Disintegrins
Viperidae
Viper Venoms
Crotalid Venoms
Agkistrodon
Snake Venoms
Crotalus
Venoms
ADAM Proteins
Platelet Aggregation Inhibitors
Vitreoretinopathy, Proliferative
Integrins
Elapid Venoms
Integrin alpha5
Amino Acid Sequence
Molecular Sequence Data
Peptides
Platelet Glycoprotein GPIIb-IIIa Complex
Salivary Glands
Retinal Detachment
Platelet Aggregation
Receptors, Vitronectin
Fibrinogen
Sequence Homology, Amino Acid
Platelet Membrane Glycoproteins
Sequence Alignment
Vitreous Body
Amino Acid Motifs
EC3, a novel heterodimeric disintegrin from Echis carinatus venom, inhibits alpha4 and alpha5 integrins in an RGD-independent manner. (1/290)
EC3, a heterodimeric disintegrin (Mr = 14,762) isolated from Echis carinatus venom is a potent antagonist of alpha4 integrins. Two subunits called EC3A and EC3B were isolated from reduced and alkylated EC3 by reverse-phase high performance liquid chromatography. Each subunit contained 67 residues, including 10 cysteines, and displayed a high degree of homology to each other and to other disintegrins. EC3 inhibited adhesion of cells expressing alpha4beta1 and alpha4beta7 integrins to natural ligands vascular cell adhesion molecule 1 (VCAM-1) and mucosal addressin cell adhesion molecule 1 (MadCAM-1) with IC50 = 6-30 nM, adhesion of K562 cells (alpha5beta1) to fibronectin with IC50 = 150 nM, and adhesion of alphaIIbbeta3 Chinese hamster ovary cells to fibrinogen with IC50 = 500 nM; it did not inhibit adhesion of alphavbeta3 Chinese hamster ovary cells to vitronectin. Ethylpyridylethylated EC3B inhibited adhesion of Jurkat cells to immobilized VCAM-1 (IC50 = 6 microM), whereas EC3A was inactive in this system. The MLDG motif appeared to be essential for activity of EC3B. Linear MLDG peptide inhibited the adhesion of Jurkat to VCAM-1 in a dose-dependent manner (IC50 = 4 mM), whereas RGDS peptide was not active at the same concentration. MLDG partially inhibited adhesion of K562 cells to fibronectin (5-10 mM) in contrast to RGDS peptide (IC50 = 3 mM), inhibiting completely at 10 mM. (+info)Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins. (2/290)
We purified, cloned, and expressed aggrecanase, a protease that is thought to be responsible for the degradation of cartilage aggrecan in arthritic diseases. Aggrecanase-1 [a disintegrin and metalloproteinase with thrombospondin motifs-4 (ADAMTS-4)] is a member of the ADAMTS protein family that cleaves aggrecan at the glutamic acid-373-alanine-374 bond. The identification of this protease provides a specific target for the development of therapeutics to prevent cartilage degradation in arthritis. (+info)Nucleotide sequence of a cDNA encoding a common precursor of disintegrin flavostatin and hemorrhagic factor HR2a from the venom of Trimeresurus flavoviridis. (3/290)
The venom of Trimeresurus flavoviridis has three disintegrins that act as platelet aggregation inhibitors by binding to integrin alphaIIb beta3 on platelets through its Arg-Gly-Asp sequence. We isolated the cDNA encoding the flavostatin precursor that is one of the disintegrins in T. flavoviridis venom. The open reading frame consisted of four regions, a pre-peptide region, a metalloprotease region, a spacer region and a disintegrin region, indicating that the flavostatin precursor belongs to the metalloprotease/disintegrin family. Surprisingly, the deduced amino acid sequence of the metalloprotease region was completely consistent with that of hemorrhagic metalloprotease HR2a, which indicated that this metalloprotease released from the flavostatin precursor functions as a hemorrhagic factor. These observations indicated that a disintegrin and a hemorrhagic metalloprotease were synthesized as a common precursor. Thus, our results support the hypothesis that a disintegrin is synthesized as a metalloprotease/disintegrin precursor and matures by cleavage from the precursor molecule. (+info)ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix. (4/290)
Cellular disintegrin and metalloproteinases (ADAMs) are a family of genes with a sequence similar to the snake venom metalloproteinases and disintegrins. ADAMTS-1 is a unique ADAM family protein with respect to the presence of thrombospondin type I motifs and the capacity to bind to the extracellular matrix. Because ADAMTS-1 has a potential zinc-binding motif in the metalloproteinase domain, we examined in this study whether ADAMTS-1 is an active metalloproteinase by means of the proteinase trapping mechanism of alpha2-macroglobulin. We found that the soluble type of ADAMTS-1 protein is able to form a covalent-binding complex with alpha2-macroglobulin. Furthermore, the point mutation within the zinc-binding motif of ADAMTS-1 protein eliminates its capacity to bind to alpha2-macroglobulin. These data demonstrate that the metalloproteinase domain of ADAMTS-1 is catalytically active. In addition, we showed that the removal of the pro-domain from the ADAMTS-1 precursor is impaired in the furin-deficient cell line, LoVo, and that the processing ability of the cells is restored by the co-expression of the furin cDNA. These data provide evidence that the ADAMTS-1 precursor is processed in vivo by furin endopeptidase in the secretory pathway. Consequently, ADAMTS-1 is an active metalloprotease that is associated with the extracellular matrix. This study strongly suggests that ADAMTS-1 may play a role in the inflammatory process through its protease activity. (+info)Proinflammatory cytokines regulate tissue inhibitors of metalloproteinases and disintegrin metalloproteinase in cardiac cells. (5/290)
OBJECTIVE: Tissue inhibitors of metalloproteinases (TIMPs) are downregulated in the failing human heart. The objective of the present study was to test the hypothesis that cytokines might be involved in the regulation of TIMPs in cardiac cells. METHODS: Neonatal Sprague-Dawley rat ventricular cells were exposed to 100 units/ml tumor necrosis factor-alpha and/or 5 ng/ml interleukin-1 beta. The mRNA and protein expression of TIMPs-1-4 and disintegrin metalloproteinase was analyzed using Northern blot, ELISA and/or Western blot, respectively. Proteolytic activity and extracellular matrix degradation and turnover were determined using gelatin zymography and pulse-chase experiments. RESULTS: The TIMP-1 mRNA was upregulated in cardiac cells, while TIMP-1 protein levels were unchanged in myocytes but downregulated in non-myocytes. The TIMP-2 expression did not change with the cytokine treatment. TIMP-3 was downregulated at both the mRNA and protein levels in cardiac cells. TIMP-4 protein was transiently increased and then returned to control level. In contrast, disintegrin metalloproteinase mRNA and protein were significantly upregulated in those cells. The gelatinolytic activity and extracellular matrix protein degradation were significantly increased. CONCLUSIONS: Tumor necrosis factor-alpha and interleukin-1 beta regulate the expression of TIMPs and disintegrin metalloproteinase, which may in turn contribute to the increased matrix degradation in cardiac cells. Since heart failure in humans is characterized by both re-expression of myocardial cytokines and remodeling of the extracellular matrix, those in vitro results suggest a potential role for those cytokines in the regulation of extracellular matrix remodeling and therefore in the transition to the end-stage heart failure phenotype. (+info)METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity. (6/290)
We have studied two related proteins that contain a repeated amino acid motif homologous to the anti-angiogenic type 1 repeats of thrombospondin-1 (TSP1). Complete sequence analysis revealed no other similarities with TSP1, but identified unique signal sequences, as well as metalloprotease and disintegrin-like domains in the NH(2) termini. We named these proteins METH-1 and METH-2 due to the novel combination of metalloprotease and thrombospondin domains. Overall amino acid sequence identity between METH-1 and METH-2 is 51. 7%, yet transcript distribution revealed non-overlapping patterns of expression in tissues and cultured cell lines. To characterize these proteins functionally, we isolated full-length cDNAs, produced recombinant protein, and generated antisera to the recombinant proteins. Both METH-1 and METH-2 represent single copy genes, which encode secreted and proteolytically processed proteins. METH proteins suppressed fibroblast growth factor-2-induced vascularization in the cornea pocket assay and inhibited vascular endothelial growth factor-induced angiogenesis in the chorioallantoic membrane assay. Suppression of vessel growth in both assays was considerably greater than that mediated by either thrombospondin-1 or endostatin on a molar basis. Consistent with an endothelial specific response, METH-1 and METH-2 were shown to inhibit endothelial cell proliferation, but not fibroblast or smooth muscle growth. We propose that METH-1 and METH-2 represent a new family of proteins with metalloprotease, disintegrin, and thrombospondin domains. The distinct distribution of each gene product suggests that each has evolved distinct regulatory mechanisms that potentially allow for fine control of activity during distinct physiological and pathological states. (+info)ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family. (7/290)
We report the primary structure of three novel, putative zinc metalloproteases designated ADAM-TS5, ADAM-TS6, and ADAM-TS7. All have a similar domain organization, comprising a preproregion, a reprolysin-type catalytic domain, a disintegrin-like domain, a thrombospondin type-1 (TS) module, a cysteine-rich domain, a spacer domain without cysteine residues, and a COOH-terminal TS module. These genes are differentially regulated during mouse embryogenesis and in adult tissues, with Adamts5 highly expressed in the peri-implantation period in embryo and trophoblast. These proteins are similar to four other cognate gene products, defining a distinct family of human reprolysin-like metalloproteases, the ADAM-TS family. The other members of the family are ADAM-TS1, an inflammation-induced gene, the procollagen I/II amino-propeptide processing enzyme (PCINP, ADAM-TS2), and proteins predicted by the KIAA0366 and KIAA0688 genes (ADAM-TS3 and ADAM-TS4). Individual ADAM-TS members differ in the number of COOH-terminal TS modules, and some have unique COOH-terminal domains. The ADAM-TS genes are dispersed in human and mouse genomes. (+info)MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes. (8/290)
The metalloprotease disintegrin cysteine-rich (MDC) proteins are a recently identified family of transmembrane proteins that function in proteolytic processing of cell surface molecules and in cell adhesion. Since lymphocytes must interact with a constantly changing environment, we hypothesized that lymphocytes would express unique MDC proteins. To identify MDC proteins expressed in human lymph node, a polymerase chain reaction-based strategy combined with degenerate oligonucleotide primers was employed. We report here the identification of MDC-L (ADAM 23), a novel member of the MDC protein family. The results obtained from cDNA cloning and Northern blot analysis of mRNA isolated from various lymphoid tissues indicate that a 2.8-kilobase mRNA encoding a transmembrane form, MDC-Lm, and a 2.2-kilobase mRNA encoding a secreted form, MDC-Ls, are expressed in a tissue-specific manner. MDC-L mRNA was shown to be predominantly expressed in secondary lymphoid tissues, such as lymph node, spleen, small intestine, stomach, colon, appendix, and trachea. Furthermore, immunohistochemical staining with an anti-MDC-L antibody demonstrated that cells with typical lymphocyte morphology are responsible for expression of the MDC-L antigen in these lymphoid tissues. MDC-Lm was found to be expressed on the surface of human peripheral blood lymphocytes and transformed B- and T-lymphocyte cell lines as an 87-kDa protein. Thus, we have identified a novel lymphocyte-expressed MDC protein family member. (+info)Disintegrins are a group of small, cysteine-rich proteins that are derived from the venom of certain snakes, such as vipers and pit vipers. They are named for their ability to disrupt the integrin-mediated adhesion of cells, which is an important process in many physiological and pathological processes, including hemostasis, inflammation, and cancer metastasis.
Disintegrins contain a conserved RGD (Arg-Gly-Asp) or KTS (Lys-Thr-Ser) sequence that allows them to bind specifically to integrin receptors on the surface of cells. This binding can cause various effects, such as inhibiting cell adhesion, migration, and proliferation, or promoting apoptosis (programmed cell death).
Due to their potent biological activities, disintegrins have been studied for their potential therapeutic applications in various diseases, including thrombosis, cancer, and inflammation. However, further research is needed to fully understand their mechanisms of action and safety profiles before they can be used clinically.
Viperidae is not a term that has a medical definition per se, but it is a term used in the field of biology and zoology. Viperidae is the family name for a group of venomous snakes commonly known as vipers. This family includes various types of pit vipers, adders, and rattlesnakes.
While Viperidae itself may not have direct medical relevance, understanding the biology and behavior of these creatures is important in the context of medical fields such as toxicology and emergency medicine. Knowledge about the venomous properties of viper snakes and their potential to cause harm to humans is crucial for appropriate treatment and management of snakebites.
"Viper venoms" refer to the toxic secretions produced by members of the Viperidae family of snakes, which include pit vipers (such as rattlesnakes, copperheads, and cottonmouths) and true vipers (like adders, vipers, and gaboon vipers). These venoms are complex mixtures of proteins, enzymes, and other bioactive molecules that can cause a wide range of symptoms in prey or predators, including local tissue damage, pain, swelling, bleeding, and potentially life-threatening systemic effects such as coagulopathy, cardiovascular shock, and respiratory failure.
The composition of viper venoms varies widely between different species and even among individuals within the same species. However, many viper venoms contain a variety of enzymes (such as phospholipases A2, metalloproteinases, and serine proteases) that can cause tissue damage and disrupt vital physiological processes in the victim. Additionally, some viper venoms contain neurotoxins that can affect the nervous system and cause paralysis or other neurological symptoms.
Understanding the composition and mechanisms of action of viper venoms is important for developing effective treatments for venomous snakebites, as well as for gaining insights into the evolution and ecology of these fascinating and diverse creatures.
Crotalid venoms are the toxic secretions produced by the members of the Crotalinae subfamily, also known as pit vipers. This group includes rattlesnakes, cottonmouths (or water moccasins), and copperheads, which are native to the Americas, as well as Old World vipers found in Asia and Europe, such as gaboon vipers and saw-scaled vipers.
Crotalid venoms are complex mixtures of various bioactive molecules, including enzymes, proteins, peptides, and other low molecular weight components. They typically contain a variety of pharmacologically active components, such as hemotoxic and neurotoxic agents, which can cause extensive local tissue damage, coagulopathy, cardiovascular dysfunction, and neuromuscular disorders in the victim.
The composition of crotalid venoms can vary significantly between different species and even among individual specimens within the same species. This variability is influenced by factors such as geographic location, age, sex, diet, and environmental conditions. As a result, the clinical manifestations of crotalid envenomation can be highly variable, ranging from mild local reactions to severe systemic effects that may require intensive medical treatment and supportive care.
Crotalid venoms have been the subject of extensive research in recent years due to their potential therapeutic applications. For example, certain components of crotalid venoms have shown promise as drugs for treating various medical conditions, such as cardiovascular diseases, pain, and inflammation. However, further studies are needed to fully understand the mechanisms of action of these venom components and to develop safe and effective therapies based on them.
'Agkistrodon' is a genus of venomous snakes commonly known as pit vipers, found predominantly in North America and parts of Asia. This genus includes several species, among them the copperhead (A. contortrix), cottonmouth or water moccasin (A. piscivorus), and the cantil (A. bilineatus). These snakes are characterized by their triangular heads, heat-sensing pits between the eyes and nostrils, and elliptical pupils. They deliver venom through hollow fangs and can cause significant harm to humans if they bite.
It is important to note that 'Agkistrodon' species are often misidentified due to their similarities with other pit vipers. Accurate identification of a snakebite victim is crucial for proper medical treatment, so seeking professional help from herpetologists or medical professionals is highly recommended in such situations.
Snake venoms are complex mixtures of bioactive compounds produced by specialized glands in snakes. They primarily consist of proteins and peptides, including enzymes, neurotoxins, hemotoxins, cytotoxins, and cardiotoxins. These toxins can cause a variety of pharmacological effects on the victim's body, such as disruption of the nervous system, blood coagulation, muscle function, and cell membrane integrity, ultimately leading to tissue damage and potentially death. The composition of snake venoms varies widely among different species, making each species' venom unique in its toxicity profile.
'Crotalus' is a genus of venomous snakes commonly known as rattlesnakes. These snakes are native to the Americas, ranging from southern Canada to Argentina. They are characterized by the distinctive rattle on the end of their tails, which they use to warn potential predators before striking. The venom of Crotalus species is hemotoxic, meaning that it causes damage to blood vessels and tissue.
Some examples of species in this genus include the Western diamondback rattlesnake (Crotalus atrox), the timber rattlesnake (Crotalus horridus), and the sidewinder (Crotalus cerastes). It is important to note that all rattlesnakes are potentially dangerous and should be treated with caution. If you encounter a rattlesnake in the wild, it is best to leave it alone and avoid approaching it.
Metalloendopeptidases are a type of enzymes that cleave peptide bonds in proteins, specifically at interior positions within the polypeptide chain. They require metal ions as cofactors for their catalytic activity, typically zinc (Zn2+) or cobalt (Co2+). These enzymes play important roles in various biological processes such as protein degradation, processing, and signaling. Examples of metalloendopeptidases include thermolysin, matrix metalloproteinases (MMPs), and neutrophil elastase.
Venom is a complex mixture of toxic compounds produced by certain animals, such as snakes, spiders, scorpions, and marine creatures like cone snails and stonefish. These toxic substances are specifically designed to cause damage to the tissues or interfere with the normal physiological processes of other organisms, which can lead to harmful or even lethal effects.
Venoms typically contain a variety of components, including enzymes, peptides, proteins, and small molecules, each with specific functions that contribute to the overall toxicity of the mixture. Some of these components may cause localized damage, such as tissue necrosis or inflammation, while others can have systemic effects, impacting various organs and bodily functions.
The study of venoms, known as toxinology, has important implications for understanding the evolution of animal behavior, developing new therapeutics, and advancing medical treatments for envenomation (the process of being poisoned by venom). Additionally, venoms have been used in traditional medicine for centuries, and ongoing research continues to uncover novel compounds with potential applications in modern pharmacology.
ADAM (A Disintegrin And Metalloprotease) proteins are a family of type I transmembrane proteins that contain several distinct domains, including a prodomain, a metalloprotease domain, a disintegrin-like domain, a cysteine-rich domain, a transmembrane domain, and a cytoplasmic tail. These proteins are involved in various biological processes such as cell adhesion, migration, proteolysis, and signal transduction.
ADAM proteins have been found to play important roles in many physiological and pathological conditions, including fertilization, neurodevelopment, inflammation, and cancer metastasis. For example, ADAM12 is involved in the fusion of myoblasts during muscle development, while ADAM17 (also known as TACE) plays a crucial role in the shedding of membrane-bound proteins such as tumor necrosis factor-alpha and epidermal growth factor receptor ligands.
Abnormalities in ADAM protein function have been implicated in various diseases, including cancer, Alzheimer's disease, and arthritis. Therefore, understanding the structure and function of these proteins has important implications for the development of novel therapeutic strategies.
Platelet aggregation inhibitors are a class of medications that prevent platelets (small blood cells involved in clotting) from sticking together and forming a clot. These drugs work by interfering with the ability of platelets to adhere to each other and to the damaged vessel wall, thereby reducing the risk of thrombosis (blood clot formation).
Platelet aggregation inhibitors are often prescribed for people who have an increased risk of developing blood clots due to various medical conditions such as atrial fibrillation, coronary artery disease, peripheral artery disease, stroke, or a history of heart attack. They may also be used in patients undergoing certain medical procedures, such as angioplasty and stenting, to prevent blood clot formation in the stents.
Examples of platelet aggregation inhibitors include:
1. Aspirin: A nonsteroidal anti-inflammatory drug (NSAID) that irreversibly inhibits the enzyme cyclooxygenase, which is involved in platelet activation and aggregation.
2. Clopidogrel (Plavix): A P2Y12 receptor antagonist that selectively blocks ADP-induced platelet activation and aggregation.
3. Prasugrel (Effient): A third-generation thienopyridine P2Y12 receptor antagonist, similar to clopidogrel but with faster onset and greater potency.
4. Ticagrelor (Brilinta): A direct-acting P2Y12 receptor antagonist that does not require metabolic activation and has a reversible binding profile.
5. Dipyridamole (Persantine): An antiplatelet agent that inhibits platelet aggregation by increasing cyclic adenosine monophosphate (cAMP) levels in platelets, which leads to decreased platelet reactivity.
6. Iloprost (Ventavis): A prostacyclin analogue that inhibits platelet aggregation and causes vasodilation, often used in the treatment of pulmonary arterial hypertension.
7. Cilostazol (Pletal): A phosphodiesterase III inhibitor that increases cAMP levels in platelets, leading to decreased platelet activation and aggregation, as well as vasodilation.
8. Ticlopidine (Ticlid): An older P2Y12 receptor antagonist with a slower onset of action and more frequent side effects compared to clopidogrel or prasugrel.
Oligopeptides are defined in medicine and biochemistry as short chains of amino acids, typically containing fewer than 20 amino acid residues. These small peptides are important components in various biological processes, such as serving as signaling molecules, enzyme inhibitors, or structural elements in some proteins. They can be found naturally in foods and may also be synthesized for use in medical research and therapeutic applications.
Proliferative vitreoretinopathy (PVR) is a sight-threatening complication that can occur after open-globe eye injuries or retinal reattachment surgery. It is characterized by the abnormal growth and contraction of fibrous tissue on the surface of the retina and/or inside the vitreous cavity, which can cause distortion or detachment of the retina. This process can lead to visual impairment or even blindness if left untreated.
The term "proliferative" refers to the abnormal growth of cells (specifically, fibrous and inflammatory cells) on the retinal surface and within the vitreous cavity. These cells form membranes that can contract and cause traction on the retina, leading to distortion or detachment.
PVR is classified into three stages (A, B, and C) based on the extent of fibrous tissue formation and retinal changes. Stage A is characterized by the presence of cellular proliferation without any visible membranes or retinal changes. In stage B, fibrous membranes are present, but there is no retinal detachment. Finally, stage C involves the development of tractional retinal detachment due to the contraction of fibrous membranes.
Treatment for PVR typically involves additional surgical intervention to remove or release the fibrous tissue and reattach the retina. The prognosis for visual recovery depends on the severity and extent of the PVR, as well as the timing and success of treatment.
Integrins are a type of cell-adhesion molecule that play a crucial role in cell-cell and cell-extracellular matrix (ECM) interactions. They are heterodimeric transmembrane receptors composed of non-covalently associated α and β subunits, which form more than 24 distinct integrin heterodimers in humans.
Integrins bind to specific ligands, such as ECM proteins (e.g., collagen, fibronectin, laminin), cell surface molecules, and soluble factors, through their extracellular domains. The intracellular domains of integrins interact with the cytoskeleton and various signaling proteins, allowing them to transduce signals from the ECM into the cell (outside-in signaling) and vice versa (inside-out signaling).
These molecular interactions are essential for numerous biological processes, including cell adhesion, migration, proliferation, differentiation, survival, and angiogenesis. Dysregulation of integrin function has been implicated in various pathological conditions, such as cancer, fibrosis, inflammation, and autoimmune diseases.
Elapid venoms are the toxic secretions produced by elapid snakes, a family of venomous snakes that includes cobras, mambas, kraits, and coral snakes. These venoms are primarily composed of neurotoxins, which can cause paralysis and respiratory failure in prey or predators.
Elapid venoms work by targeting the nervous system, disrupting communication between the brain and muscles. This results in muscle weakness, paralysis, and eventually respiratory failure if left untreated. Some elapid venoms also contain hemotoxins, which can cause tissue damage, bleeding, and other systemic effects.
The severity of envenomation by an elapid snake depends on several factors, including the species of snake, the amount of venom injected, the location of the bite, and the size and health of the victim. Prompt medical treatment is essential in cases of elapid envenomation, as the effects of the venom can progress rapidly and lead to serious complications or death if left untreated.
I'm sorry for any confusion, but "snakes" is not a medical term. It refers to a group of legless reptiles that can be found on every continent except Antarctica. If you have any questions about snakes in a different context, please provide more information and I'll do my best to help!
Integrin α5 (also known as CD49e) is a subunit of the heterodimeric integrin receptor called very late antigen-5 (VLA-5). Integrins are transmembrane adhesion receptors that play crucial roles in cell-cell and cell-extracellular matrix interactions. The α5β1 integrin, formed by the association of α5 and β1 subunits, specifically recognizes and binds to fibronectin, a major extracellular matrix protein. This binding event is essential for various biological processes such as cell migration, proliferation, differentiation, and survival.
In summary, Integrin alpha5 (α5) is an essential subunit of the α5β1 integrin receptor that mediates cell-fibronectin interactions and contributes to several vital cellular functions.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
Peptides are short chains of amino acid residues linked by covalent bonds, known as peptide bonds. They are formed when two or more amino acids are joined together through a condensation reaction, which results in the elimination of a water molecule and the formation of an amide bond between the carboxyl group of one amino acid and the amino group of another.
Peptides can vary in length from two to about fifty amino acids, and they are often classified based on their size. For example, dipeptides contain two amino acids, tripeptides contain three, and so on. Oligopeptides typically contain up to ten amino acids, while polypeptides can contain dozens or even hundreds of amino acids.
Peptides play many important roles in the body, including serving as hormones, neurotransmitters, enzymes, and antibiotics. They are also used in medical research and therapeutic applications, such as drug delivery and tissue engineering.
The platelet glycoprotein GPIIb-IIIa complex, also known as integrin αIIbβ3 or CD41/CD61, is a heterodimeric transmembrane receptor found on the surface of platelets and megakaryocytes. It plays a crucial role in platelet aggregation and thrombus formation during hemostasis and pathological conditions such as arterial thrombosis.
The GPIIb-IIIa complex is composed of two non-covalently associated subunits, GPIIb (αIIb or CD41) and IIIa (β3 or CD61). Upon platelet activation by various agonists like ADP, thrombin, or collagen, the GPIIb-IIIa complex undergoes a conformational change that allows it to bind fibrinogen, von Willebrand factor, and other adhesive proteins. This binding event leads to platelet aggregation and the formation of a hemostatic plug or pathological thrombus.
Inhibition of the GPIIb-IIIa complex has been a target for antiplatelet therapy in the prevention and treatment of arterial thrombosis, such as myocardial infarction and stroke. Several pharmacological agents, including monoclonal antibodies and small molecule antagonists, have been developed to block this complex and reduce platelet aggregation.
Cell adhesion refers to the binding of cells to extracellular matrices or to other cells, a process that is fundamental to the development, function, and maintenance of multicellular organisms. Cell adhesion is mediated by various cell surface receptors, such as integrins, cadherins, and immunoglobulin-like cell adhesion molecules (Ig-CAMs), which interact with specific ligands in the extracellular environment. These interactions lead to the formation of specialized junctions, such as tight junctions, adherens junctions, and desmosomes, that help to maintain tissue architecture and regulate various cellular processes, including proliferation, differentiation, migration, and survival. Disruptions in cell adhesion can contribute to a variety of diseases, including cancer, inflammation, and degenerative disorders.
Salivary glands are exocrine glands that produce saliva, which is secreted into the oral cavity to keep the mouth and throat moist, aid in digestion by initiating food breakdown, and help maintain dental health. There are three major pairs of salivary glands: the parotid glands located in the cheeks, the submandibular glands found beneath the jaw, and the sublingual glands situated under the tongue. Additionally, there are numerous minor salivary glands distributed throughout the oral cavity lining. These glands release their secretions through a system of ducts into the mouth.
Retinal detachment is a serious eye condition that occurs when the retina, a thin layer of tissue at the back of the eye responsible for processing light and sending visual signals to the brain, pulls away from its normal position. This can lead to significant vision loss or even blindness if not promptly treated. Retinal detachment can be caused by various factors such as aging, trauma, eye disease, or an inflammatory condition. Symptoms of retinal detachment may include sudden flashes of light, floaters, a shadow in the peripheral vision, or a curtain-like covering over part of the visual field. Immediate medical attention is necessary to prevent further damage and preserve vision.
Platelet aggregation is the clumping together of platelets (thrombocytes) in the blood, which is an essential step in the process of hemostasis (the stopping of bleeding) after injury to a blood vessel. When the inner lining of a blood vessel is damaged, exposure of subendothelial collagen and tissue factor triggers platelet activation. Activated platelets change shape, become sticky, and release the contents of their granules, which include ADP (adenosine diphosphate).
ADP then acts as a chemical mediator to attract and bind additional platelets to the site of injury, leading to platelet aggregation. This forms a plug that seals the damaged vessel and prevents further blood loss. Platelet aggregation is also a crucial component in the formation of blood clots (thrombosis) within blood vessels, which can have pathological consequences such as heart attacks and strokes if they obstruct blood flow to vital organs.
Vitronectin receptors, also known as integrin αvβ3 or integrin avb3, are a type of cell surface receptor that bind to the protein vitronectin. These receptors are heterodimeric transmembrane proteins composed of αv and β3 subunits. They play important roles in various biological processes including cell adhesion, migration, proliferation, and survival. Vitronectin receptors are widely expressed in many different cell types, including endothelial cells, smooth muscle cells, and platelets. In addition to vitronectin, these receptors can also bind to other extracellular matrix proteins such as fibronectin, von Willebrand factor, and osteopontin. They are also involved in the regulation of angiogenesis, wound healing, and bone metabolism.
Fibrinogen is a soluble protein present in plasma, synthesized by the liver. It plays an essential role in blood coagulation. When an injury occurs, fibrinogen gets converted into insoluble fibrin by the action of thrombin, forming a fibrin clot that helps to stop bleeding from the injured site. Therefore, fibrinogen is crucial for hemostasis, which is the process of stopping bleeding and starting the healing process after an injury.
Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.
Platelet membrane glycoproteins are specialized proteins found on the surface of platelets, which are small blood cells responsible for clotting. These glycoproteins play crucial roles in various processes related to hemostasis and thrombosis, including platelet adhesion, activation, and aggregation.
There are several key platelet membrane glycoproteins, such as:
1. Glycoprotein (GP) Ia/IIa (also known as integrin α2β1): This glycoprotein mediates the binding of platelets to collagen fibers in the extracellular matrix, facilitating platelet adhesion and activation.
2. GP IIb/IIIa (also known as integrin αIIbβ3): This is the most abundant glycoprotein on the platelet surface and functions as a receptor for fibrinogen, von Willebrand factor, and other adhesive proteins. Upon activation, GP IIb/IIIa undergoes conformational changes that enable it to bind these ligands, leading to platelet aggregation and clot formation.
3. GPIb-IX-V: This glycoprotein complex is involved in the initial tethering and adhesion of platelets to von Willebrand factor (vWF) in damaged blood vessels. It consists of four subunits: GPIbα, GPIbβ, GPIX, and GPV.
4. GPVI: This glycoprotein is essential for platelet activation upon contact with collagen. It associates with the Fc receptor γ-chain (FcRγ) to form a signaling complex that triggers intracellular signaling pathways, leading to platelet activation and aggregation.
Abnormalities in these platelet membrane glycoproteins can lead to bleeding disorders or thrombotic conditions. For example, mutations in GPIIb/IIIa can result in Glanzmann's thrombasthenia, a severe bleeding disorder characterized by impaired platelet aggregation. On the other hand, increased expression or activation of these glycoproteins may contribute to the development of arterial thrombosis and cardiovascular diseases.
In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.
The vitreous body, also known simply as the vitreous, is the clear, gel-like substance that fills the space between the lens and the retina in the eye. It is composed mainly of water, but also contains collagen fibers, hyaluronic acid, and other proteins. The vitreous helps to maintain the shape of the eye and provides a transparent medium for light to pass through to reach the retina. With age, the vitreous can become more liquefied and may eventually separate from the retina, leading to symptoms such as floaters or flashes of light.
Amino acid motifs are recurring patterns or sequences of amino acids in a protein molecule. These motifs can be identified through various sequence analysis techniques and often have functional or structural significance. They can be as short as two amino acids in length, but typically contain at least three to five residues.
Some common examples of amino acid motifs include:
1. Active site motifs: These are specific sequences of amino acids that form the active site of an enzyme and participate in catalyzing chemical reactions. For example, the catalytic triad in serine proteases consists of three residues (serine, histidine, and aspartate) that work together to hydrolyze peptide bonds.
2. Signal peptide motifs: These are sequences of amino acids that target proteins for secretion or localization to specific organelles within the cell. For example, a typical signal peptide consists of a positively charged n-region, a hydrophobic h-region, and a polar c-region that directs the protein to the endoplasmic reticulum membrane for translocation.
3. Zinc finger motifs: These are structural domains that contain conserved sequences of amino acids that bind zinc ions and play important roles in DNA recognition and regulation of gene expression.
4. Transmembrane motifs: These are sequences of hydrophobic amino acids that span the lipid bilayer of cell membranes and anchor transmembrane proteins in place.
5. Phosphorylation sites: These are specific serine, threonine, or tyrosine residues that can be phosphorylated by protein kinases to regulate protein function.
Understanding amino acid motifs is important for predicting protein structure and function, as well as for identifying potential drug targets in disease-associated proteins.
Blood platelets, also known as thrombocytes, are small, colorless cell fragments in our blood that play an essential role in normal blood clotting. They are formed in the bone marrow from large cells called megakaryocytes and circulate in the blood in an inactive state until they are needed to help stop bleeding. When a blood vessel is damaged, platelets become activated and change shape, releasing chemicals that attract more platelets to the site of injury. These activated platelets then stick together to form a plug, or clot, that seals the wound and prevents further blood loss. In addition to their role in clotting, platelets also help to promote healing by releasing growth factors that stimulate the growth of new tissue.
Disintegrin - Wikipedia
Frontiers | A Disintegrin and Metalloprotease 17 in the Cardiovascular and Central Nervous Systems
Adam34 MGI Mouse Gene Detail - MGI:2181992 - a disintegrin and metallopeptidase domain 34
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Disintegrins | Profiles RNS
Rat ADAM9(A Disintegrin And Metalloprotease 9) ELISA Kit - Scalegenomics
Human ADAM9(A Disintegrin And Metalloprotease 9) ELISA Kit - AGTC Sequencing
Rat ADAMTS5(A Disintegrin And Metalloproteinase With Thrombospondin 5) ELISA Kit - Isogem
Human ADAM9(A Disintegrin And Metalloprotease 9) ELISA Kit - Biofarmaceutical Research Labs
ADAM Proteins - Medical Dictionary online-medical-dictionary.org
Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: metalloproteinase inhibitors as a new therapy
ADAM9 (A Disintegrin And Metalloproteinase 9, MCMP, MDC9, CORD9, Mltng) (HRP), IgG, Rabbit, Polyclonal | Labstore
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Y IL-1 expected a disintegrin and metalloproteinase 17 (ADAM17)-dependent shedding of your ligand neuregulin-1 (NRG-1). | Ezh2...
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Toxins | August 2018 - Browse Articles
ADAMTS10 gene: MedlinePlus Genetics
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Recombinant Anti-ADAM10 antibody [EPR23491-74] (ab252234) | Abcam
Snake Venom Extracellular vesicles (SVEVs) reveal wide molecular and functional proteome diversity | Scientific Reports
Proteins8
- Disintegrins are a family of small proteins (45-84 amino acids in length) from viper venoms that function as potent inhibitors of both platelet aggregation and integrin-dependent cell adhesion. (wikipedia.org)
- Disintegrin-like proteins are found in various species ranging from slime mold to humans. (wikipedia.org)
- Some other proteins known to contain a disintegrin domain are: Some snake venom zinc metalloproteinases consist of an N-terminal catalytic domain fused to a disintegrin domain. (wikipedia.org)
- ADAM17 is a metalloprotease and disintegrin that lodges in the plasmatic membrane of several cell types and is able to cleave a wide variety of cell surface proteins. (frontiersin.org)
- A Disintegrin and Metalloproteases (ADAM), originally named metalloproteinases disintegrin cystein-rich (MDC), are membrane-anchored cell surface proteins containing both disintegrin and metalloproteinase domains. (frontiersin.org)
- A family of cellular proteins related to snake venom disintegrins. (jax.org)
- The A disintegrin and metalloproteinases are a new gene family of proteins having a metalloprotease domain with matrix metalloproteinases and play an important role in the chondrocyte development process. (elsevierpure.com)
- SVEVs isolated from lyophilized venoms collected from four different species of snakes ( Agkistrodon contortrix contortrix , Crotalus atrox , Crotalus viridis and Crotalus cerberus oreganus ) were analyzed by mass spectrometry-based proteomic, which allowed the identification of proteins belonging to eight main functional protein classes such as SVMPs, serine proteinases, PLA 2 , LAAO, 5′nucleotidase, C-type lectin, CRISP and Disintegrin. (nature.com)
Cloned a disintegrin and metalloprotease1
- We cloned a disintegrin and metalloprotease 12 (ADAM12) as a specific enzyme to shed HB-EGF in the heart and found that dominant-negative expression of ADAM12 abrogated this signaling. (nih.gov)
Thrombospondin10
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Rat A Disintegrin And Metalloproteinase With Thrombospondin 5 (ADAMTS5) in samples from Serum, plasma, tissue homogenates and other biological fluids. (isogem.org)
- Description: A sandwich ELISA kit for detection of A Disintegrin And Metalloproteinase With Thrombospondin 5 from Rat in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (isogem.org)
- Description: A sandwich quantitative ELISA assay kit for detection of Human A Disintegrin And Metalloproteinase With Thrombospondin 5 (ADAMTS5) in samples from tissue homogenates, cell lysates or other biological fluids. (isogem.org)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human A Disintegrin And Metalloproteinase With Thrombospondin 5 (ADAMTS5) in tissue homogenates, cell lysates and other biological fluids. (isogem.org)
- Description: Quantitativesandwich ELISA kit for measuring Human A disintegrin and metalloproteinase with thrombospondin motifs 9 (ADAMTS9) in samples from serum, plasma, cell culture supernates, tissue homogenates. (master-sistemisanitari-medicinenonconvenzionali.org)
- Proteases produced by macrophages, such as matrix metalloproteinases and members of ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) family, play potential roles in regulating atherosclerotic plaque stability. (cardiff.ac.uk)
- Figure 3 A disintegrin-like and metalloproteinase with thrombospondin type-1 motifs 13 activity before and after treatment for acute rejection in a liver transplant recipient. (wjgnet.com)
- Endogenous inhibitors of angiogenesis include thrombospondin 1 (TSP-1) and a disintegrin and metalloproteinase with thrombospondin motifs 1 (ADAMTS-1), and their aberrant expression may contribute to the diabetes-related dysregulation of retinal vascular homeostasis and vasculopathies ( 7 , 8 ). (spandidos-publications.com)
- GLPG1972/S201086 is a disintegrin and metalloproteinase with thrombospondin motif-5 (ADAMTS-5) inhibitor in development as an osteoarthritis disease-modifying therapy. (lu.se)
- To Study the Role of Plasma Von Willebrand Factor Antigen (vWF) to A Disintegrin-like and Metalloproteinase With Thrombospondin Type-1 Motifs 13 (ADAMTS-13) Activity Ratio as a Predictor of Development of Extrahepatic Organ Failure in Acute on Chronic Liver Failure (ACLF) Patients. (who.int)
Contain a disintegrin1
- A family of membrane -anchored glycoproteins that contain a disintegrin and metalloprotease domain. (online-medical-dictionary.org)
Metalloproteinase 172
- Y IL-1 expected a disintegrin and metalloproteinase 17 (ADAM17)-dependent shedding of your ligand neuregulin-1 (NRG-1). (ezh2inhibitor.com)
- Analysis of published microarray data identified a network of genes up-regulated by HVECs in response to TSST-1 that includes the sheddase, a disintegrin and metalloproteinase 17 (ADAM17). (perfectusbiomed.com)
Metalloproteinases2
- Small Disintegrins: 49-51 amino acids, 4 disulfide bonds Medium Disintegrins: 70 amino acids, 6 disulfide bonds Large Disintegrins: 84 amino acids, 7 disulfide bonds Dimeric Disintegrins: 67 amino acids, 4 intra-chain disulfide bonds Snake Venom Metalloproteinases: 100 amino acids, 8 disulfide bond Disintegrins evolved via gene duplication of an ancestral protein family, the ADAM family. (wikipedia.org)
- Therefore, we analyzed the expression of A disintegrin and metalloproteinases and matrix metalloproteinases in several kinds of cartilaginous bone tumors at the messenger RNA level and immunohistochemical protein level and ascertained their relationships to the histologic degree of malignancy. (elsevierpure.com)
Gene1
- Study of the asthma susceptibility gene A Disintegrin and Metalloprotease 33 (ADAM33) in early life and adult asthma and other chronic lung diseases. (southampton.ac.uk)
ADAM97
- Here, we identified a disintegrin and a metalloproteinase domain 9 (ADAM9) protein as an important host factor for SARS-CoV-2 entry. (flutrackers.com)
- Here, we identify a disintegrin and metalloproteinase domain 9 (ADAM9) protein as a co-factor of ACE2 important for SARS-CoV-2 entry, even for the variants of concern, and show that ADAM9 interacts with Spike to aid virus entry. (flutrackers.com)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat A Disintegrin And Metalloprotease 9 (ADAM9) in Tissue homogenates, cell lysates and other biological fluids. (scalegen.com)
- Description: Quantitativesandwich ELISA kit for measuring Human A Disintegrin And Metalloprotease 9, ADAM9 in samples from serum, plasma, tissue homogenates, cell culture supernates, asciticfluid. (scalegen.com)
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human A Disintegrin And Metalloprotease 9 (ADAM9) in samples from Tissue homogenates, cell lysates, cell culture supernates and other biological fluids with no significant corss-reactivity with analogues from other species. (agctsequencing.com)
- Description: This Human A Disintegrin And Metalloprotease 9 (ADAM9) ELISA Kit employs a two-site sandwich ELISA to quantitate ADAM9. (agctsequencing.com)
- Description: A sandwich quantitative ELISA assay kit for detection of Human A Disintegrin And Metalloprotease 9 (ADAM9) in samples from tissue homogenates, cell lysates, cell culture supernates or other biological fluids. (pharmas-eu.org)
ADAM3
- ADAM10, a metalloprotease-disintegrin in the family of mammalian ADAM (for a disintegrin and metalloprotease), was recently identified to cleave TNF-a, notch and its ligand delta (1-3). (thermofisher.com)
- Matrix metalloproteinase-7 and adam-12 (a disintegrin and metalloproteinase-12) define a signaling axis in agonist-induced hypertension and cardiac hypertrophy. (ualberta.ca)
- En contraste con las proteínas ADAM, que residen en las MEMBRANAS CELULARES, las proteasas ADAMTS se segregan y actúan en la MATRIZ EXTRACELULAR. (bvsalud.org)
Inhibitors2
- Disintegrins thus block adhesive functions and act as platelet aggregation inhibitors. (rush.edu)
- Hirudin-derived thrombin inhibitors with disintegrin activity. (bvsalud.org)
Domain5
- Structurally, ADAM7 consists of an N-terminal domain, followed by a zinc metalloproteinase domain, a disintegrin domain, and a large C-terminal domain that contains a transmembrane region. (wikipedia.org)
- Monoclonal antibodies targeting the disintegrin-like domain of ADAMDEC1 modulates the proteolytic activity and enables quantification of ADAMDEC1 protein in human plasma. (ox.ac.uk)
- Binding of mAbs to one epitope bin in the C-terminal disintegrin-like domain efficiently reduces the proteolytic activity of ADAMDEC1. (ox.ac.uk)
- A unique mAb, also recognizing the disintegrin-like domain, stimulates the caseinolytic activity of ADAMDEC1 while having no significant effect on the proteolysis of carboxymethylated transferrin. (ox.ac.uk)
- Using two different mAbs binding the disintegrin-like domain, we developed a robust, quantitative sandwich ELISA and demonstrate secretion of mature ADAMDEC1 protein by primary human macrophages. (ox.ac.uk)
Thrombin1
- Disintegrins act as receptor antagonists, inhibiting aggregation induced by ADP, thrombin, platelet-activating factor and collagen. (wikipedia.org)
Receptors2
- Disintegrins contain an RGD (Arg-Gly-Asp) or KGD (Lys-Gly-Asp) sequence motif that binds specifically to integrin IIb-IIIa receptors on the platelet surface, thereby blocking the binding of fibrinogen to the receptor-glycoprotein complex of activated platelets. (wikipedia.org)
- Snake disintegrins inhibit the binding of ligands to integrin receptors. (embl.de)
ELISA1
- Description: A sandwich ELISA kit for detection of A Disintegrin And Metalloprotease 9 from Rat in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (scalegen.com)
Cleave1
- It has been suggested that these proteinases are able to cleave themselves from the disintegrin domains and that the latter may arise from such a post-translational processing. (wikipedia.org)
ADAM101
- Furthermore, D-Pen mainly regulated A disintegrin and metalloprotease 10 (ADAM10) expression via melatonin receptor 1 (MTNR1α) and the downstream PKA/ERK/CREB pathway. (figshare.com)
ADAMs1
- Molecules containing both disintegrin and metalloprotease domains are known as ADAMs. (embl.de)
Motifs1
- Figure 1 Plasma a disintegrin-like and metalloproteinase with throm-bospondin type-1 motifs 13 activity before and after living-related liver transplantation. (wjgnet.com)
Family2
- Small, medium, large, and dimeric disintegrin family are found only in the family Viperidae, suggesting duplication and diversification about 12-20 million years ago. (wikipedia.org)
- Reverse transciptase-polymerase chain reaction and real-time quantitative reverse transciptase-polymerase chain reaction of the expression of the A disintegrin and metalloproteinase family in cartilaginous bone tumors demonstrated that A disintegrin and metalloproteinase 28 messenger RNA levels in grade I chondrosarcoma were significantly higher than those in enchondroma (P = .009). (elsevierpure.com)
Blood2
- Disintegrins work by countering the blood clotting steps, inhibiting the clumping of platelets. (wikipedia.org)
- The role of disintegrin in preventing blood coagulation renders it of medical interest, particularly with regard to its use as an anti-coagulant. (wikipedia.org)
Cells2
- The metalloprotease-disintegrin ADAM8 is highly expressed in GBM tumor and immune cells and correlates with poor. (uni-marburg.de)
- A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. (embl.de)
Positive2
- Moreover, positive immunoreactivity of A disintegrin and metalloproteinase 28 was observed in 12 (59%) of 22 patients with grade I chondrosarcoma and in 21 (91%) of 23 patients with grade II chondrosarcoma, respectively. (elsevierpure.com)
- In contrast, only 2 (9%) of 21 cases of enchondromas demonstrated positive staining for A disintegrin and metalloproteinase 28. (elsevierpure.com)
Medical1
- Disintegrins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (rush.edu)
Thrombospondin5
- Intra-assay Precision (Precision within an assay): 3 samples with low, middle and high level A Disintegrin And Metalloproteinase With Thrombospondin 1 (ADAMTS1) were tested 20 times on one plate, respectively. (biomatik.com)
- Inter-assay Precision (Precision between assays): 3 samples with low, middle and high level A Disintegrin And Metalloproteinase With Thrombospondin 1 (ADAMTS1) were tested on 3 different plates, 8 replicates in each plate. (biomatik.com)
- This assay has high sensitivity and excellent specificity for detection of A Disintegrin And Metalloproteinase With Thrombospondin 1 (ADAMTS1). (biomatik.com)
- No significant cross-reactivity or interference between A Disintegrin And Metalloproteinase With Thrombospondin 1 (ADAMTS1) and analogues was observed. (biomatik.com)
- Aggrecanases belong to ADAMTS (A disintegrin and metalloprotease with thrombospondin motif) family of proteases. (mobitec.com)
ADAM171
- The disintegrin and metalloproteinase ADAM17, also known as tumor necrosis factor alpha converting enzyme, is expressed in adipocytes, and elevated levels of expression have been linked to obesity and insulin resistance. (usda.gov)
Metalloprotease disintegrin4
- Here we report the cloning of cDNAs encoding three full-length ( xMDC9 , xMDC11b, and xMDC13), and one partial (xMDC11a) metalloprotease- disintegrin from the amphibian Xenopus laevis, and the analysis of their expression during early X. laevis development and in adult tissues. (xenbase.org)
- The jararhagin is a type of metalloprotease disintegrin isolated from the venom of Bothrops jararaca, comprising metalloproteinase domain, disintegrin (ECD), and rich in cysteine. (fapesp.br)
- The metalloprotease-disintegrin ADAM8 is critically involved in the progression of pancreatic cancer. (uni-marburg.de)
- The Metalloprotease-Disintegrin ADAM8 Alters the Tumor Suppressor miR-181a-5p Expression Profile in Glioblastoma Thereby Contributing to Its Aggressiveness by: Schäfer, Agnes, et al. (uni-marburg.de)
Integrins1
- 7. Vipera lebetina venom contains two disintegrins inhibiting laminin-binding beta1 integrins. (nih.gov)
Metallopeptidase domain1
- ENSEMBL annotation of mouse reference assembly GRCm39, protein_coding, a disintegrin and metallopeptidase domain 29 [Source:MGI Symbol;Acc:MGI:2676326]. (jax.org)
Platelet aggregatio1
- Disintegrins thus block adhesive functions and act as platelet aggregation inhibitors. (bvsalud.org)
ADAM333
- Various studies reported a disintegrin and metalloprotease 33 (ADAM33) as an important susceptibility gene for asthma, which is frequently detected among certain populations. (nih.gov)
- A disintegrin and metalloprotease 33 ( ADAM33 ) has been identified as a susceptibility gene for asthma and single nucleotide polymorphisms (SNPs) in this gene have been associated with excessive decline of lung function in individuals with asthma. (atsjournals.org)
- A disintegrin and metalloprotease 33 ( ADAM33 ) has been identified as an asthma susceptibility gene ( 1 ). (atsjournals.org)
Apoptosis2
- 1. Lebein, a Snake Venom Disintegrin, Induces Apoptosis in Human Melanoma Cells. (nih.gov)
- 2. Lebein, a snake venom disintegrin, suppresses human colon cancer cells proliferation and tumor-induced angiogenesis through cell cycle arrest, apoptosis induction and inhibition of VEGF expression. (nih.gov)
Snake2
- Small Disintegrins: 49-51 amino acids, 4 disulfide bonds Medium Disintegrins: 70 amino acids, 6 disulfide bonds Large Disintegrins: 84 amino acids, 7 disulfide bonds Dimeric Disintegrins: 67 amino acids, 4 intra-chain disulfide bonds Snake Venom Metalloproteinases: 100 amino acids, 8 disulfide bond Disintegrins evolved via gene duplication of an ancestral protein family, the ADAM family. (wikipedia.org)
- This review gathers information on functional characteristics of disintegrins isolated from snake venoms, emphasizing a comprehensive view of the possibility of direct use of these molecules in the development of new drugs, or even indirectly as structural models. (ufla.br)
ELISA Kit1
- Description: This Human A Disintegrin And Metalloprotease 9 (ADAM9) ELISA Kit employs a two-site sandwich ELISA to quantitate ADAM9. (agctsequencing.com)
Obtustatin1
- The disintegrins Obtustatin and Viperistatin, were used as lead compounds for the synthesis of linear and cyclic peptides containing the KTS binding motif. (eurekaselect.com)
Tumor development1
- A disintegrin and metalloprotease 12 (ADAM12) has been associated with tumor development and progression. (mdpi.com)
Cells1
- 6. Disintegrin Tablysin-15 Suppresses Cancer Hallmarks in Melanoma Cells by Blocking FAK/Akt/ERK and NF-κB Signaling. (nih.gov)
Term1
- Also, a term starts with "a disintegrin and metalloprot" might have spVar in a varienty of form. (nih.gov)
Domains1
- It has been suggested that these proteinases are able to cleave themselves from the disintegrin domains and that the latter may arise from such a post-translational processing. (wikipedia.org)
Development1
- Neural crest -specific and general expression of distinct metalloprotease-disintegrins in early Xenopus laevis development. (xenbase.org)