Chain Proteins (chain + protein)

Distribution by Scientific Domains


Selected Abstracts


Inducible lineage tracing of Pax7-descendant cells reveals embryonic origin of adult satellite cells

GENESIS: THE JOURNAL OF GENETICS AND DEVELOPMENT, Issue 7 2010
Christoph Lepper
Descendants of E9.5 Pax7-expressing (in red, ,-gal+) central dermomyotome cells contribute to myofibers (in green, MF-20+, a myosin heavy chain protein) in the E16.5 mouse embryo. Nuclei are blue (DAPI). The ,-gal+/MF-20_ cells that are intermingled with myofibers are likely myogenic progenitors. See the article by Lepper and Fan in this issue. [source]


Decreased TCR , -chain expression in T cells from patients with acquired aplastic anaemia

BRITISH JOURNAL OF HAEMATOLOGY, Issue 1 2007
Elena E. Solomou
Summary In aplastic anaemia, T cells have a central role in the pathophysiology of bone marrow destruction. This study showed that T cells from patients with aplastic anaemia expressed decreased T-cell receptor (TCR) , -chain protein and mRNA levels compared to healthy controls. Patients with decreased TCR , -chain showed an abnormal response in intracellular calcium following stimulation through the TCR. We also observed an altered pattern of the transcription factors CREM, and Elf-1 that are implicated in , -chain transcription. We concluded that TCR , -chain expression was decreased in the majority of patients with aplastic anaemia, regardless of disease activity or treatment status. [source]


Transforming growth factor-,1-regulated proteins in human endothelial cells identified by two-dimensional gel electrophoresis and mass spectrometry

PROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 4 2004
Marta Lomnytska
Abstract Transforming growth factor-, (TGF,) is a potent regulator of angiogenesis affecting proliferation, differentiation and migration of endothelial cells. The effect of TGF, on endothelial cells depends on the origin of the cells and on the experimental conditions. Global analysis of TGF, signalling is expected to unveil mechanisms of this variability and identify novel targets of the growth factor. Here, we report proteome profiling of human microvascular endothelial cells obtained from dermis, which were treated with TGF,1 and compared to nontreated cells. We identified 54 proteins affected by TGF,1 using two-dimensional gel electrophoresis and peptide mass fingerprinting. Thirteen of the identified proteins are involved in various signalling processes. Seven proteins are involved in cytoskeleton rearrangements and six are involved in regulation of metabolism. Ten proteins were identical to predicted hypothetical proteins with no assigned functions. In agreement with the effect of TGF,1 on components of the cytoskeleton, TGF,1 induces actin cytoskeleton rearrangements. TGF,1 also affected expression of E2F6, p57Kip2, G(q),, hnRNP A1 and myosin light chain proteins as shown by immunoblotting. Down-regulation of the transcriptional repressor E2F6 by TGF,1 correlated with a weak growth-inhibitory activity of TGF,1 on HMVEC-d cells. Twenty-five of the identified proteins have not previously been described as being regulated by TGF,1, providing new insights into TGF,1 signalling in endothelial cells. [source]


Synthesis and assembly of a full-length human monoclonal antibody in algal chloroplasts

BIOTECHNOLOGY & BIOENGINEERING, Issue 4 2009
Miller Tran
Abstract Monoclonal antibodies can be effective therapeutics against a variety of human diseases, but currently marketed antibody-based drugs are very expensive compared to other therapeutic options. Here, we show that the eukaryotic green algae Chlamydomonas reinhardtii is capable of synthesizing and assembling a full-length IgG1 human monoclonal antibody (mAb) in transgenic chloroplasts. This antibody, 83K7C, is derived from a human IgG1 directed against anthrax protective antigen 83 (PA83), and has been shown to block the effects of anthrax toxin in animal models. Here we show that 83K7C heavy and light chain proteins expressed in the chloroplast accumulate as soluble proteins that assemble into complexes containing two heavy and two light chain proteins. The algal-expressed 83K7C binds PA83 in vitro with similar affinity to the mammalian-expressed 83K7C antibody. In addition, a second human IgG1 and a mouse IgG1 were also expressed and shown to properly assemble in algal chloroplast. These results show that chloroplasts have the ability to fold and assemble full-length human mAbs, and suggest the potential of algae as a platform for the cost effective production of complex human therapeutic proteins. Biotechnol. Bioeng. 2009; 104: 663,673 © 2009 Wiley Periodicals, Inc. [source]


Expression of antibodies using single-open reading frame vector design and polyprotein processing from mammalian cells

BIOTECHNOLOGY PROGRESS, Issue 3 2009
Yune Z. Kunes
Abstract We describe a novel polyprotein precursor-based approach to express antibodies from mammalian cells. Rather than expressing heavy and light chain proteins from separate expression units, the antibody heavy and light chains are contained in one single-open reading frame (sORF) separated by an intein gene fused in frame. Inside mammalian cells this ORF is transcribed into a single mRNA, and translated into one polypeptide. The antibody heavy and light chains are separated posttranslationally, assembled into the functional antibody molecule, and secreted into culture medium. It is demonstrated that Pol I intein from P. horikoshii mediates protein splicing and cleavage reactions in mammalian cells, in the context of antibody heavy and light chain amino acid sequences. To allow the separation of antibody heavy chain, light chain, and the intein, we investigated a number of intein mutations designed to inhibit intein-mediated splicing but preserve cleavage reactions. We have also designed constructs in which the signal peptide downstream from intein has altered hydrophobicity. The use of some of these mutant constructs resulted in more efficient antibody secretion, highlighting areas that can be further explored in improving such an expression system. An antibody secreted using one of the sORF constructs was characterized. This antibody has correct N-terminal sequences for both of its heavy and light chains, correct heavy and light chain MW as well as intact MW as measured by mass spectrometry. Its affinity to antigen, as measured by surface plasmon resonance (SPR), is indistinguishable from that of the same antibody produced using conventional method. © 2009 American Institute of Chemical Engineers Biotechnol. Prog., 2009 [source]