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Neuromelanin - Wikipedia. 5,6-dihydroxyindole, the monomer out of which neuromelanin polymers are formed.

Neuromelanin - Wikipedia

Neuromelanin (NM) is a dark pigment found in the brain which is structurally related to melanin. It is a polymer of 5,6-dihydroxyindole monomers. [citation needed] Neuromelanin is expressed in large quantities in catecholaminergic cells of the substantia nigra pars compacta and locus coeruleus, giving dark color to the structures.[1] Importance in humans[edit] Neuromelanin is found in higher concentrations among humans than in other primates.[1] Neuromelanin-containing neurons in the substantia nigra undergo neurodegeneration during Parkinson's disease. Synthetic pathways[edit] Neuromelanin is directly biosynthesized from L-DOPA, precursor to dopamine, by tyrosine hydroxylase (TH) and aromatic acid decarboxylase (AADC).

Related disease[edit] Motor symptoms of Parkinson's disease are caused by cell death in the substantia nigra, which may be partly due to oxidative stress. L-DOPA - Wikipedia. Medical use[edit] In addition, L-DOPA, co-administered with a peripheral DDCI, has been investigated as a potential treatment for restless leg syndrome.

L-DOPA - Wikipedia

However, studies have demonstrated "no clear picture of reduced symptoms".[8] The two types of response seen with administration of L-DOPA are: The short-duration response is related to the half-life of the drug.The longer-duration response depends on the accumulation of effects over at least two weeks, during which ΔFosB accumulates in nigrostriatal neurons. In the treatment of Parkinson's disease, this response is evident only in early therapy, as the inability of the brain to store dopamine is not yet a concern.

Max Planck Institute of Colloids and Interfaces. The byssus threads of the common mussel are produced by a combination of self-assembly processes and biologically active steps March 01, 2017 The chemical industry can learn a lot from the common mussel.

Max Planck Institute of Colloids and Interfaces

Not only are the mollusc’s mother of pearl and tough threads with which it clings to the seafloor remarkable, but the way in which these materials are produced could also serve as a blueprint for the environmentally friendly production of complex polymer structures. Scientists at the Max Planck Institute of Colloids and Interfaces have gained the first insights into how mussel attachment fibres, known as byssus threads, are produced in the mollusc foot. They discovered that many steps in this process proceed autonomously, i.e. without any active intervention by the mussel. ASCL1 - Wikipedia. Achaete-scute homolog 1 is a protein that in humans is encoded by the ASCL1 gene.[3][4] Because it was discovered subsequent to studies on its homolog in Drosophila, the Achaete-scute complex, it was originally named MASH-1 for mammalian achaete scute homolog-1.[5] Function[edit] This gene encodes a member of the basic helix-loop-helix (BHLH) family of transcription factors.

ASCL1 - Wikipedia

The protein activates transcription by binding to the E box (5'-CANNTG-3'). Dimerization with other BHLH proteins is required for efficient DNA binding. This protein plays a role in the neuronal commitment and differentiation and in the generation of olfactory and autonomic neurons. Role in neuronal commitment[edit] Development of the vertebrate nervous system begins when the neural tube forms in the early embryo. Mesenchyme - Wikipedia. Mesenchyme is a type of tissue characterized by loosely associated cells that lack polarity and are surrounded by a large extracellular matrix.

Mesenchyme - Wikipedia

Development[edit] The mesenchyme originates from the mesoderm. From the mesoderm, the mesenchyme appears as an embryologically primitive "soup". NG2 proteoglycan - Wikipedia. NG2, or neural/glial antigen 2, is a rat integral membrane proteoglycan found in the plasma membrane of many diverse cell types.[1] Homologous proteins in other species include human CSPG4, also known as melanoma-associated chondroitin sulfate proteoglycan (MCSP), Mouse AN2, and Sea urchin ECM3.[2] This single-pass transmembrane molecule may be plasma membrane-bound or secreted and associated with the extracellular matrix.[3] It is believed to play a role in functions such as cell adhesion, cell-cell and cell-ECM communication, migration and metastasis, proliferation, and axonal growth, guidance and regeneration.

NG2 proteoglycan - Wikipedia

NG2-positive cells include oligodendrocyte progenitor cells (OPCs) and other progenitor cell populations, such as chondroblasts, myoblasts, and pericytes, as well as several different tumors including glioblastoma multiforme and melanoma.[4][5][6][7][8][9][10] Structure[edit] NG2 cDNA contains 8,071 nucleotides corresponding to 2,325 amino acids.

Glial fibrillary acidic protein - Wikipedia. Glial fibrillary acidic protein (GFAP) is a protein that is encoded by the GFAP gene in humans.[3] Glial fibrillary acidic protein is an intermediate filament (IF) protein that is expressed by numerous cell types of the central nervous system (CNS) including astrocytes[4] and ependymal cells.[5] GFAP has also been found to be expressed in glomeruli and peritubular fibroblasts taken from rat kidneys[6] Leydig cells of the testis in both hamsters[7] and humans,[8] human keratinocytes,[9] human osteocytes and chondrocytes[10] and stellate cells of the pancreas and liver in rats.[11] First described in 1971,[12] GFAP is a type III IF protein that maps, in humans, to 17q21.[13] It is closely related to its non-epithelial family members, vimentin, desmin, and peripherin, which are all involved in the structure and function of the cell’s cytoskeleton.

Glial fibrillary acidic protein - Wikipedia

Structure[edit] Type III intermediate filaments contain three domains, named the head, rod and tail domains. Disease states[edit] Sign In. Type IV collagen C4 domain - Wikipedia. The collagen IV C4 domain contains 12 cysteines, and all of them are involved in disulphide bonds.

Type IV collagen C4 domain - Wikipedia

It folds into a tertiary structure with predominantly beta-strands. The collagen IV C4 domain is composed of two similarly folded subdomains stabilised by 3 intrachain dissulphide bonds involving the following pairs: C1-C6, C2-C5, and C3-C4. Each subdomain represents a compact disulphide-stabilised triangular structure, from which a finger-like hairpin loop projects into an incompletely formed six-stranded beta-sheet of an adjacent subdomain of the same or of an adjacent chain clamping the subdomains tightly together.[1][2][3] ^ Jump up to: a b Than ME, Henrich S, Huber R, Ries A, Mann K, Kuhn K, Timpl R, Bourenkov GP, Bartunik HD, Bode W (May 2002).

Multimerization. THE INTERACTIVE FLY. Desai, C.

THE INTERACTIVE FLY

J., Popova, E. and Zinn, K. (1994). A Drosophila receptor tyrosine phosphatase expressed in the embryonic CNS and larval optic lobes is a member of the set of proteins bearing the "HRP" carbohydrate epitope. J. Evolution of Extracellular Matrix - Google Books. Extracellular matrix dynamics and functions in the social amoeba Dictyostelium: A critical review. Cephalopod Biology. Fibrillin (IPR011398) < InterPro. Microfibril-associated glycoprotein (IPR008673) < InterPro. Research Interests. Bilateria - Wikipedia. Except for a few phyla (i.e. flatworms and gnathostomulids), bilaterians have complete digestive tracts with a separate mouth and anus.

Bilateria - Wikipedia

Some bilaterians lack body cavities (acoelomates, i.e. Platyhelminthes, Gastrotricha and Gnathostomulida), while others display primary body cavities (deriving from the blastocoel, as pseudocoel) or secondary cavities (that appear de novo, for example the coelom). [3] [4] Evolution[edit] Illustration of the different types of symmetry in lifeforms (Field Museum, Chicago). Bilateria - Buscar con Google. The evolution of tenascins and fibronectin. - Abstract - Europe PMC. Tenascins are extracellular matrix glycoproteins that act both as integrin ligands and as modifiers of fibronectin-integrin interactions to regulate cell adhesion, migration, proliferation and differentiation.

In tetrapods, both tenascins and fibronectin bind to integrins via RGD and LDV-type tripeptide motifs found in exposed loops in their fibronectin-type III domains. We previously showed that tenascins appeared early in the chordate lineage and are represented by single genes in extant cephalochordates and tunicates. Here we have examined the genomes of the coelacanth Latimeria chalumnae, the elephant shark Callorhinchus milii as well as the lampreys Petromyzon marinus and Lethenteron japonicum to learn more about the evolution of the tenascin gene family as well as the timing of the appearance of fibronectin during chordate evolution.

BMP-1 Regulation of TGF-beta Activity: R&D Systems. Bone morphogenetic protein 1/tolloid-like protein (IPR015446) < InterPro. CYR61 - Wikipedia. Cysteine-rich angiogenic inducer 61 (CYR61) or CCN family member 1 (CCN1), is a matricellular protein that in humans is encoded by the CYR61 gene.[3] CYR61 is a secreted, extracellular matrix (ECM)-associated signaling protein of the CCN family (CCN intercellular signaling protein).[4][5] CYR61 is capable of regulating a broad range of cellular activities, including cell adhesion, migration, proliferation, differentiation, apoptosis, and senescence through interaction with cell surface integrin receptors and heparan sulfate proteoglycans. During embryonic development, CYR61 is critical for cardiac septal morphogenesis, blood vessel formation in placenta, and vascular integrity. In adulthood CYR61 plays important roles in inflammation and tissue repair, and is associated with diseases related to chronic inflammation, including rheumatoid arthritis, atherosclerosis, diabetes-related nephropathy and retinopathy, and many different forms of cancers.

Fibulin - Wikipedia. Fibulin (FY-beau-lin) (now known as Fibulin-1 FBLN1) is the prototypic member of a multigene family, currently with seven members. Fibulin-1 is a calcium-binding glycoprotein. In vertebrates, fibulin-1 is found in blood and extracellular matrices. In the extracellular matrix, fibulin-1 associates with basement membranes and elastic fibers. The association with these matrix structures is mediated by its ability to interact with numerous extracellular matrix constituents including fibronectin, proteoglycans, laminins and tropoelastin. In blood, fibulin-1 binds to fibrinogen and incorporates into clots. Fibulins are secreted glycoproteins that become incorporated into a fibrillar extracellular matrix when expressed by cultured cells or added exogenously to cell monolayers.[2][3] The five known members of the family share an elongated structure and many calcium-binding sites, owing to the presence of tandem arrays of epidermal growth factor-like domains.

Mesangium - Wikipedia. Renal corpuscle. The entire structure is the renal corpuscle. The blue structure (A) is the Bowman's capsule (2 and 3). The pink structure is the glomerulus with its capillaries. At the left, blood flows from the afferent arteriole (9), through the capillaries (10), and out the efferent arteriole (11). The mesangium (5a, 5b) is the purple structure inside the glomerulus between the capillaries and extending outside the glomerulus. 263. FBN2 gene - Genetics Home Reference. Fibrillin - Wikipedia. Fibrillin is a glycoprotein, which is essential for the formation of elastic fibers found in connective tissue.[2] Fibrillin is secreted into the extracellular matrix by fibroblasts and becomes incorporated into the insoluble microfibrils, which appear to provide a scaffold for deposition of elastin.[3] Clinical aspect[edit] Mutations in FBN1 and FBN2 are associated with adolescent idiopathic scoliosis .[4] In vivo fragmentation of heparan sulfate by heparanase overexpression renders mice resistant to amyloid protein A amyloidosis.

Table 19-5, Some Types of Collagen and Their Properties - Molecular Biology of the Cell - NCBI Bookshelf. Table 19-4, Some Common Proteoglycans - Molecular Biology of the Cell - NCBI Bookshelf. Neurogenic locus Notch 1 (IPR022362) < InterPro < EMBL-EBI. Family Short name: Notch_1 Family relationships. Proteinase inhibitor I35b (TIMP), C-terminal (IPR027465) < InterPro < EMBL-EBI. Matrix metalloproteinase-9 (IPR028688) < InterPro < EMBL-EBI. Tenascin-R (IPR033079) < InterPro < EMBL-EBI. Tenascin-C (IPR033078) < InterPro < EMBL-EBI. Tenascin-W (IPR033080) < InterPro < EMBL-EBI. None. Tenascin-X (IPR033081) < InterPro < EMBL-EBI. Tenascin-R (IPR033079) < InterPro < EMBL-EBI. EMI domain (IPR011489) < InterPro < EMBL-EBI.

Domain Short name: EMI_domain Domain relationships None. Description The EMI domain, first named after its presence in proteins of the EMILIN family, is a small cysteine-rich module of around 75 amino acids. The EMI domain possesses six highly conserved cysteines residues, which likely form disulphide bonds. FAS1 domain (IPR000782) < InterPro < EMBL-EBI. Domain. Recognition molecules and neural repair. Hyaluronan. Bench-to-bedside review: The role of glycosaminoglycans in respiratory disease. Hyaluronan. Figure 19-53, The structure of a fibronectin dimer - Molecular Biology of the Cell - NCBI Bookshelf. RGD and other recognition sequences for integrins. An Error Occurred Setting Your User Cookie.

Anti Keratan sulfate (373E1) Monoclonal antibody / Cosmo Bio. Figure 19-47, The intracellular and extracellular events in the formation of a collagen fibril - Molecular Biology of the Cell - NCBI Bookshelf. Heparan sulfate - Wikipedia. Faculty. mIRN21 - Wikipedia. Chondroitin and Keratin Sulfate - Wheeless' Textbook of Orthopaedics. Choanoflagellate monosiga brevicollis: Topics by Science.gov. GlycoWord / Evolution-ES-A02. Keratan sulfate - Wikipedia. Learn Science at Scitable. Gla domain - Wikipedia. Glycosaminoglycans and Proteoglycans.

Fibronectin Molecular Interactions - tenascin. PTPRC - Wikipedia. CD44 - Wikipedia. EMI domain - Wikipedia. Tenascin - Wikipedia. FLNA - Wikipedia. Fasciclin domain. EMI domain - Wikipedia. Laboratory Investigation - The role of the fibrocyte, a bone marrow-derived mesenchymal progenitor, in reactive and reparative fibroses. Matrix metalloproteinase - Wikipedia. Thrombospondin - Wikipedia. Annexin A2 - Wikipedia. Perlecan - Wikipedia. Basement membrane - Wikipedia. Epithelial–mesenchymal transition - Wikipedia. CYR61 - Wikipedia. Chondroitin sulfate proteoglycan - Wikipedia. The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein– protein interactions independent of carbohydrate moiety. The Extracellular Matrix of Animals - Molecular Biology of the Cell - NCBI Bookshelf. Box 1 : Hyaluronan: from extracellular glue to pericellular cue : Nature Reviews Cancer.

Heparan sulfate - Wikipedia. Glycosaminoglycans and Proteoglycans. Chondroitin sulfate proteoglycan. Glycosaminoglycan - Wikipedia. Tenascin; Cytotactin; Hexabrachion; Tenascin-C.