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Enamelin
Enamelin is an enamel matrix protein (EMPs), that in humans is encoded by the ''ENAM'' gene. It is part of the non- amelogenins, which comprise 10% of the total enamel matrix proteins. It is one of the key proteins thought to be involved in amelogenesis (enamel development). The formation of enamel's intricate architecture is thought to be rigorously controlled in ameloblasts through interactions of various organic matrix protein molecules that include: enamelin, amelogenin, ameloblastin, tuftelin, dentine sialophosphoprotein, and a variety of enzymes. Enamelin is the largest protein (~168kDa) in the enamel matrix of developing teeth and is the least abundant (encompasses approximately 1-5%) of total enamel matrix proteins. It is present predominantly at the growing enamel surface. Structure Enamelin is thought to be the oldest member of the enamel matrix protein (EMP) family, with animal studies showing remarkable conservation of the gene phylogenetically. All other EMPs a ...
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Amelogenesis Imperfecta
Amelogenesis imperfecta (AI) is a congenital disorder which presents with a rare abnormal formation of the enamel or external layer of the crown of teeth, unrelated to any systemic or generalized conditions. Enamel is composed mostly of mineral, that is formed and regulated by the proteins in it. Amelogenesis imperfecta is due to the malfunction of the proteins in the enamel (ameloblastin, enamelin, tuftelin and amelogenin) as a result of abnormal enamel formation via amelogenesis. People with amelogenesis imperfecta may have teeth with abnormal color: yellow, brown or grey; this disorder can affect any number of teeth of both dentitions. Enamel hypoplasia manifests in a variety of ways depending on the type of AI an individual has (see below), with pitting and plane-form defects common. The teeth have a higher risk for dental cavities and are hypersensitive to temperature changes as well as rapid attrition, excessive calculus deposition, and gingival hyperplasia.American Acade ...
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Amelogenesis Imperfecta
Amelogenesis imperfecta (AI) is a congenital disorder which presents with a rare abnormal formation of the enamel or external layer of the crown of teeth, unrelated to any systemic or generalized conditions. Enamel is composed mostly of mineral, that is formed and regulated by the proteins in it. Amelogenesis imperfecta is due to the malfunction of the proteins in the enamel (ameloblastin, enamelin, tuftelin and amelogenin) as a result of abnormal enamel formation via amelogenesis. People with amelogenesis imperfecta may have teeth with abnormal color: yellow, brown or grey; this disorder can affect any number of teeth of both dentitions. Enamel hypoplasia manifests in a variety of ways depending on the type of AI an individual has (see below), with pitting and plane-form defects common. The teeth have a higher risk for dental cavities and are hypersensitive to temperature changes as well as rapid attrition, excessive calculus deposition, and gingival hyperplasia.American Acade ...
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Amelogenesis
Amelogenesis is the formation of enamel on teeth and begins when the crown is forming during the advanced bell stage of tooth development after dentinogenesis forms a first layer of dentin. Dentin must be present for enamel to be formed. Ameloblasts must also be present for dentinogenesis to continue. A message is sent from the newly differentiated odontoblasts to the inner enamel epithelium (IEE) that causes epithelial cells to further differentiate into active secretory ameloblasts. Dentinogenesis is in turn dependent on signals from the differentiating IEE in order for the process to continue. This prerequisite is an example of the biological concept known as ''reciprocal induction'', in this instance between mesenchymal and epithelial cells. Stages Amelogenesis is considered to have three stages. The first stage is known as the inductive stage, the second is the secretory stage, and the third stage is known as the maturation stage. During the inductive stage, ameloblast ...
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Tuftelin
Tuftelin is an acidic phosphorylated glycoprotein found in tooth enamel. In humans, the Tuftelin protein is encoded by the ''TUFT1'' gene. It is an acidic protein that is thought to play a role in dental enamel mineralization and is implicated in caries susceptibility. It is also thought to be involved with adaptation to hypoxia, mesenchymal stem cell function, and neurotrophin nerve growth factor mediated neuronal differentiation. Classification There are two kinds of enamel proteins: Amelogenins & Nonamelogenins. Tuftelin falls under nonamelogenins. Function This protein is formed for a short time during amelogenesis. The function of tuftelins is under contention, but it is proposed that it acts to start the mineralization process of enamel during tooth development. Other significant proteins in enamel are amelogenins, enamelins, and ameloblastins. Research The human encoding gene for tuftelin (TUFT1) was cloned by Profs. Danny Deutsch and Aharon Palmon from the H ...
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Amelogenesis
Amelogenesis is the formation of enamel on teeth and begins when the crown is forming during the advanced bell stage of tooth development after dentinogenesis forms a first layer of dentin. Dentin must be present for enamel to be formed. Ameloblasts must also be present for dentinogenesis to continue. A message is sent from the newly differentiated odontoblasts to the inner enamel epithelium (IEE) that causes epithelial cells to further differentiate into active secretory ameloblasts. Dentinogenesis is in turn dependent on signals from the differentiating IEE in order for the process to continue. This prerequisite is an example of the biological concept known as ''reciprocal induction'', in this instance between mesenchymal and epithelial cells. Stages Amelogenesis is considered to have three stages. The first stage is known as the inductive stage, the second is the secretory stage, and the third stage is known as the maturation stage. During the inductive stage, ameloblast ...
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Biomineralization
Biomineralization, also written biomineralisation, is the process by which living organisms produce minerals, often to harden or stiffen existing tissues. Such tissues are called mineralized tissues. It is an extremely widespread phenomenon; all six taxonomic kingdoms contain members that are able to form minerals, and over 60 different minerals have been identified in organisms. Examples include silicates in algae and diatoms, carbonates in invertebrates, and calcium phosphates and carbonates in vertebrates. These minerals often form structural features such as sea shells and the bone in mammals and birds. Organisms have been producing mineralized skeletons for the past 550 million years. Calcium carbonates and calcium phosphates are usually crystalline, but silica organisms (sponges, diatoms...) are always non crystalline minerals. Other examples include copper, iron and gold deposits involving bacteria. Biologically formed minerals often have special uses such as ma ...
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Amelogenin
Amelogenins are a group of protein isoforms produced by alternative splicing or proteolysis from the ''AMELX'' gene, on the X chromosome, and also the ''AMELY'' gene in males, on the Y chromosome. They are involved in amelogenesis, the development of enamel. Amelogenins are type of extracellular matrix protein, which, together with ameloblastins, enamelins and tuftelins, direct the mineralization of enamel to form a highly organized matrix of rods, interrod crystal and proteins. Although the precise role of amelogenin(s) in regulating the mineralization process is unknown, it is known that amelogenins are abundant during amelogenesis. Developing human enamel contains about 70% protein, 90% of which are amelogenins. Function Amelogenins are believed to be involved in the organizing of enamel rods during tooth development. The latest research indicates that these proteins regulate the initiation and growth of hydroxyapatite crystals during the mineralization of enamel. In a ...
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Amelogenin
Amelogenins are a group of protein isoforms produced by alternative splicing or proteolysis from the ''AMELX'' gene, on the X chromosome, and also the ''AMELY'' gene in males, on the Y chromosome. They are involved in amelogenesis, the development of enamel. Amelogenins are type of extracellular matrix protein, which, together with ameloblastins, enamelins and tuftelins, direct the mineralization of enamel to form a highly organized matrix of rods, interrod crystal and proteins. Although the precise role of amelogenin(s) in regulating the mineralization process is unknown, it is known that amelogenins are abundant during amelogenesis. Developing human enamel contains about 70% protein, 90% of which are amelogenins. Function Amelogenins are believed to be involved in the organizing of enamel rods during tooth development. The latest research indicates that these proteins regulate the initiation and growth of hydroxyapatite crystals during the mineralization of enamel. In a ...
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Ameloblastin
Ameloblastin (abbreviated AMBN and also known as Sheathlin or Amelin) is an enamel matrix protein that in humans is encoded by the AMBN gene. Function Ameloblastin is a specific protein found in tooth enamel. Although less than 5% of enamel consists of protein, ameloblastins constitute 5–10% of all enamel protein, making it the second most abundant enamel matrix protein. This protein is formed by ameloblasts during the early secretory to late maturation stages of amelogenesis. Although not completely understood, the function of ameloblastins is believed to be in controlling the elongation of enamel crystals and generally directing enamel mineralization during tooth development. Ameloblastin helps in the growth of a crystalline enameloid layer consisting of randomly oriented short enamel crystals. Ameloblastin cleavage products are found in the sheath space between rod and interrod enamel, while intact ameloblastin accumulates on the enamel rods. This difference in localization ...
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Ameloblastin
Ameloblastin (abbreviated AMBN and also known as Sheathlin or Amelin) is an enamel matrix protein that in humans is encoded by the AMBN gene. Function Ameloblastin is a specific protein found in tooth enamel. Although less than 5% of enamel consists of protein, ameloblastins constitute 5–10% of all enamel protein, making it the second most abundant enamel matrix protein. This protein is formed by ameloblasts during the early secretory to late maturation stages of amelogenesis. Although not completely understood, the function of ameloblastins is believed to be in controlling the elongation of enamel crystals and generally directing enamel mineralization during tooth development. Ameloblastin helps in the growth of a crystalline enameloid layer consisting of randomly oriented short enamel crystals. Ameloblastin cleavage products are found in the sheath space between rod and interrod enamel, while intact ameloblastin accumulates on the enamel rods. This difference in localization ...
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Dentistry
Dentistry, also known as dental medicine and oral medicine, is the branch of medicine focused on the teeth, gums, and mouth. It consists of the study, diagnosis, prevention, management, and treatment of diseases, disorders, and conditions of the mouth, most commonly focused on dentition (the development and arrangement of teeth) as well as the oral mucosa. Dentistry may also encompass other aspects of the craniofacial complex including the temporomandibular joint. The practitioner is called a dentist. The history of dentistry is almost as ancient as the history of humanity and civilization with the earliest evidence dating from 7000 BC to 5500 BC. Dentistry is thought to have been the first specialization in medicine which have gone on to develop its own accredited degree with its own specializations. Dentistry is often also understood to subsume the now largely defunct medical specialty of stomatology (the study of the mouth and its disorders and diseases) for which reas ...
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Proteins
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residu ...
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