| 1. |
- Uhlén, Mathias, et al.
(author)
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The human secretome
- 2019
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In: Science Signaling. - : American Association for the Advancement of Science (AAAS). - 1945-0877 .- 1937-9145. ; 12:609
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Journal article (peer-reviewed)abstract
- The proteins secreted by human cells (collectively referred to as the secretome) are important not only for the basic understanding of human biology but also for the identification of potential targets for future diagnostics and therapies. Here, we present a comprehensive analysis of proteins predicted to be secreted in human cells, which provides information about their final localization in the human body, including the proteins actively secreted to peripheral blood. The analysis suggests that a large number of the proteins of the secretome are not secreted out of the cell, but instead are retained intracellularly, whereas another large group of proteins were identified that are predicted to be retained locally at the tissue of expression and not secreted into the blood. Proteins detected in the human blood by mass spectrometry-based proteomics and antibody-based immuno-assays are also presented with estimates of their concentrations in the blood. The results are presented in an updated version 19 of the Human Protein Atlas in which each gene encoding a secretome protein is annotated to provide an open-access knowledge resource of the human secretome, including body-wide expression data, spatial localization data down to the single-cell and subcellular levels, and data about the presence of proteins that are detectable in the blood.
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| 2. |
- Brandt, J., et al.
(author)
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Acutely-dissociated Schwann cells used in tendon autografts for bridging nerve defects in rats: a new principle for tissue engineering in nerve reconstruction
- 2005
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In: Scand J Plast Reconstr Surg Hand Surg. - 0284-4311. ; 39:6, s. 321-5
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Journal article (peer-reviewed)abstract
- A new method of acute dissociation of Schwann cells was used to study the effect of addition of such cells to a tendon autograft--a recently-described graft material--on peripheral nerve regeneration in rats. Autologous Schwann cells were obtained from enzymatic dissociation of predegenerated nerves. The tendon autografts were supplied with Schwann cells through brief in vitro coincubation. Schwann cell-free tendon autografts were used as controls. Axonal outgrowth was measured immunohistochemically after four, seven, and 10 days. At seven days, outgrowth was significantly longer in the pretreated autografts. The use of acutely-dissociated Schwann cells is a new approach to tissue engineering in nerve reconstruction, and may abolish the need for time-consuming culture of Schwann cells.
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| 3. |
- Ekström, Per, et al.
(author)
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A calmodulin inhibitor with high specificity, compound 48/80, inhibits axonal transport in frog nerves without disruption of axonal microtubules.
- 1991
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In: Acta physiologica Scandinavica. - 0001-6772. ; 142:2, s. 181-9
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Journal article (peer-reviewed)abstract
- The calmodulin inhibitor compound 48/80 has previously been shown to arrest axonal transport in vitro in the regenerating frog sciatic nerve. The inhibition was limited to the outgrowth region of nerves, which had been allowed to regenerate in vivo for 6 days after a crush lesion, before they were incubated with or without drugs in vitro overnight. The effects of compound 48/80 on the regenerating nerve were further investigated. A concentration of compound 48/80 (50 micrograms ml-1), which effectively inhibits axonal transport, did not cause observable changes of the microtubules of regenerating axons in the outgrowth region as judged by electron microscopy. Furthermore, it was shown that also a lower concentration (25 micrograms ml-1) inhibited axonal transport. As a measure of possible metabolic effects, the level of ATP was assessed in the regenerating nerve after exposure to compound 48/80. Compound 48/80 at 25 micrograms ml-1 did not change the level of ATP in the nerve. The assembly of bovine brain microtubule proteins in a cell-free system was unaffected by 25 micrograms ml-1 of compound 48/80 and slightly inhibited by 50 micrograms ml-1. At higher concentrations (greater than 100 micrograms ml-1) assembly of microtubules appeared stimulated, and microtubule spirals as well as closely aligned microtubules could be seen. These effects appeared to be unrelated to the transport effects. The present results indicate that compound 48/80 arrests axonal transport via mechanisms other than destruction of axonal microtubules or interference with the energy metabolism. It is possible that these mechanisms involve inhibition of calmodulin-regulated events essential to the transport.
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