In Vitro Innervation as an Experimental Model to Study the Expression and Functions of Acetylcholinesterase and Agrin in Human Skeletal Muscle
Acetylcholinesterase (AChE) and agrin, a heparan-sulfate proteoglycan, reside in the basal lamina of the neuromuscular junction (NMJ) and play key roles in cholinergic transmission and synaptogenesis. Unlike most NMJ components, AChE and agrin are expressed in skeletal muscle and α-motor neurons. AC...
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MDPI AG
2017-08-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/22/9/1418 |
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| author | Katarina Mis Zoran Grubic Paola Lorenzon Marina Sciancalepore Tomaz Mars Sergej Pirkmajer |
| author_facet | Katarina Mis Zoran Grubic Paola Lorenzon Marina Sciancalepore Tomaz Mars Sergej Pirkmajer |
| author_sort | Katarina Mis |
| collection | DOAJ |
| description | Acetylcholinesterase (AChE) and agrin, a heparan-sulfate proteoglycan, reside in the basal lamina of the neuromuscular junction (NMJ) and play key roles in cholinergic transmission and synaptogenesis. Unlike most NMJ components, AChE and agrin are expressed in skeletal muscle and α-motor neurons. AChE and agrin are also expressed in various other types of cells, where they have important alternative functions that are not related to their classical roles in NMJ. In this review, we first focus on co-cultures of embryonic rat spinal cord explants with human skeletal muscle cells as an experimental model to study functional innervation in vitro. We describe how this heterologous rat-human model, which enables experimentation on highly developed contracting human myotubes, offers unique opportunities for AChE and agrin research. We then highlight innovative approaches that were used to address salient questions regarding expression and alternative functions of AChE and agrin in developing human skeletal muscle. Results obtained in co-cultures are compared with those obtained in other models in the context of general advances in the field of AChE and agrin neurobiology. |
| first_indexed | 2024-12-14T19:45:48Z |
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| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-12-14T19:45:48Z |
| publishDate | 2017-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-ea25c1248c904c28bcd2248cfbfffc8d2022-12-21T22:49:34ZengMDPI AGMolecules1420-30492017-08-01229141810.3390/molecules22091418molecules22091418In Vitro Innervation as an Experimental Model to Study the Expression and Functions of Acetylcholinesterase and Agrin in Human Skeletal MuscleKatarina Mis0Zoran Grubic1Paola Lorenzon2Marina Sciancalepore3Tomaz Mars4Sergej Pirkmajer5Institute of Pathophysiology, Faculty of Medicine, University of Ljubljana, Zaloška 4, SI-1000 Ljubljana, SloveniaInstitute of Pathophysiology, Faculty of Medicine, University of Ljubljana, Zaloška 4, SI-1000 Ljubljana, SloveniaDepartment of Life Sciences, University of Trieste, via A. Fleming 22, I-34127 Trieste, ItalyDepartment of Life Sciences, University of Trieste, via A. Fleming 22, I-34127 Trieste, ItalyInstitute of Pathophysiology, Faculty of Medicine, University of Ljubljana, Zaloška 4, SI-1000 Ljubljana, SloveniaInstitute of Pathophysiology, Faculty of Medicine, University of Ljubljana, Zaloška 4, SI-1000 Ljubljana, SloveniaAcetylcholinesterase (AChE) and agrin, a heparan-sulfate proteoglycan, reside in the basal lamina of the neuromuscular junction (NMJ) and play key roles in cholinergic transmission and synaptogenesis. Unlike most NMJ components, AChE and agrin are expressed in skeletal muscle and α-motor neurons. AChE and agrin are also expressed in various other types of cells, where they have important alternative functions that are not related to their classical roles in NMJ. In this review, we first focus on co-cultures of embryonic rat spinal cord explants with human skeletal muscle cells as an experimental model to study functional innervation in vitro. We describe how this heterologous rat-human model, which enables experimentation on highly developed contracting human myotubes, offers unique opportunities for AChE and agrin research. We then highlight innovative approaches that were used to address salient questions regarding expression and alternative functions of AChE and agrin in developing human skeletal muscle. Results obtained in co-cultures are compared with those obtained in other models in the context of general advances in the field of AChE and agrin neurobiology.https://www.mdpi.com/1420-3049/22/9/1418acetylcholinesterasein vitro innervationhuman muscleneuromuscular junctionco-culturesagrinapoptosis |
| spellingShingle | Katarina Mis Zoran Grubic Paola Lorenzon Marina Sciancalepore Tomaz Mars Sergej Pirkmajer In Vitro Innervation as an Experimental Model to Study the Expression and Functions of Acetylcholinesterase and Agrin in Human Skeletal Muscle Molecules acetylcholinesterase in vitro innervation human muscle neuromuscular junction co-cultures agrin apoptosis |
| title | In Vitro Innervation as an Experimental Model to Study the Expression and Functions of Acetylcholinesterase and Agrin in Human Skeletal Muscle |
| title_full | In Vitro Innervation as an Experimental Model to Study the Expression and Functions of Acetylcholinesterase and Agrin in Human Skeletal Muscle |
| title_fullStr | In Vitro Innervation as an Experimental Model to Study the Expression and Functions of Acetylcholinesterase and Agrin in Human Skeletal Muscle |
| title_full_unstemmed | In Vitro Innervation as an Experimental Model to Study the Expression and Functions of Acetylcholinesterase and Agrin in Human Skeletal Muscle |
| title_short | In Vitro Innervation as an Experimental Model to Study the Expression and Functions of Acetylcholinesterase and Agrin in Human Skeletal Muscle |
| title_sort | in vitro innervation as an experimental model to study the expression and functions of acetylcholinesterase and agrin in human skeletal muscle |
| topic | acetylcholinesterase in vitro innervation human muscle neuromuscular junction co-cultures agrin apoptosis |
| url | https://www.mdpi.com/1420-3049/22/9/1418 |
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