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Light and heavy chains of myosin from atrial and ventricular myocardium of turkey and rat.
No full textTYROSINE PHOSPHORYLATION OF CYTOSOLIC PROTEINS IN HUMAN ERYTHROCYTES
No full textSome cytosolic proteins of human erythrocytes can be phosphorylated on tyrosine residues by endogenous Tyr-protein kinase(s). Their phosphorylation is enhanced by addition of Tyr-protein kinase, purified from human erythrocyte cytosol. The most phosphorylatable is a 19 kDa protein. Its phosphorylation is more activated by Mn2+ than by Mg2+. It is inhibited by NaC1, 2,3-bisphosphoglycerate and by heparin. Similar response to the above effectors is exhibited by the phosphorylation of the other protein bands. However, the phosphorylation of a 73 kDa double band, which is negligible in the absence of added NaC1, is stimulated by this salt
Myosin light and heavy chains in muscle regenerating in absence of the nerve: transient appearance of the embryonic light chains
No full textWe examined myosin of fast and slow skeletal rat muscles regenerating after ischemia and bupivacaine injection in denervated limbs. Four days after injury two-dimensional gel electrophoresis revealed the presence of the embryonic light chain in the myosin isolated from the portion of muscle showing a homogeneous population of new small fibers by histological examination. Two weeks after injury this subunit was absent, whereas the two light chains, LC1F and LC2F, became prominent. One month after injury the still denervated soleus muscle maintained this light chain pattern. Gel electrophoresis in native condition of the myosin and peptide mapping of electrophoretically purified heavy chains confirmed that the muscle regenerating in absence of the nerve accumulated a myosin that had the general features of a fast, not slow, myosin but contained definite differences from the former. © 1983
Participatory processes and Strategic Environmental Assessment: looking for regional meshes among actors and ecosystems
No full textEffects of beta 1-integrin antisense phosphorothioate-modified oligonucleotide on myoblast behaviour in vitro.
No full textCell Biochem Funct. 1995 Jun;13(2):99-104.
Effects of beta 1-integrin antisense phosphorothioate-modified oligonucleotide on myoblast behaviour in vitro.
Carraro U, Bruson A, Catani C, Dalla Libera L, Massimino ML, Rizzi C, Rossini K, Sandri M, Cantini M.
Source
University of Padova, CNR Unit for Muscle Biology and Physiopathology, Department of Biomedical Sciences, Italy.
Abstract
Myoblasts gene-engineered in vitro and then injected in vivo are safe, efficient options for gene therapy. While isolation of satellite cells is routinely achieved, their proliferation potential in vitro remains a limiting factor for cell transplantation under clinical conditions. We have studied the role of reversible inhibition of gene expression by antisense oligonucleotides on the proliferation of the myogenic cells. Addition of antisense oligonucleotides to myoblast cultures has been used to inhibit specifically the expression of the beta 1-integrin subunit gene. Here we show that the effects of multiple pulses of a phosphorothioate oligodeoxinucleotide antisense on the attachment to substrata and on the proliferation of myoblasts are dose-dependent. The addition of antisense to rat myoblasts caused rounding up of the cells and most of the cells became detached after several days in culture. A single pulse did not show any consistent effect, while in the presence of continuously administered antisense, the relative numbers of myoblasts in the treated muscle culture increased. We have no evidence of inhibition of myoblast fusion under these conditions. On the other hand, [3H]-TdR incorporation, total DNA and total number of cells decreased in antisense-treated cultures thus demonstrating an inhibitory effect of the phosphorothioate oligonucleotides on DNA synthesis. These side-effects could be overcome by substituting the phosphorothioate by unmodified oligonucleotides, so decreasing the half-life of the antisense, but also its toxicity. The overall results suggest a potential role of integrin antisense strategy in modulating the potential of myoblasts to proliferate.
PMID:
7538914
[PubMed - indexed for MEDLINE
Going Beyond Counting First Authors in Author Co-citation Analysis
Full text linkThe present study examines one of the fundamental aspects of author co-citation analysis (ACA) - the way co-citation
counts are defined. Co-citation counting provides the data on which all subsequent statistical analyses and mappings
are based, and we compare ACA results based on two different types of co-citation counting - the traditional type that
only counts the first one among a cited work's authors on the one hand and a non-traditional type that takes into
account the first 5 authors of a cited work on the other hand. Results indicate that the picture produced through this non-traditional author co-citation counting contains more coherent author groups and is therefore considerably clearer. However, this picture represents fewer specialties in the research field being studied than that produced through the traditional first-author co-citation counting when the same number of top-ranked authors is selected and analyzed. Reasons for these effects are discussed
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