Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Elastin-binding protein

Yanagisawa, H., Davis, E. C., Starcher, B. C., Ouchi, T., Yanagisawa, M., Richardson, J. A., and Olsen, E. N. (2002). Fibulin-5 is an elastin-binding protein essential for elastic fibre development in vivo. Nature 415, 168-171. [Pg.436]

Hinek, A., Keeley, F. W., and Callahan, J. (1995). Recycling of the 67-kDa elastin binding protein in arterial myocytes is imperative for secretion of tropoelastin. Exp. Cell Res. 220, 312-324. [Pg.456]

A. Caciotti, M. A. Donati, T. Bardelli, A. d Azzo, G. Massai, L. Luciani, E. Zammarchi, and A. Morrone, Primary and secondary elastin-binding protein defect leads to impaired elastogenesis in fibroblasts from GMl-gangliosidosis patients. Am. J. Pathol, 167 (2005) 1689-1698. [Pg.463]

Elastin VGVAPG Elastin-binding protein Maintaining elasticity in vascular smooth muscle cells [7]... [Pg.199]

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. [Pg.431]

Privitera, S., Prody, C. A., Callahan, J. W., and Hinek, A. (1998). The 67-kDa enzymatically inactive alternatively spliced variant of beta-galactosidase is identical to the elastin/laminin-binding protein./. Biol. Chem. 273, 6319-6326. [Pg.459]

A. Hinek, M. Rabinovitch, F. Keeley, Y. Okamura-Oho, and J. Callahan, The 67-kD elastin/laminin-binding protein is related to an enzymatieally inactive, alternatively spliced form of beta-galactosidase, J. Clin. Invest., 91 (1993) 1198-1205. [Pg.463]

R.P Mecham, L. Whitehouse, M. Hay, A. Hinek, M.P. Sheetz, Ligand affinity of the 67-kD elastin/laminin binding protein is modulated by the protein s lectin domain visualization of elastin/ laminin-receptor complexes with gold-tagged ligands, J. Cell Biol. 113 (1991) 187-194. [Pg.57]

Elastin gene expression in rat lung fibroblasts was selectively inhibited by okadaic acid (Berk et al. 1996). In vitro, 5 nM had minimal effects (91 % control values) on elastin mRNA levels okadaic acid at 25 nm and 50 nm decreased elastin mRNA to 23 and 6 % of control levels, respectively. Inhibition of protein synthesis with cycloheximide did not block okadaic add-induced suppression of elastin mRNA levels. Okadaic acid had minimal effect of rat GTP-binding protein mRNA levels. Sodium orthovanadate, a tyrosine phosphatase inhibitor, induced minor decreases in elastin mRNA levels at micromolar concentration. Protein kinase C desensitisation by prolonged exposure to phorbol 12-myristate 13-acetate did not alter the effect of okadaic add on elestin mRNA levels. [Pg.399]

Protein engineering strategies have also allowed the incorporation of biological function into elastin-like protein polymers and SELPs. The incorporation of cell-binding amino acid seqnences, such as RGD (82,142) and REDV (from the CS5 domain of fibronectin) (66) (Table 2), permits endothelial cell adhesion to... [Pg.3540]

The extracellular matrix of vascular wall cells, a complex array of collagen, elastin, adhesion proteins, and proteoglycans (see Chapter 13), mediates a variety of functions with significance for the development of atherosclerosis and cardiovascular disease. These include blood cell adhesion, lipoprotein binding, vascular wall... [Pg.355]

A. Minato, H. Ise, M. Goto, T. Akaike, Cardiac differentiation of embryonic stem cells by substrate immobilization of insulin-like growth factor binding protein 4 with elastin-like polypeptides, Biomaterials 33 (2012) 515-523. [Pg.111]

Albumen has the largest number of acid and basic groups. It is the most soluble of the proteins present in a hide. The albumen is not a fibrous material, however, and therefore has no value in the leather. Keratin is the protein of the hair and the outermost surface of the hide. Unless the hair is desired for the final product it is removed by chemical and/or physical means. The elastin has Htde acid- or base-binding capacity and is the least soluble of the proteins present. The lack of reactivity of the elastin is a detriment for most leather manufacture. The presence of elastin in the leather greatly limits the softness of the leather. [Pg.82]


See other pages where Elastin-binding protein is mentioned: [Pg.74]    [Pg.441]    [Pg.443]    [Pg.404]    [Pg.414]    [Pg.45]    [Pg.429]    [Pg.74]    [Pg.441]    [Pg.443]    [Pg.404]    [Pg.414]    [Pg.45]    [Pg.429]    [Pg.137]    [Pg.109]    [Pg.84]    [Pg.456]    [Pg.179]    [Pg.200]    [Pg.255]    [Pg.47]    [Pg.47]    [Pg.251]    [Pg.266]    [Pg.38]    [Pg.97]    [Pg.99]    [Pg.121]    [Pg.121]    [Pg.121]    [Pg.106]    [Pg.65]    [Pg.508]    [Pg.98]    [Pg.194]    [Pg.159]   
See also in sourсe #XX -- [ Pg.74 ]

See also in sourсe #XX -- [ Pg.414 ]




SEARCH



Elastin

© 2024 chempedia.info