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Molecular Weight Complexes (molecular + weight_complex)

Distribution by Scientific Domains
Medical Sciences50%
Life Sciences50%

Kinds of Molecular Weight Complexes

  • high molecular weight complex
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    Selected Abstracts

    Characterization of fibronectin assembly by platelets adherent to adsorbed laminin-111

    JOURNAL OF THROMBOSIS AND HAEMOSTASIS, Issue 5 2006
    J. CHO
    Summary.,Background: Various types of laminin (LN) are ubiquitous components of basement membrane and exposed to blood upon localized damage of vascular endothelial cells. Fibronectin is a plasma protein that is insolubilized into fibrils in a regulated fashion by, for example, lysophosphatidic acid (LPA)-stimulated fibroblasts or platelets spread on supportive adhesive ligands. Objective: To study assembly of plasma fibronectin by LPA-activated platelets adherent to LN-111 via ,6,1 integrin. Results: Platelets adherent to LN-111-bound plasma fibronectin or its N-terminal 70 kD fragment in fibrillar arrays at the periphery of spread platelets under static but not shear conditions. Formation of fibronectin arrays under static conditions was inhibited by co-incubation with the N-terminal 70 kD fragment or with a 49-amino acid peptide that binds to the N-terminal region of fibronectin. Approximately 7000 fibronectin dimers bound per adherent platelet with a Kd of 50 nm. Bound 70 kD fragment was readily solubilized with deoxycholate (DOC), whereas bound fibronectin became progressively insoluble. Bound 70 kD fragment became resistant to DOC extraction after treatment with a cell-impermeable, reducible crosslinker. Crosslinked 70 kD fragment was found in a high molecular weight complex. As with fibroblasts, signaling molecules modulating actin cytoskeletal organization controlled expression of binding sites for the N-terminal 70 kD region of fibronectin on adherent platelets. Conclusions: These results indicate that platelets adherent to LN-111 via ,6,1 support subsequent assembly of fibronectin, but possibly only under conditions of intermittent or stagnant blood flow. [source]

    Actin-like protein 1 (ALP1) is a component of dynamic, high molecular weight complexes in Toxoplasma gondii,

    CYTOSKELETON, Issue 1 2010
    Jennifer L. Gordon
    Abstract Apicomplexan parasites, such as Toxoplasma gondii, rely on actin-based motility for cell invasion, yet conventional actin does not appear to be required for cell division in these parasites. Apicomplexans also contain a variety of actin-related proteins (Arps); however, most of these not directly orthologous to Arps in well-studied systems. We recently identified an apicomplexan-specific member of this family called Actin-Like Protein 1, (ALP1), which plays a role in the assembly of vesicular components recruited to the inner membrane complex (IMC) of daughter cells during cell division. In addition to its enrichment at daughter cell membranes, ALP1 is localized throughout the cytoplasm both diffusely distributed and concentrated in clusters that are detected by fluorescence microscopy, suggesting it forms complexes. Using quantitative optical imaging methods, including fluorescence recovery after photobleaching (FRAP) and fluorescence loss in photobleaching (FLIP), we demonstrated that ALP1 is a component of a large complex, and that it readily exchanges between diffusible and complex-bound forms. Sedimentation and density gradient analyses revealed that ALP1 is found in a freely soluble state as well as high molecular weight complexes. During cell division, ALP1 was dynamically associated with the IMC, suggesting it rapidly cycles between freely diffusible and complex forms during daughter cell assembly. © 2009 Wiley-Liss, Inc. [source]

    SMC Proteins at the Crossroads of Diverse Chromosomal Processes

    IUBMB LIFE, Issue 12 2003
    Rolf Jessberger
    Abstract How should a protein be designed to serve in processes as diverse as chromosome condensation, sister chromatid cohesion, DNA recombination, gene dosage regulation, and perhaps even gene silencing or transcriptional regulation - which occur in both mitosis and meiosis? Such a protein or protein complex needs to bear DNA interaction domains, it needs the capacity to use energy to move DNA, it needs to enter into highly specific protein interactions, it needs to be large enough to link two DNA molecules, it needs to be of sufficient flexibility to cope with different types of chromatin structure, yet it also needs to be rigid enough to pull, push or enclose DNA. SMC proteins fulfill these requirements and form the core units of high molecular weight complexes that act in all those processes, and are essential for some of them. SMC stands for 'Structural Maintenance of Chromosomes', although SMC proteins are not static scaffold proteins merely providing support for a particular chromosome structure. SMC proteins are rather highly dynamic actors, that generate and modulate chromosome structures, affecting a plethora of biological processes. IUBMB Life, 55: 643-652, 2003 [source]

    Differential Aggregation Of The Trembler And Trembler J Mutants Of Peripheral Myelin Protein 22

    JOURNAL OF THE PERIPHERAL NERVOUS SYSTEM, Issue 3 2002
    AR Tobler
    Mutations in the gene encoding the peripheral myelin protein 22 (PMP22), a tetraspan protein in compact peripheral myelin, are one of the causes of inherited demyelinating peripheral neuropathy. Most PMP22 mutations alter the trafficking of the PMP22 protein in Schwann cells, and this different trafficking has been proposed as the underlying mechanism of the disease. To explore this problem further, we compared the aggregation of wild-type Pmp22 with those of the two Pmp22 mutations found in Trembler (Tr) and Trembler J (TrJ) mice. All three Pmp22s can be crosslinked readily as homodimers in transfected cells. Wild-type Pmp22 also forms heterodimers with Tr and TrJ Pmp22, and these heterodimers traffic with their respective mutant Pmp22 homodimers. All three Pmp22s form complexes larger than dimers with Tr Pmp22 especially prone to aggregate into high molecular weight complexes. Despite the differences in aggregation of Tr and TO Pmp22, these two mutant Pmp22s sequester the same amount of wild-type Pmp22 in heterodimers and heterooligomers. Thus, the differences in the phenotypes of Tr and TrJ mice may depend more on the ability of the mutant protein to aggregate than on the dominant-negative effect of the mutant Pmp22 on wild-type Pmp22 trafficking. [source]

    Mutation of conserved aspartates affect maturation of presenilin 1 and presenilin 2 complexes

    ACTA NEUROLOGICA SCANDINAVICA, Issue 2000
    G. Yu
    Presenilin (PS1 and PS2) holoproteins are transiently incorporated into low molecular weight (MW) complexes. During subsequent incorporation into a higher MW complex, they undergo endoproteolysis to generate stable N- and C-terminal fragments (NTF/CTF). Mutation of either of two conserved aspartate residues in transmembrane domains inhibits both presenilin-endoproteolysis and the proteolytic processing of APP and Notch. We show that aspartate-mutant holoprotein presenilins are not incorporated into the high molecular weight, NTF/CTF-containing complexes. Aspartate-mutant presenilin holoproteins also preclude entry of endogenous wild-type PS1/PS2 into the high molecular weight complexes, but do not affect the incorporation of wild-type holoproteins into lower molecular weight holoprotein complexes. These data suggest that the loss-of-function aspartate-mutants cause altered PS complex maturation, and argue that the functional presenilin moieties are contained in the high molecular weight presenilin NTF/CTF-containing complexes. [source]