Detail of "37213-56-2"

Reference

Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPARg

Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPARg. Hu, Erding; Kim, Jae Bum; Sarraf, Pasha; Spiegelman, Bruce M. ( Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA). Science (Washington, D. C. 37213-56-2 and 142243-02-5 are cas registry numbers. These chemicals are also mentioned in this article.), 274(5295), 2100-2103 (English) 1996 American Association for the Advancement of Science. CODEN: SCIEAS. ISSN: 0036-8075. DOCUMENT TYPE: Journal CA Section: 13 (Mammalian Biochemistry) Adipocyte differentiation is an important component of obesity and other metabolic diseases. This process is strongly inhibited by many mitogens and oncogenes. Several growth factors that inhibit fat cell differentiation caused mitogen-activated protein (MAP) kinase-mediated phosphorylation of the dominant adipogenic transcription factor peroxisome proliferator-activated receptor g (PPARg) and redn. of its transcriptional activity. Expression of PPARg with a nonphosphorylatable mutation at this site (serine-112) yielded cells with increased sensitivity to ligand-induced adipogenesis and resistance to inhibition of differentiation by mitogens. These results indicate that covalent modification of PPARg by serum and growth factors is a major regulator of the balance between cell growth and differentiation in the adipose cell lineage. .

Molecular Dissection of Interactions between Components of the Alternative Pathway of Complement and Decay Accelerating Factor (CD55)

Molecular Dissection of Interactions between Components of the Alternative Pathway of Complement and Decay Accelerating Factor (CD55).Several substances are used for example 37213-56-2 and 7439-95-4 which are their cas registry numbers. Harris, Claire L.; Abbott, Rachel J. M.; Smith, Richard A.; Morgan, B. Paul; Lea, Susan M. (Complement Biology Group, Department of Medical Biochemistry and Immunology, School of Medicine, Cardiff University, Cardiff CF14 4XN, UK). Journal of Biological Chemistry, 280(4), 2569-2578 (English) 2005 American Society for Biochemistry and Molecular Biology. CODEN: JBCHA3. ISSN: 0021-9258. DOCUMENT TYPE: Journal CA Section: 15 (Immunochemistry) The complement regulatory protein decay accelerating factor (DAF; CD55), inhibits the alternative complement pathway by accelerating decay of the convertase enzymes formed by C3b and factor B. the authors show, using surface plasmon resonance, that in the absence of Mg2+, DAF binds C3b, factor B, and the Bb subunit with low affinity (KD, 14, 44, and 20 mM, resp.). In the presence of Mg2+, DAF bound Bb or the von Willebrand factor type A subunit of Bb with higher affinities (KD, 1.3 and 2.2 mM, resp.). Interaction with the proenzyme C3bB was investigated by flowing factor B across a C3b-coated surface in the absence of factor D. The dissocn. rate was dependent on the time of incubation, suggesting that a time-dependent conformational transition stabilized the C3b-factor B interaction. Activation by factor D (forming C3bBb) increased the complex half-life; however, the enzyme became susceptible to rapid decay by DAF, unlike the proenzyme, which was unaffected. A convertase assembled with cobra venom factor and Bb was decayed by DAF, albeit far less efficiently than C3bBb. DAF did not bind cobra venom factor, implying that Bb decay is accelerated, at least in part, through DAF binding of this subunit. It is likely that DAF binds the complex with higher affinity/avidity, promoting a conformational change in either or both subunits accelerating decay. Such anal. of component and regulator interactions will inform the authors' understanding of inhibitory mechanisms and the ways in which regulatory proteins cooperate to control the complement cascade. .