidneys, with crescent-shaped tissue growth in the glomeruli.
* Class V (lupus nephritis with sclerotic changes): This type is characterized by hardening and shrinkage of the glomeruli due to scarring.
Lupus Nephritis can cause a range of symptoms, including:
* Proteinuria (excess protein in the urine)
* Hematuria (blood in the urine)
* Reduced kidney function
* Swelling (edema)
* Joint pain
Lupus Nephritis can be diagnosed through a combination of physical examination, medical history, laboratory tests, and kidney biopsy. Treatment options for lupus nephritis include medications to suppress the immune system, control inflammation, and prevent further damage to the kidneys. In severe cases, dialysis or a kidney transplant may be necessary.
There are several key features of inflammation:
1. Increased blood flow: Blood vessels in the affected area dilate, allowing more blood to flow into the tissue and bringing with it immune cells, nutrients, and other signaling molecules.
2. Leukocyte migration: White blood cells, such as neutrophils and monocytes, migrate towards the site of inflammation in response to chemical signals.
3. Release of mediators: Inflammatory mediators, such as cytokines and chemokines, are released by immune cells and other cells in the affected tissue. These molecules help to coordinate the immune response and attract more immune cells to the site of inflammation.
4. Activation of immune cells: Immune cells, such as macrophages and T cells, become activated and start to phagocytose (engulf) pathogens or damaged tissue.
5. Increased heat production: Inflammation can cause an increase in metabolic activity in the affected tissue, leading to increased heat production.
6. Redness and swelling: Increased blood flow and leakiness of blood vessels can cause redness and swelling in the affected area.
7. Pain: Inflammation can cause pain through the activation of nociceptors (pain-sensing neurons) and the release of pro-inflammatory mediators.
Inflammation can be acute or chronic. Acute inflammation is a short-term response to injury or infection, which helps to resolve the issue quickly. Chronic inflammation is a long-term response that can cause ongoing damage and diseases such as arthritis, asthma, and cancer.
There are several types of inflammation, including:
1. Acute inflammation: A short-term response to injury or infection.
2. Chronic inflammation: A long-term response that can cause ongoing damage and diseases.
3. Autoimmune inflammation: An inappropriate immune response against the body's own tissues.
4. Allergic inflammation: An immune response to a harmless substance, such as pollen or dust mites.
5. Parasitic inflammation: An immune response to parasites, such as worms or fungi.
6. Bacterial inflammation: An immune response to bacteria.
7. Viral inflammation: An immune response to viruses.
8. Fungal inflammation: An immune response to fungi.
There are several ways to reduce inflammation, including:
1. Medications such as nonsteroidal anti-inflammatory drugs (NSAIDs), corticosteroids, and disease-modifying anti-rheumatic drugs (DMARDs).
2. Lifestyle changes, such as a healthy diet, regular exercise, stress management, and getting enough sleep.
3. Alternative therapies, such as acupuncture, herbal supplements, and mind-body practices.
4. Addressing underlying conditions, such as hormonal imbalances, gut health issues, and chronic infections.
5. Using anti-inflammatory compounds found in certain foods, such as omega-3 fatty acids, turmeric, and ginger.
It's important to note that chronic inflammation can lead to a range of health problems, including:
3. Heart disease
5. Alzheimer's disease
6. Parkinson's disease
7. Autoimmune disorders, such as lupus and rheumatoid arthritis.
Therefore, it's important to manage inflammation effectively to prevent these complications and improve overall health and well-being.
There are three main forms of ACH:
1. Classic congenital adrenal hyperplasia (CAH): This is the most common form of ACH, accounting for about 90% of cases. It is caused by mutations in the CYP21 gene, which codes for an enzyme that converts cholesterol into cortisol and aldosterone.
2. Non-classic CAH (NCAH): This form of ACH is less common than classic CAH and is caused by mutations in other genes involved in cortisol and aldosterone production.
3. Mineralocorticoid excess (MOE) or glucocorticoid deficiency (GD): These are rare forms of ACH that are characterized by excessive production of mineralocorticoids (such as aldosterone) or a deficiency of glucocorticoids (such as cortisol).
The symptoms of ACH can vary depending on the specific form of the disorder and the age at which it is diagnosed. In classic CAH, symptoms typically appear in infancy and may include:
* Premature puberty (in girls) or delayed puberty (in boys)
* Abnormal growth patterns
* Distended abdomen
* Weight gain or obesity
* Easy bruising or bleeding
In NCAH and MOE/GD, symptoms may be less severe or may not appear until later in childhood or adulthood. They may include:
* High blood pressure
* Low blood sugar (hypoglycemia)
* Weight gain or obesity
* Mood changes
If left untreated, ACH can lead to serious complications, including:
* Adrenal gland insufficiency
* Heart problems
* Bone health problems
* Increased risk of infections
* Mental health issues (such as depression or anxiety)
Treatment for ACH typically involves hormone replacement therapy to restore the balance of hormones in the body. This may involve taking medications such as cortisol, aldosterone, or other hormones to replace those that are deficient or imbalanced. In some cases, surgery may be necessary to remove an adrenal tumor or to correct physical abnormalities.
With proper treatment, many individuals with ACH can lead healthy, active lives. However, it is important for individuals with ACH to work closely with their healthcare providers to manage their condition and prevent complications. This may involve regular check-ups, hormone level monitoring, and lifestyle changes such as a healthy diet and regular exercise.
Proteinuria is usually diagnosed by a urine protein-to-creatinine ratio (P/C ratio) or a 24-hour urine protein collection. The amount and duration of proteinuria can help distinguish between different underlying causes and predict prognosis.
Proteinuria can have significant clinical implications, as it is associated with increased risk of cardiovascular disease, kidney damage, and malnutrition. Treatment of the underlying cause can help reduce or eliminate proteinuria.
There are two main types of MD:
1. Dry Macular Degeneration (DMD): This is the most common form of MD, accounting for about 90% of cases. It is caused by the gradual accumulation of waste material in the macula, which can lead to cell death and vision loss over time.
2. Wet Macular Degeneration (WMD): This type of MD is less common but more aggressive, accounting for about 10% of cases. It occurs when new blood vessels grow underneath the retina, leaking fluid and causing damage to the macula. This can lead to rapid vision loss if left untreated.
The symptoms of MD can vary depending on the severity and type of the condition. Common symptoms include:
* Blurred vision
* Distorted vision (e.g., straight lines appearing wavy)
* Difficulty reading or recognizing faces
* Difficulty adjusting to bright light
* Blind spots in central vision
MD can have a significant impact on daily life, making it difficult to perform everyday tasks such as driving, reading, and recognizing faces.
There is currently no cure for MD, but there are several treatment options available to slow down the progression of the disease and manage its symptoms. These include:
* Anti-vascular endothelial growth factor (VEGF) injections: These medications can help prevent the growth of new blood vessels and reduce inflammation in the macula.
* Photodynamic therapy: This involves the use of a light-sensitive drug and low-intensity laser to damage and shrink the abnormal blood vessels in the macula.
* Vitamin supplements: Certain vitamins, such as vitamin C, E, and beta-carotene, have been shown to slow down the progression of MD.
* Laser surgery: This can be used to reduce the number of abnormal blood vessels in the macula and improve vision.
It is important for individuals with MD to receive regular monitoring and treatment from an eye care professional to manage their condition and prevent complications.
There are several types of disease susceptibility, including:
1. Genetic predisposition: This refers to the inherent tendency of an individual to develop a particular disease due to their genetic makeup. For example, some families may have a higher risk of developing certain diseases such as cancer or heart disease due to inherited genetic mutations.
2. Environmental susceptibility: This refers to the increased risk of developing a disease due to exposure to environmental factors such as pollutants, toxins, or infectious agents. For example, someone who lives in an area with high levels of air pollution may be more susceptible to developing respiratory problems.
3. Lifestyle susceptibility: This refers to the increased risk of developing a disease due to unhealthy lifestyle choices such as smoking, lack of exercise, or poor diet. For example, someone who smokes and is overweight may be more susceptible to developing heart disease or lung cancer.
4. Immune system susceptibility: This refers to the increased risk of developing a disease due to an impaired immune system. For example, people with autoimmune disorders such as HIV/AIDS or rheumatoid arthritis may be more susceptible to opportunistic infections.
Understanding disease susceptibility can help healthcare providers identify individuals who are at risk of developing certain diseases and provide preventive measures or early intervention to reduce the risk of disease progression. Additionally, genetic testing can help identify individuals with a high risk of developing certain diseases, allowing for earlier diagnosis and treatment.
In summary, disease susceptibility refers to the predisposition of an individual to develop a particular disease or condition due to various factors such as genetics, environment, lifestyle choices, and immune system function. Understanding disease susceptibility can help healthcare providers identify individuals at risk and provide appropriate preventive measures or early intervention to reduce the risk of disease progression.
There are several symptoms of RA, including:
1. Joint pain and stiffness, especially in the hands and feet
2. Swollen and warm joints
3. Redness and tenderness in the affected areas
4. Fatigue, fever, and loss of appetite
5. Loss of range of motion in the affected joints
6. Firm bumps of tissue under the skin (rheumatoid nodules)
RA can be diagnosed through a combination of physical examination, medical history, blood tests, and imaging studies such as X-rays or ultrasound. Treatment typically involves a combination of medications, including nonsteroidal anti-inflammatory drugs (NSAIDs), disease-modifying anti-rheumatic drugs (DMARDs), and biologic agents. Lifestyle modifications such as exercise and physical therapy can also be helpful in managing symptoms and improving quality of life.
There is no cure for RA, but early diagnosis and aggressive treatment can help to slow the progression of the disease and reduce symptoms. With proper management, many people with RA are able to lead active and fulfilling lives.
Explanation: Genetic predisposition to disease is influenced by multiple factors, including the presence of inherited genetic mutations or variations, environmental factors, and lifestyle choices. The likelihood of developing a particular disease can be increased by inherited genetic mutations that affect the functioning of specific genes or biological pathways. For example, inherited mutations in the BRCA1 and BRCA2 genes increase the risk of developing breast and ovarian cancer.
The expression of genetic predisposition to disease can vary widely, and not all individuals with a genetic predisposition will develop the disease. Additionally, many factors can influence the likelihood of developing a particular disease, such as environmental exposures, lifestyle choices, and other health conditions.
Inheritance patterns: Genetic predisposition to disease can be inherited in an autosomal dominant, autosomal recessive, or multifactorial pattern, depending on the specific disease and the genetic mutations involved. Autosomal dominant inheritance means that a single copy of the mutated gene is enough to cause the disease, while autosomal recessive inheritance requires two copies of the mutated gene. Multifactorial inheritance involves multiple genes and environmental factors contributing to the development of the disease.
Examples of diseases with a known genetic predisposition:
1. Huntington's disease: An autosomal dominant disorder caused by an expansion of a CAG repeat in the Huntingtin gene, leading to progressive neurodegeneration and cognitive decline.
2. Cystic fibrosis: An autosomal recessive disorder caused by mutations in the CFTR gene, leading to respiratory and digestive problems.
3. BRCA1/2-related breast and ovarian cancer: An inherited increased risk of developing breast and ovarian cancer due to mutations in the BRCA1 or BRCA2 genes.
4. Sickle cell anemia: An autosomal recessive disorder caused by a point mutation in the HBB gene, leading to defective hemoglobin production and red blood cell sickling.
5. Type 1 diabetes: An autoimmune disease caused by a combination of genetic and environmental factors, including multiple genes in the HLA complex.
Understanding the genetic basis of disease can help with early detection, prevention, and treatment. For example, genetic testing can identify individuals who are at risk for certain diseases, allowing for earlier intervention and preventive measures. Additionally, understanding the genetic basis of a disease can inform the development of targeted therapies and personalized medicine."
The disorder is caused by mutations in the HBB gene that codes for the beta-globin subunit of hemoglobin. These mutations result in the production of abnormal hemoglobins that are unstable and prone to breakdown, leading to the release of free hemoglobin into the urine.
HP is classified into two types based on the severity of symptoms:
1. Type 1 HP: This is the most common form of the disorder and is characterized by mild to moderate anemia, occasional hemoglobinuria, and a normal life expectancy.
2. Type 2 HP: This is a more severe form of the disorder and is characterized by severe anemia, recurrent hemoglobinuria, and a shorter life expectancy.
There is no cure for HP, but treatment options are available to manage symptoms and prevent complications. These may include blood transfusions, folic acid supplements, and medications to reduce the frequency and severity of hemoglobinuria episodes.
The term "immune complex disease" was first used in the 1960s to describe a group of conditions that were thought to be caused by the formation of immune complexes. These diseases include:
1. Systemic lupus erythematosus (SLE): an autoimmune disorder that can affect multiple organ systems and is characterized by the presence of anti-nuclear antibodies.
2. Rheumatoid arthritis (RA): an autoimmune disease that causes inflammation in the joints and can lead to joint damage.
3. Type III hypersensitivity reaction: a condition in which immune complexes are deposited in tissues, leading to inflammation and tissue damage.
4. Pemphigus: a group of autoimmune diseases that affect the skin and mucous membranes, characterized by the presence of autoantibodies against desmosomal antigens.
5. Bullous pemphigoid: an autoimmune disease that affects the skin and is characterized by the formation of large blisters.
6. Myasthenia gravis: an autoimmune disorder that affects the nervous system, causing muscle weakness and fatigue.
7. Goodpasture's syndrome: a rare autoimmune disease that affects the kidneys and lungs, characterized by the presence of immune complexes in the glomeruli of the kidneys.
8. Hemolytic uremic syndrome (HUS): a condition in which red blood cells are destroyed and waste products accumulate in the kidneys, leading to kidney failure.
Immune complex diseases can be caused by various factors, including genetic predisposition, environmental triggers, and exposure to certain drugs or toxins. Treatment options for these diseases include medications that suppress the immune system, such as corticosteroids and immunosuppressive drugs, and plasmapheresis, which is a process that removes harmful antibodies from the blood. In some cases, organ transplantation may be necessary.
In conclusion, immune complex diseases are a group of disorders that occur when the body's immune system mistakenly attacks its own tissues and organs, leading to inflammation and damage. These diseases can affect various parts of the body, including the skin, kidneys, lungs, and nervous system. Treatment options vary depending on the specific disease and its severity, but may include medications that suppress the immune system and plasmapheresis.
List of proteins
Proteins produced and secreted by the liver
Classical complement pathway
List of primary immunodeficiencies
Complement component 1s
List of MeSH codes (D12.776.124)
Acquired C1 esterase inhibitor deficiency
Passive antibody therapy
Complement component 1r
Outline of immunology
List of MeSH codes (D12.776)
List of skin conditions
List of OMIM disorder codes
Timeline of senescence research
Browsing by Subject "Complement C1 Inhibitor Protein"
Complement regulatory protein C1 inhibitor binds to selectins and interferes with endothelial-leukocyte adhesion. | J Immunol...
Subjects: Complement C1 Inhibitor Protein -- economics - Digital Collections - National Library of Medicine Search Results
A Study to Evaluate the Long-term Clinical Safety and Efficacy of Subcutaneously Administered C1-esterase Inhibitor in the...
Long-term prophylaxis in hereditary angioedema management: Current practices in France and unmet needs
Successful pregnancy outcome after treatment with C1-inhibitor concentrate in a patient with hereditary angioedema and a...
Recombinant human C1 esterase inhibitor (Conestat alfa) for prophylaxis to prevent attacks in adult and adolescent patients...
MESH TREE NUMBER CHANGES - 2008 MeSH
HUMAN C1-ESTERASE INHIBITOR - Books - NCBI
C1 Inhibitor Protein and Functional Tests | Quest Diagnostics
MESH TREE NUMBER CHANGES - 2008 MeSH
Ruconest | European Medicines Agency
NDF-RT Code NDF-RT Name
NEW (2010) MESH HEADINGS WITH SCOPE NOTES (UNIT RECORD FORMAT; 8/31/2009
Complement c7. Medical search
MH DELETED MN ADDED MN
MH DELETED MN ADDED MN
MH DELETED MN ADDED MN
Significance of Complement Activation in Alzheimer's Disease - touchNEUROLOGY
Hemopexin | Profiles RNS
DailyMed - HAEGARDA C1 ESTERASE INHIBITOR SUBCUTANEOUS (HUMAN)- human c1-esterase inhibitor kit
JBGSR.MS.ID.00216.text - Biogeneric science and Research
All About Heaven - Some science behind the scenes
HSP47 Heat-Shock Proteins | Profiles RNS
- The aim of this study is to assess the long-term safety of C1-esterase inhibitor (C1-INH) in preventing hereditary angioedema (HAE) attacks when it is administered under the skin of subjects with HAE. (clinicaltrials.gov)
- 4. Serum concentrations of C reactive protein, alpha1 antitrypsin, and complement (C3, C4, C1 esterase inhibitor) before and during the Vuelta a Espańa. (nih.gov)
- The C1 esterase inhibitor protein is required to control the 'complement' and 'contact' systems, collections of proteins in the blood that fight against infection and cause inflammation. (europa.eu)
- The active substance in Ruconest, conestat alfa, is a copy of the C1 esterase inhibitor protein and works in the same way as the natural human protein. (europa.eu)
- Ruconest was studied in two main studies involving a total of 70 adults and adolescents with hereditary angioedema caused by low levels of C1 esterase inhibitor protein. (europa.eu)
- HAE type I - The most common form of the disorder is HAE type I, which is the result of abnormally low levels of certain complex proteins in the blood (C1 esterase inhibitors), known as complements. (allaboutheaven.org)
- Most of people with HAE acquire a C1 esterase inhibitor (C1-INH) mutation from one of their parents. (allaboutheaven.org)
- HAEGARDA is a plasma-derived concentrate of C1 Esterase Inhibitor (Human) (C1-INH) indicated for routine prophylaxis to prevent Hereditary Angioedema (HAE) attacks in patients 6 years of age and older. (nih.gov)
- C1 esterase inhibitor (C1-INH) is a protein found in the fluid part of your blood. (medlineplus.gov)
- Your health care provider will also measure the functional activity level of your C1 esterase inhibitor. (medlineplus.gov)
- Types I and II are clinically identical, involving deficiency or malfunction of the protein C1 inhibitor (C1-INH) - also called C1 esterase inhibitor. (patient.info)
- Angioedema is associated with the following disorders: 1) acquired C1-esterase inhibitor deficiency and 2) hereditory C1-esterase inhibitor deficiency. (mhmedical.com)
- HAE type I, which accounts for approximately 85% of patients is the result of decreased C1-esterase inhibitor production. (mhmedical.com)
- The remainder 15% of patients suffer from HAE type II, which is characterized by normal or even elevated levels of a functionally impaired C1-esterase inhibitor. (mhmedical.com)
- The hereditary form is autosomal dominant transmitted and caused by a mutation in the C1 inhibitor gene (C1-esterase inhibitor) located on chromosome 11p11.2-q13.1. (mhmedical.com)
- Activation leads to cleavage producing the C1 esterase, which may now act on C4 and C2. (mhmedical.com)
- C1-esterase inhibitor is the control protein that inhibits the spontaneous activation. (mhmedical.com)
- C1-INH is also called C1 esterase inhibitor, due C1s is often cleaved by synthetic esters in spectrophotometry. (eaglebio.com)
- There were 714 patients with C1 inhibitor (C1-INH) deficiency, of whom 423 (59.2%) were treated with LTP. (nih.gov)
- Hereditary angioedema (HAE) due to C1 inhibitor (C1-INH) deficiency is a debilitating and potentially lethal disease. (nih.gov)
- Areas covered: This review will critically appraise available information about rhC1-INH (conestat alfa) prophylactic treatment in adult and adolescent patients with congenital C1-INH deficiency. (nih.gov)
- The underlying cause of HAE is attributed to autosomal dominant inheritance of mutations in the C1 inhibitor (C1-INH gene or SERPING1 gene), which is mapped to chromosome 11 (11q12-q13.1).To date there are over 300 known genetic mutations that result in a deficiency of functional C1 Inhibitor. (allaboutheaven.org)
- Rarely, people may inherit deficiency of some complement proteins. (medlineplus.gov)
- Diagnosis, course, and management of angioedema in patients with acquired C1-inhibitor deficiency. (medlineplus.gov)
- Cases of complement deficiency have helped defined the role of complement in host defense. (medscape.com)
- A North African study of molecular basis of complement factor I deficiency in atypical hemolytic and uremic syndrome patients suggested that the Ile357Met mutation may be a founding effect. (medscape.com)
- C1‐INH deficiency can be acquired, or there are other causes. (patient.info)
- A disease commonly caused by heterozygous deficiency of C1-INH and leading to low levels of functional C1-INH and recurrent episodes of dermal and submucosal swelling. (eaglebio.com)
- Management of hereditary angioedema with C1-inhibitor concentrate during two successive pregnancies. (nih.gov)
- 19. Protein sgp 120 as a marker of an acquired angioedema. (nih.gov)
- Los individuos con déficit de C1-INH sufren ANGIOEDEMA HEREDITARIO. (bvsalud.org)
- Patients with low levels of this protein have excessive activity of these two systems, which leads to the symptoms of angioedema. (europa.eu)
- The low level of C1 inhibitor in the plasma leads to increased activation of pathways that release bradykinin, the chemical responsible for the angioedema due to increased vascular permeability, and the pain seen in individuals with HAE. (allaboutheaven.org)
- In a review of patients who do not have a history of HAE in their family, but who have relatively low levels of mutated C1-INH with persistent angioedema, 25% of new patients who had HAE had C1-INH changes that do not show signs of being inherited but rather new. (allaboutheaven.org)
- Both forms of angioedema are caused by low levels of C1-INH. (medlineplus.gov)
- Low levels of C1-INH may cause certain types of angioedema. (medlineplus.gov)
- There are two types of angioedema that result from decreased levels of C1-INH. (medlineplus.gov)
- C1-INH administration is the common treatment for hereditary angioedema (HAE). (eaglebio.com)
- Hereditary angioedema (HAE) is an autosomal dominant disorder that involves a defect in the C1-INH protein. (symptoma.com)
- Controlling prekallikrein activation by C1 inhibitor (C1Inh) represents the most essential mechanism for angioedema patient protection. (biomedfrontiers.org)
- The measurement of C1 Inhibitor (C1Inh) is the core laboratory testing for angioedema diagnosis. (biomedfrontiers.org)
- C1 inhibitor (C1INH), a member of the serine proteinase inhibitor ( serpin ) family , is an inhibitor of proteases in the complement system, the contact system of kinin generation, and the intrinsic coagulation pathway. (bvsalud.org)
- It is generated when C3b is inactivated (iC3b) and its alpha chain is cleaved by COMPLEMENT FACTOR I into C3c, and C3dg (955-1303) in the presence COMPLEMENT FACTOR H. Serum proteases further degrade C3dg into C3d (1002-1303) and C3g (955-1001). (lookformedical.com)
- C1 inhibitor function using contact-phase proteases as target: evaluation of an innovative assay. (biomedfrontiers.org)
- Table I. Control of contact phase, fibrinolysis, and complement proteases by C1 Inhibitor and α2Macroglobulin. (biomedfrontiers.org)
- There are 21666 SERPIN domains in 21322 proteins in SMART's nrdb database. (embl.de)
- Taxonomic distribution of proteins containing SERPIN domain. (embl.de)
- The complete taxonomic breakdown of all proteins with SERPIN domain is also avaliable . (embl.de)
- Click on the protein counts, or double click on taxonomic names to display all proteins containing SERPIN domain in the selected taxonomic class. (embl.de)
- Because the deduced amino acid sequence qualified the protein as a novel member of the serpin family of serine protease inhibitors, we called it neuroserpin. (embl.de)
- 5. Evidence for the involvement of arginine 462 and the flanking sequence of human C4 beta-chain in mediating C5 binding to the C4b subcomponent of the classical complement pathway C5 convertase. (nih.gov)
- 7. A single arginine to tryptophan interchange at beta-chain residue 458 of human complement component C4 accounts for the defect in classical pathway C5 convertase activity of allotype C4A6. (nih.gov)
- 11. Distal recognition site for classical pathway convertase located in the C345C/netrin module of complement component C5. (nih.gov)
- A glycoprotein that is central in both the classical and the alternative pathway of COMPLEMENT ACTIVATION. (lookformedical.com)
- This complex is arranged in nine subunits (six disulfide-linked dimers of A and B, and three disulfide-linked homodimers of C). C1q has binding sites for antibodies (the heavy chain of IMMUNOGLOBULIN G or IMMUNOGLOBULIN M). The interaction of C1q and immunoglobulin activates the two proenzymes COMPLEMENT C1R and COMPLEMENT C1S, thus initiating the cascade of COMPLEMENT ACTIVATION via the CLASSICAL COMPLEMENT PATHWAY. (lookformedical.com)
- It is a constituent of the ALTERNATIVE PATHWAY C3 CONVERTASE (C3bBb), and COMPLEMENT C5 CONVERTASES in both the classical (C4b2a3b) and the alternative (C3bBb3b) pathway. (lookformedical.com)
- C1q (the first protein in the classic complement pathway), early complement activation proteins (C4 and C3 activation fragments), and the MAC have been demonstrated by immunocytochemical staining in the Alzheimer's disease (AD) brain on senile plaques, NFTs, neuropil threads, and dystrophic neurites 9-12 (see Figure 2 ). (touchneurology.com)
- Aggregated Aβ efficiently binds C1q, activating the classic complement pathway, 2 and this process further enhances Aβ aggregation and fibril formation. (touchneurology.com)
- Complement activation in AD was initially reported to be limited to the classic pathway, 9 but alternative pathway activation was later reported as well. (touchneurology.com)
- Complement deficiencies, especially in the early classical pathway, predispose to the development of SLE, while activation of complement proteins is associated with disease activity [1, 8-10]. (biogenericpublishers.com)
- The complement cascade consists of 3 separate pathways that converge in a final common pathway. (medscape.com)
- The classical pathway is triggered by interaction of the Fc portion of an antibody (immunoglobulin [Ig] M, IgG1, IgG2, IgG3) or C-reactive protein with C1q. (medscape.com)
- Lectins activate the lectin pathway in a manner similar to the antibody interaction with complement in the classical pathway. (medscape.com)
- C1, the first component of the classical pathway of the complement system is a complex macromolecule. (mhmedical.com)
- Factor D is unique to the Alternative Complement Pathway. (quidel.com)
- 1. Serum alpha1-antitrypsin but not complement C3 and C4 predicts chronic inflammation in hemodialysis patients. (nih.gov)
- 7. [Circadian rhythms of the so-called inflammation proteins in healthy subjects]. (nih.gov)
- Complement activation leads to inflammation, and eventually, organ damages occur. (biogenericpublishers.com)
- Anti-dsDNA antibodies and histones stimulate the circulation of immune complexes leading to inflammation, complement activation, and tissue damage . (biogenericpublishers.com)
- at the same time, the inflammation promoted by complement activation can result in cellular damage when not kept in check. (medscape.com)
- C1-INH plays an important role in suppression of inflammation and vascular permeability. (eaglebio.com)
Initiating complement activation1
- Factors initiating complement activation include ANTIGEN-ANTIBODY COMPLEXES, microbial ANTIGENS, or cell surface POLYSACCHARIDES. (lookformedical.com)
Serine protease i1
- Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors. (umbc.edu)
Pathways of complement activation1
- There are three pathways of complement activation. (eaglebio.com)
- Complement regulatory protein C1 inhibitor binds to selectins and interferes with endothelial-leukocyte adhesion. (bvsalud.org)
- The major fragment C5b binds to the membrane initiating the spontaneous assembly of the late complement components, C5-C9, into the MEMBRANE ATTACK COMPLEX. (lookformedical.com)
- 16. Cytokines associated with amyloid plaques in Alzheimer's disease brain stimulate human glial and neuronal cell cultures to secrete early complement proteins, but not C1-inhibitor. (nih.gov)
Acute phase pr1
- 16. C3 and C4 complement components and acute phase proteins in late pregnancy and parturition. (nih.gov)
Cleavage of complement2
- C1-INH is part of the complement system, coagulation system and fibrinolytic system. (patient.info)
- 7 Complement activation is normally closely regulated through the actions of endogenous complement inhibitory proteins, 8 including CD59, clusterin, vitronectin, C1-inhibitor, complement inhibitor C4b-binding protein, decay-activating factor, and factor H. When these regulatory mechanisms are insufficient, then tissue damage can result. (touchneurology.com)
- 5. [Effect of a high saturated fatty acids load on serum concentrations of C-reactive protein, alpha1-antitrypsin, fibrinogen and alpha1-acid glycoprotein in obese women]. (nih.gov)
- 9. Host serum protein levels in cysts of human hydatidosis. (nih.gov)
- 14. The relationship between serum levels of lipoprotein(a) and proteins associated with the acute phase response. (nih.gov)
- 14. Effect of plicatic acid on human serum complement includes interference with C1 inhibitor function. (nih.gov)
- Serum glycoproteins participating in the host defense mechanism of COMPLEMENT ACTIVATION that creates the COMPLEMENT MEMBRANE ATTACK COMPLEX. (lookformedical.com)
- A 105-kDa serum glycoprotein with significant homology to the other late complement components, C7-C9. (lookformedical.com)
- The complement system is composed of more than 30 plasma and membrane-associated proteins, accounting for approximately 10% of the globulins in vertebrate serum, which function as an inflammatory cascade. (touchneurology.com)
- The Eagle Biosciences Human C1-INH ELISA Assay Kit is to be used for the in vitro quantitative determination of C1-INH in plasma and serum samples. (eaglebio.com)
- 13. Functional role of the linker between the complement control protein modules of complement protease C1s. (nih.gov)
- 20. Functional analysis of activated C1s, a subcomponent of the first component of human complement, by monoclonal antibodies. (nih.gov)
- Analysis of the primary structural features further characterized neuroserpin as a heparin-independent, functional inhibitor of a trypsin-like serine protease. (embl.de)
- Plasma derived C1-INH is an established treatment for both on demand and prophylaxis of HAE. (nih.gov)
- Physicians' concerns varied among therapies: poor tolerability for androgens and progestins, a lack of efficacy for tranexamic acid and progestins, dosage form, and high costs for C1-INHs and lanadelumab. (nih.gov)
- Some patients with type III HAE have a mutation in the F12 gene which produces a protein involved in blood clotting. (allaboutheaven.org)
- Genes that encode the proteins of complement components or their isotypes are distributed throughout different chromosomes, with 19 genes comprising 3 significant complement gene clusters in the human genome. (medscape.com)
Terminal complement complex2
- 15 Whether elevated complement activation in AD may result, in part, from impaired local defense mechanisms is not clear, due to conflicting reports about the status of complement inhibitory proteins in the AD brain. (touchneurology.com)
- Patient identification requires the determination of C1Inh function, this function is currently measured using C1 protease as target. (biomedfrontiers.org)
- We developed a laboratory assay for C1Inh function using contact-phase proteins, the target involved in the pathological process, without interference of α2M or plasma protease. (biomedfrontiers.org)
- 20. Circulating immune complexes, complement factors C3, C4, C1-inhibitor, alpha-1-antitrypsin and immunoglobulins in asthmatic patients. (nih.gov)
- Complement activation is a major inflammatory process whose primary functions are to assist in removing micro-organisms and cellular debris and processing of immune complexes. (touchneurology.com)
- Complement can be activated by many factors, including immune complexes, polysaccharides (including lipopolysaccharide, the major component of the outer membrane of Gram-negative bacteria), and neuropathological structures such as senile plaques, neurofibrillary tangles (NFTs), and Lewy bodies. (touchneurology.com)
- The complement proteins work with your immune system to protect the body from infections. (medlineplus.gov)
- The complement system is part of the innate immune system. (medscape.com)
- In addition to playing an important role in host defense against infection, the complement system is a mediator in both the pathogenesis and prevention of immune complex diseases, such as systemic lupus erythematosus (SLE). (medscape.com)
- New studies point to the complex interplay between the complement cascade and adaptive immune response, and complement is also being studied in association with ischemic injury as a target of therapy. (medscape.com)
- The complement system plays important roles in both innate and adaptive immune response and can produce an inflammatory and protective reaction to challenges from pathogens before an adaptive response can occur. (eaglebio.com)
Basis of complement1
- 8. Molecular basis of complement resistance of human melanoma cells expressing the C3-cleaving membrane protease p65. (nih.gov)
- As a part of the innate immunity, the complement system and its activation pathways (classical, lectin, and alternative pathways) play a complex role in SLE pathogenesis. (biogenericpublishers.com)
- Although the complement system is part of the body's innate, relatively nonspecific defense against pathogens, its role is hardly primitive or easily understood. (medscape.com)
- C1-INH spares the AP, leaving part of the innate antibacterial defense intact. (eaglebio.com)
- The complement system is a group of nearly 60 proteins in blood plasma or on the surface of some cells. (medlineplus.gov)
- 2007). The existing observations of AtECA:sGFP localization claim that these proteins could be involved with plasma membrane-associated procedures. (baxkyardgardener.com)
- AtECA:sGFP protein localize primarily towards the plasma membrane in protoplasts. (baxkyardgardener.com)
- AtECAs indicated as sGFP fusion protein localize towards the plasma membrane (PM), endosomes, and cell dish in transgenic vegetation. (baxkyardgardener.com)
- We prevented any interference from a possible high plasma kininogenase activity by preincubating the samples with protease inhibitor. (biomedfrontiers.org)
- The complement system plays an important part in defense against pyogenic organisms. (medscape.com)
- Conestat alfa is a recombinant form of human C1-INH (rhC1-INH) produced in transgenic rabbits. (nih.gov)
- Conestat alfa is produced by 'recombinant DNA technology': it is extracted from the milk of rabbits that have been given genes that make them able to produce the human protein in their milk. (europa.eu)
- C3 can be cleaved into COMPLEMENT C3A and COMPLEMENT C3B, spontaneously at low level or by C3 CONVERTASE at high level. (lookformedical.com)
- The minor fragment formed when C5 convertase cleaves C5 into C5a and COMPLEMENT C5B. (lookformedical.com)
- Each generates a C3 convertase, a serine protease that cleaves the central complement protein C3, and generates the major cleavage fragment C3b. (eaglebio.com)
- However, thrombosis has occurred in treatment attempts with high doses of C1-INH intravenous (I.V.) for prevention or therapy of capillary leak syndrome before, during or after cardiac surgery (unapproved indication and dose). (nih.gov)
- 1. Complement component C5: engineering of a mutant that is specifically cleaved by the C4-specific C1s protease. (nih.gov)
- 4. Mutants of complement component C3 cleaved by the C4-specific C1-s protease. (nih.gov)
- 6. A 100-kDa protein in the C4-activating component of Ra-reactive factor is a new serine protease having module organization similar to C1r and C1s. (nih.gov)
- 9. The structure and function of the first component of complement: genetic engineering approach (a review). (nih.gov)
- 10. Identification of a catalytic exosite for complement component C4 on the serine protease domain of C1s. (nih.gov)
- 12. Structural homologies of component C5 of human complement with components C3 and C4 by neutron scattering. (nih.gov)
- 15. Murine complement component C4 and sex-limited protein: identification of amino acid residues essential for C4 function. (nih.gov)
- 18. Third component of trout complement. (nih.gov)
- C6 is the next complement component to bind to the membrane-bound COMPLEMENT C5B in the assembly of MEMBRANE ATTACK COMPLEX. (lookformedical.com)
- Each eligible subject will enter the treatment phase, wherein subjects will be randomized to treatment with either low- or medium-volume C1-INH. (clinicaltrials.gov)
- 17. Complement C2 receptor inhibitor trispanning and the beta-chain of C4 share a binding site for complement C2. (nih.gov)
- The important components of this system are various cell membrane-associated proteins such as complement receptor 1 (CR1), complement receptor 2 (CR2), and decay accelerating factor (DAF). (medscape.com)
- Deficiencies in the complement cascade can lead to overwhelming infection and sepsis. (medscape.com)
- Complement deficiencies are said to comprise between 1 and 10% of all primary immunodeficiencies. (medscape.com)
- [ 4 ] A registry of complement deficiencies has been established as a means to promote joint projects on treatment and prevention of diseases associated with defective complement function. (medscape.com)
- This article outlines some of the disease states associated with complement deficiencies and their clinical implications. (medscape.com)
- Complement pathways and deficiencies. (medscape.com)
- Deficiencies in complement predispose patients to infection via 2 mechanisms: (1) ineffective opsonization and (2) defects in lytic activity (defects in MAC). (medscape.com)
- Specific complement deficiencies are also associated with an increased risk of developing autoimmune disease, such as SLE. (medscape.com)
- When activation of the system occurs, native complement proteins are enzymatically cleaved, generating complement 'activation proteins' that function as opsinins, anaphylatoxins, and chemokines (see Table 1 ). (touchneurology.com)
- C1-INH binding of C1 to the catalytic site of both C1r and C1s releases the latter two from the complex. (eaglebio.com)
- This study aimed to investigate the involvement of the complement system in the pathophysiology of childhood-onset SLE. (biogenericpublishers.com)
- This domain occurred 32 times on human genes ( 63 proteins). (umbc.edu)
- 8. Antiphospholipid Antibodies are Associated with Low Levels of Complement C3 and C4 in Patients with Systemic Lupus Erythematosus. (nih.gov)
- sTCC concentration as well as the extent of activation capacity of the three complement pathways could serve as reliable parameters for monitoring the individual course of disease in paediatric SLE patients. (biogenericpublishers.com)
- Do not use in patients with a history of life-threatening immediate hypersensitivity reactions, including anaphylaxis to C1-INH preparations or its excipients. (nih.gov)
Systemic Lupus Erythem2
- Additionally, we studied the correlation between the systemic lupus erythematosus disease activity index (SLEDAI) and the complement-specific values measured at the time of blood withdrawal. (biogenericpublishers.com)
- Complement factors may also be important in testing for autoimmune diseases, such as systemic lupus erythematosus. (medlineplus.gov)
- 2,3,12 Soluble, non-fibrillar Aβ may also be capable of activating complement, albeit to less of an extent than fibrillar Aβ. (touchneurology.com)
- Because complement activation exerts both protective and deleterious effects, it has been referred to as a 'double-edged sword. (touchneurology.com)
- Complement activation is thought to be triggered in the AD brain primarily by the interaction of complement proteins with aggregated forms of amyloidbeta (Aβ) and tau protein, the major components in plaques and NFTs, respectively. (touchneurology.com)
- 14 Complement activation and plaque formation are mutually promoting mechanisms. (touchneurology.com)
- 18 The significance of complement activation in the development and progression of AD is unclear. (touchneurology.com)
- Several of the activation proteins generated in this process have been demonstrated to exert neuroprotective effects in vitro , including protecting against excitotoxicity, 19 Aβ-induced neurotoxicity, 20 and apoptosis, 7 as well as facilitating the clearance of Aβ by microglia. (touchneurology.com)
- As a result the activation of the complement system is blocked. (eaglebio.com)
- The lack or non-functionality of said inhibitors leads to activation of an inflammatory cascade, which result in cutaneous and mucosal edema . (symptoma.com)
- It occurs as the result of the production of abnormal complement proteins and accounts for about 15-20% of this disorder. (allaboutheaven.org)
- Erythrocyte sedimentation rate, c-reactive-protein) . (biogenericpublishers.com)
- Besides, C1-INH can directly bind and neutralize LPS, inhibiting sepsis and endotoxin shock. (eaglebio.com)
- CrmA rapidly inhibits ICE with an association rate constant (kon) of 1.7 x 10(7) M-1 s-1, forming a tight complex with an equilibrium constant for inhibition (Ki) of less than 4 x 10(-12) M. These data indicate that CrmA is a potent inhibitor of ICE, consistent with the dramatic effects of CrmA on modifying host responses to virus infection. (embl.de)