Microfibril-associated protein

Microfibril-associated protein-1 (MFAP-1 also known as AMP), MFAP-3, and MFAP-4 (also known as MAGP-36) colocalize with microfibrils and elastic fibers in skin and other tissues (Abrams et al, 1995 Hirano et al, 2002 Horrigan et al., 1992 Lausen et al, 1999 Liu et al, 1997 Toyoshima et al, 1999). In aging and immune conditions, microfibrils can associate with amyloid deposits and accumulate a coating of adhesive glycoproteins, such as vitronectin (Dahlback et al, 1990). 

Isogai, Z., Ono, R. N., Ushiro, S., Keene, D. R., Chen, Y., Mazzieri, R., Charbonneau, N. L., Reinhardt, D. P., Rifkin, D. B., and Sakai, L. Y. (2003). Latent transforming growth factor beta-binding protein 1 interacts with fibrillin and is a microfibril-associated protein. / Biol. Chem. 278, 2750-2757. 

Kitahama, S., Gibson, M. A., Hatzinikolas, G., Hay, S., Kuliwaba, J. L., Evdokiou, A., Atkins, G. J., and Findlay, D. M. (2000). Expression of fibrillins and other microfibril-associated proteins in human bone and osteoblast-like cells. Bone 27, 61-67. 

Lausen, M., Lynch, N., Schlosser, A., Tornoe, I., Sackmose, S. G., Teisner, B., Willis, A. C., Crouch, E., Schwaeble, W., and Holmskov, U. (1999). Microfibril-associated protein 4 is present in lung washings and binds to the collagen region of lung surfactant protein D. / Biol. Chem. 274, 32234-32240. 

Liu, W. G., Faraco, J., Qian, C. P., and Francke, U. (1997). The gene for microfibril-associated protein-1 (MFAP1) is located several megabases centromeric to FBN1 and is not mutated in Marfan syndrome. Human Genet. 99, 578-584. 

Fumichi, H., Yamashita, K., Okada, M., Toyoshima, T, Hata, Y, Suzuki, S., Itano, T, Shishibori, T, Tokumitsu, H. and Kobayashi, R. (2000) Identification of tranilast-binding protein as 36-kDa microfibril-associated glycoprotein by dmg affinity chromatography, and its localization in human skin. Biochem. Biophys. Res. Commun. 270, 1002-1008. 

Wool and hair have the most complex structures of any textile fibres. In the paper by Viney, fig. 1 shows how keratin proteins, of which there are more than one type, all having a complicated sequence of amino acids, assemble into intermediate filaments (IFs or microfibrils). But, as shown in Fig. 5a, this is only one part of the story. The microfibrils are embedded in a matrix, as shown in Fig. 5b. The keratin-associated proteins of the matrix contain substantial amounts of cy.stine, which cross-links molecules by -CH2-S-S-CH2- groups. Furthermore, terminal domains (tails) of the IFs, which also contain cystine, project into the matrix and join the cross-linked network. At a coarser scale, as indicated in Fig. 5c, wool is composed of cells, which are bonded together by the cell membrane complex (CMC), which is rich in lipids. As a whole, wool has a multi-component form, which consists of para-cortex, ortho-cortex, meso-cortex (not shown in Fig. 5a), and a multi-layer cuticle. In the para-and meso-cortex the fibril-matrix is a parallel assembly and the macrofibrils, if they are present, run into one another, but in the ortho-cortex the fibrils are assembled as helically twisted macrofibrils, which are clearly apparent in cross-section.s. 

Wood formation is a fundamental biological process of significant economic and commercial interest. During wood formation, most glucose from the carbohydrate metabolism is channeled to cellulose in the secondary cell walls. The cellulose microfibrils associate with hemicellulose, proteins, and lignin to form the strong and flexible biocomposite known as wood. As the main wood component, cellulose is essential for the smrvival of trees and for their exploitation by man. 

The middle lamella consists mainly of pectin and some lignin. The primary cell wall is elastic and contains a mesh of cellulose microfibrils associated with hemicellulose, pectin and proteins. Proteins in the primary wall can perturb the interactions between the cellulose microfibrils and hemicellulose, allowing the... 

Cellulose microfibrils make up the basic framework of the primary wall of young plant cells (3), where they form a complex network with other polysaccharides. The linking polysaccharides include hemicellulose, which is a mixture of predominantly neutral heterogly-cans (xylans, xyloglucans, arabinogalactans, etc.). Hemicellulose associates with the cellulose fibrils via noncovalent interactions. These complexes are connected by neutral and acidic pectins, which typically contain galac-turonic acid. Finally, a collagen-related protein, extensin, is also involved in the formation of primary walls. 

R. P. (1995). Bovine latent transforming growth factor /11-binding protein-2 Molecular cloning, identification of tissue isoforms, and immunolocalization to elastin-associated microfibrils. Mol. Cell. Biol. 15, 6932-6942. 

Calcified scales formed inside the Golgi and then extruded have so far only been found in coccolithophorids. In other forms, the matrix is formed in the Golgi but calcification takes place in the cytoplasm. In some cases, the plates of coccolithophorids calcify inside the T-shaped cisternae where the stem is associated with the Golgi stack while the scale is already forming with its future distal surface facing the stack. The scales of coccolithophorids always consist of two layers of a cellulose network of microfibrils radially and concentrically arranged. The outer layer of the scale is made up of acidic polysaccharides and small amounts of protein, probably containing hydroxy-... 

In contrast to the cell walls of parenchymatous tissues of dicotyledons, those of cereal grains (wheat, barley, etc.) contain very little, or no, pectic substances. The primary walls of most cereal grains have cellulose microfibrils, which are closely associated with glucomannan, and these fibrillar structures are embedded in an amorphous matrix of hemicelluloses, which consists mainly of arabinoxylans and/or P-D-glucans, some of which are cross-linked by phenolic esters and/or proteins (Selvendran,... 

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