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Collagen inhibition

LAFETINA eg, REEP B, Chang KJ. Treatment of human platelets with trypsin, thrombin or collagen inhibits the pertussis toxin-induced ADP-ribosylation of a 41-kDaprcytein ProcNatl Acad Sci USA 83 5880-5883, 1986a... [Pg.227]

Han J, Ohno N, Pasco S, Monboisse J-C, Borel JP, Kefalides NA (1997) A cell binding domain from the a3 chain of type IV collagen inhibits proliferation of melanoma cells. J Biol Oiem 272 20395-20401. doi 10.1074/jbc.272.33.20395... [Pg.274]

KOYAMA, H., RAINES, E. W., BORNFELDT, K. E., ROBERTS, 1. M. ROSS, R. 1996. Fibrillar collagen inhibits arterial smooth muscle proliferation through regulation of Cdk2 inhibitors. Cell, 87, 1069-78. [Pg.148]

Itazigrel (137) is an antithrombotic compound because of its inhibition of platelet aggregation induced by collagen. It is synthe.sizcd froin l-bromo-l-(4-methoxy)benzoyl-4-methoxytol-uene (135) by reaction in the usual way with triflucffothioacetamide (136) to give itazigrel 471. [Pg.96]

Restin (a1 Collagen IV NC1 fragment) Inhibits EC proliferation and induces EC apoptosis... [Pg.85]

Figure 10.4. Effect on apatite-collagen isotopic fractionation due to inhibition of amino acid production and preferred use of exogenous amino acids. Carnivore and herbivore, both based on C3 plants, have similar bulk isotopic composition of total edible tissues (T), leading to similar 5 C for apatite carbonate (AP). Collagen (CO) of carnivore is more enriched in Cthan that of herbivore, because of preferential utilization of amino acids derived from protein (P) of herbivore flesh in construction of carnivore s proteins. C ss = assimilated carbon. Figure 10.4. Effect on apatite-collagen isotopic fractionation due to inhibition of amino acid production and preferred use of exogenous amino acids. Carnivore and herbivore, both based on C3 plants, have similar bulk isotopic composition of total edible tissues (T), leading to similar 5 C for apatite carbonate (AP). Collagen (CO) of carnivore is more enriched in Cthan that of herbivore, because of preferential utilization of amino acids derived from protein (P) of herbivore flesh in construction of carnivore s proteins. C ss = assimilated carbon.
ADCOCKS c, COLLIN P and BUTTLE D J (2002) Catechins from green tea Camellia sinensis) inhibit bovine and human cartilage proteoglycan and type 11 collagen degradation in vitro , JNutr, 132 (3), 341-6. [Pg.150]

CIA in IFNyR null mice DBA/1 mice AMD3100 (JM3100) i Inhibition of monocyte migration to CXCL12a. Reduction of DTH response to collagen type II. 208... [Pg.174]

Vierboom MP, Zavodny PJ, Chou CC, et al. Inhibition of the development of collagen-induced arthritis in rhesus monkeys by a small molecular weight antagonist of CCR5. Arthritis Rheum 2005 52(2) 627-636. [Pg.197]

Nanki T, Urasaki Y, Imai T, et al. Inhibition of fractalkine ameliorates murine collagen-induced arthritis. J Immunol 2004 173(11) 7010-7016. [Pg.198]

Inhibition of IFN-y entails inhibition of fibroblast proliferation and differentiation, subsequent collagen synthesis, and increased expression of MMP-1 to promote degradation of matrix (105). IFN-y also triggers robust T-lymphocyte... [Pg.309]

Fig. 14.1. The Thl/Th2 balance is central to the regulation of normal wound repair. Tissue injury results in the initiation of an inflammatory response, mediated by a variety of cells and their by-products. Immune cells are recruited and cross-regulate the Thl/ Th2 balance that occurs in response to the cytokine environment. This balance is in turn cross-regulated by the chemokine/chemokine-receptor expression profile, which functions to amplify the inflammatory process. Cells residing in the injured tissue release profibrotic mediators, which promote fibroblast activation, proliferation, and differentiation to the myofibroblast phenotype. Myofibroblasts produce collagen to repair damaged tissue, which is an event that is favored by the inhibition of MMP activity. The Thl/Th2 balance is central to whether a normal or aberrant wound-repair process is established A Thl environment promotes normal tissue resolution (fibrinolysis), whereas a Th2 environment maintains the progression of fibrotic disease (excessive collagen deposition). Fig. 14.1. The Thl/Th2 balance is central to the regulation of normal wound repair. Tissue injury results in the initiation of an inflammatory response, mediated by a variety of cells and their by-products. Immune cells are recruited and cross-regulate the Thl/ Th2 balance that occurs in response to the cytokine environment. This balance is in turn cross-regulated by the chemokine/chemokine-receptor expression profile, which functions to amplify the inflammatory process. Cells residing in the injured tissue release profibrotic mediators, which promote fibroblast activation, proliferation, and differentiation to the myofibroblast phenotype. Myofibroblasts produce collagen to repair damaged tissue, which is an event that is favored by the inhibition of MMP activity. The Thl/Th2 balance is central to whether a normal or aberrant wound-repair process is established A Thl environment promotes normal tissue resolution (fibrinolysis), whereas a Th2 environment maintains the progression of fibrotic disease (excessive collagen deposition).
Sauk JJ, Smith T, Silbergeld EK, et al. 1992. Lead inhibits secretion of osteonectin/sparc without significantly altering collagen or hsp47 production in osteoblast-like ros 17/2.8 cells. Toxicol Appl Pharmacol 116(2) 240-247. [Pg.572]

In an attempt to mimic the physiological ratio of collagen type II to hyaluronan in the healthy human NP, Calderon et al. constructed hydrogels scaffolds composed of these two elements in a 9 1 (w/w) ratio [104]. Scaffolds were crosslinked with various concentrations of EDC/NHS, but it was found that 8 mM EDC/NHS resulted in a confined compressive modulus on the order of the native NP, while allowing for optimal rat mesenchymal stem cell (rMSC) viability and proliferation. Additionally, real time PCR results from rMSCs seeded on the scaffolds for 21 days indicated that the scaffolds promoted increased aggrecan expression and inhibited collagen type I expression compared to rMSCs cultured on monolayers. [Pg.215]


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See also in sourсe #XX -- [ Pg.2 , Pg.82 ]




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