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Junctional epidermolysis bullosa
Junctional epidermolysis bullosa
Junctional epidermolysis bullosa
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Laminin 332
Laminin 332 is present in the BMZ of nearly all epithelial tissues in the human body [140]. Furthermore, laminin 332 is the main component found at the upper lamina densa/lamina lucida border at the base of the anchoring filaments [120]. Mutations in laminin 332 are linked to a condition that causes skin fragility and severe blistering, which is known as junctional epidermolysis bullosa [141-143]. Moreover, the absence of laminin 332 expression considerably disrupts the epidermal adhesion, as seen in patients having the lethal disease known as Herlitz junctional epidermolysis bullosa [107, 141].
Laminin 332 can bind via the G domain to α6β4 and α3β1 integrins [144, 145]. It also has binding sites along its β-chain for laminin 311 and collagen VII [146], and other binding sites along the γ-chain for perlecan and different types of collagen (IV, VII, and XVII) [144, 146]. Several studies showed that laminin 332 is involved in various cellular processes, such as epithelial cell adhesion, spreading and migration [147, 148]. The
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The core protein includes three G domains: the G1 (N-terminal), G2, and G3 (C-terminal), which are separated by two rod-like segments. Genes encode for two kinds of nidogens with a similar structural organization: nidogen-1 (30 nm long) and nidogen-2 (40 nm long). Nidogen has various binding sites for laminins, perlecan, fibrinogen, fibronectin and collagen IV [118, 152]. The nidogen binds to collagen type IV via the G2 domain, while the G3 domain has a high affinity to laminin Y1 chain [153, 154]. Interestingly, the nidogen-laminin binding has been recognized as one of the highest binding affinities in nature [155]. However, the absence of both nidogen-1 and nidogen-2 does not disrupt the formation of a functional BMZ [103, 107,
The art piece, Rue Transnonain, is a historical lithograph that was published in a newspaper on April 15, 1834. During this time period in France, where this piece was created, there was a surge of political and social revolution. The lithograph was created to represent the massacre of innocent people that happened in Paris, France. “[The French National Guard responded] to gunshots from top-floor windows at number 12, Rue Transnonain, troops stormed the building and opened fire, killing and wounding residents” (“Rue Transnonain”). The subject of this artwork is the innocent people that were killed by the military. The most prominent element of art in this piece is line. Daumier used lines in order to depict all of the shapes, with an example
According to the text, “Lipid-soluble hormones are small in size, and has low solubility in aqueous fluid (Chapter 17, p. 573)”. Because of the property of this hormone, the probability of getting eliminated in the blood stream or the body is high. If this happens, these hormones can be eliminated through the kidneys. So in order for these hormones to not be eradicated in the system, it will need assistance from a binding protein.
called an active site. This active site is made by a few of the amino
A. NF is caused by a mutation in the NF1 gene, which creates the protein neurofibromin.
Repair after a muscle is damaged happens through the division of certain cells who then fuse to existing, undamaged muscle fibers to correct the damage. Different muscle types take different amounts of time to heal and regenerate after it has been damaged. Smooth muscle cells can regenerate with the greatest capacity due to their ability to divide and create many more cells to help out. While cardiac muscle cells hardly regenerate at all due to the lack of specialized cells that aid in repair and regeneration. In skeletal muscle, satellite cells aid in helping restoration after injury. Along with muscles, tendons are very important structures within the human body, and they to can be damaged. However, tendon repair involves fibroblast cells cross-linking collagen fibers that aid in not only reinforcing structural support, but also mechanical support as well (“Understanding Tendon Injury,” 2005). While quite different from muscle repair, tendon repair involves the similarity of reestablishing d...
Intermediate filaments have the least persistence among all cytoskeletal filaments, as they can extend to just less than one micrometer, while actin filaments have persistence to few micrometers and some millimeters for microtubules. However, the special packaging steps for intermediate filaments make them actually difficult to break. Examples for intermediate filaments are nuclear lamins, keratin and neurofilaments.
Marfan syndrome is an autosomal dominant disorder resulting from mutations in the gene fibrillin-1 (FBN1) found on chromosome 15 (McKusick V, O'Neill M, 2013). At least 140 different mutations of this gene have been recorded since 2008 (Frey R, Lutwick L, 2009). The FBN1 gene regulates the manufacturing of the fibrillin-1 protein that assists in constructing fibrous filaments which are present in portions of the fibers in connective tissue (Frey R, Lutwick L, 2009). Those filaments manage the discharge of growth factors or protein molecules which prompt the reproduction and growth of cells (Frey R, Lutwick L, 2009). In healthy individuals, the filaments discharge growth factors at the right moment but those who have Marfan syndrome are faced with the dilemma of growth factors being discharged too soon. The early release of growth factors results in fragile connective tissue and the uncommonly lengthy limbs of those with the disorder.
receptor complex site. After I design an analog of Tamoxifen, I will then use the Gaussian 03W
Albumin is a common protein in humans important for checking the health and detecting diseases. With a molecular weight of 65,000 and a density of 3.5-5.0 g/dL, it is made in the liver and released into the blood [1] [2]. Albumin has varieties of function. It maintains homeostasis to balance the amount of blood in the blood vessels [2] [4]. Albumin has a globular structure therefore it can form a colloid when mixed with water. Albumin is used for transporting drugs, lipids, and hormones by colloid osmotic pressure. Most colloid osmotic pressure comes from albumin [4]. Colloid osmotic pressure help to bind to both endogenous and exogenous substances. Drugs and other substances bind to albumin in the bloodstream so that the drug bound albumin can transport to the liver in order to make the drugs and substances less toxic to the target tissues and the water soluble substances. A lower count of albumin can result in a diseased state [4]. Albumin also can affect platelet system in the body. It can control blood clotting by binding arachidonic acid. This decrease production of thromboxane A2 and the activity of antithrombin increases and terminate clotting [1]. Blood clotting is important because it maintain permeability through vessels. Albumin is also important factor for metabolizing and detoxification drug and substances in our body [4].
The epidermis, which is the outer layer of the skin, is made up of four to five layers in some parts (Shier, Butler, & Lewis, 2009). In the majority of the areas, just four layers can be differentiated: the stratum basale, stratum spinosum, stratum granulosum, and stratum corneum (p.119). Another layer is the stratum lucidum which can be found in the thicker part of the skin of the palms and ...
The cytoskeleton is made up of three different types of filaments, actin filaments, intermediate filaments and microtubules. Actin filaments are the thinnest, they are also known as microfilaments. They create a band under the plasma membrane, this gives strength to the cell and links transmembrane proteins such as cell surface receptors to cytoplasmic proteins. Intermediate filaments include keratins, lamins, neurofilaments and vimentins. Keratins form hooves, horns and hair and are found in epithelial cells. Lamins form a type of mesh that ‘stabilizes the inner membrane of the nuclear envelope’ (Biology Pages). Neurofilaments bring strength to the axons of neurons and vimentins provide mechanical support to cells – particularly muscles. The cytoskeleton is also involved in cell
For example, some of the proteins contain pleckstrin homology domains that bind phosphoinositide and others contain C2 domains that bind membrane lipids in the presence of Ca2+, some proteins contain positively charged regions that bind to negatively charged phosphoglycerides and others contain covalently attached fatty acyl groups or prenyl groups that anchor them to membranes. Another example is Annexin shows Ca2+ dependent binding to the cytosolic surfaces of cell membranes. Ca2+ ions bind to the iface of each annexin and this promote protein–lipid interactions through a combination of electrostatic and hydrophobic mechanisms. The same result has been shown by crystallographic studies with phosphoglyceride analogs, suggested that some of the bound Ca2+ ions may bind directly to the oxygens of phospholipid head groups. Addition to this, adjacent membrane lipids that do not bind proteins directly may modulate the protein–lipid interactions, the binding of proteins to membrane surfaces may promote further changes in the structure and function of the proteins, and groups of proteins that bind to the same membrane surface may interact with each other to produce complex membrane
Sperry, R. W. (1963, October 15). Chemoaffinity in the Orderly Growth of Nerve Fiber Patterns and Connection. Natioanl Academy of Science, 50(4), 703-710.
In its nature, collagen is like the backbone of the skin and is responsible for its elasticity and structure. It’s also responsible for replacement of dead skin cells with new ones giving the skin a radiant
If we examine the detailed structures of many transmembrane proteins, we see that they often have three different domains, two hydrophilic and one hydrophobic .(fig 1&2) A hydrophilic domain (consisting of hydrophilic amino acids) at the N-terminus pokes out in the extracellular medium, a hydrophobic domain in the middle of the amino acid chain, often only 20-30 amino acids long, is threaded through the plasma membrane, and a hydrophilic domain at the C-terminus protrudes into the cytoplasm. The transmembrane domain, because it is made of amino acids having hydrophobic side chains, exists comfortably in the hydrophobic inner layers of the plasma membrane. Because these transmembrane domains anchor many proteins in the lipid bilayer, these proteins are not free-floating and cannot be isolated and purified biochemically without first dissolving away the lipid bilayer with detergents. (Indeed, much of the washing we do in our lives is necessitated by the need to solubilize proteins that are embedded in lipid membranes using detergents!)