Shear stress alters the expression of myelin-associated glycoprotein (MAG) and myelin basic protein (MBP) in Schwann cells
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چکیده
منابع مشابه
Non-myelin-forming perisynaptic schwann cells express protein zero and myelin-associated glycoprotein.
Perisynaptic Schwann cells (PSCs) envelop axonal terminals and are physiologically distinct from the nearby myelinating Schwann cells (MSCs), which surround the same innervating motor axons. PSCs have special functions at the neuromuscular synapse, where they detect and can modulate neurotransmitter release. Although PSCs are similar to non-myelinating Schwann cells in that they do not form mul...
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The myelin-associated glycoprotein (MAG) is a type I transmembrane glycoprotein localized in periaxonal Schwann cell and oligodendroglial membranes of myelin sheaths where it functions in glia-axon interactions. It contains five immunoglobulin (Ig)-like domains and is in the sialic acid-binding subgroup of the Ig superfamily. It appears to function both as a ligand for an axonal receptor that i...
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In peripheral nerves, large caliber axons are ensheathed by myelin-elaborating Schwann cells. Multiple lines of evidence demonstrate that expression of the genes encoding myelin structural proteins occurs in Schwann cells in response to axonal instructions. To gain further insight into the mechanisms controlling myelin gene expression, we used reporter constructs in transgenic mice to search fo...
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Myelin-associated glycoprotein (MAG) is an integral membrane protein expressed by myelinating glial cells that occurs in two developmentally regulated forms with different carboxyterminal cytoplasmic domains (L-MAG and S-MAG). To investigate the role of MAG in myelination a recombinant retrovirus was used to introduce a MAG cDNA (L-MAG form) into primary Schwann cells in vitro. Stably infected ...
متن کاملSchwann cell expression of a major myelin glycoprotein in the absence of myelin assembly.
Quiescent Schwann cells in the distal segment of the permanently transected nerve produced basal levels of the major myelin glycoprotein, P0, in the absence of myelin assembly. Low levels of P0 could be detected at 35 days after transection by autoradiographic analysis of radioiodinated lectin binding after protein separation by high-resolution sodium dodecyl sulfate pore gradient electrophores...
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ژورنال
عنوان ژورنال: Journal of Orthopaedic Research
سال: 2005
ISSN: 0736-0266,1554-527X
DOI: 10.1016/j.orthres.2004.12.010