PubMed · 7563306
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
G D Hautman, S J Sherman, G O Utter, M Cadieux, S M Jacques. 1995. Acrania.. https://doi.org/10.7863/jum.1995.14.7.552
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
The collagen-tailed or asymmetric forms (A) represent a major component of acetylcholinesterase (AChE) in the neuromuscular junction of higher vertebrates. They are hetero-oligomeric molecules, in which tetramers of catalytic subunits of type T (AChET) are attached to the subunits of a triple-stranded collagen "tail." We report the cloning of a rat AChE-associated collagen subunit, Q. We show that collagen tails are encoded by a single gene, COLQ. The ColQ subunits form homotrimers and readily form collagen-tailed AChE, when coexpressed with rat AChET. We found that the same ColQ subunits are incorporated, in vivo, in asymmetric forms of both AChE and butyrylcholinesterase. A splice variant from the COLQ gene encodes a proline- rich AChE attachment domain without the collagen domain but does not represent the membrane anchor of the brain tetramer. The COLQ gene is expressed in cholinergic tissues, brain, muscle, and heart, and also in noncholinergic tissues such as lung and testis.
During the early stages of mammalian ontogeny muscle fibres are innervated by more than one axon. This polyneural innervation is replaced by mononeural innervation in the course of development. The regression of polyneural innervation in the psoas muscle in the human is the topic of the present study. Innervation patterns were studied in fetuses from 15 1/2 weeks of post menstrual age (PMA) and in babies until 80 weeks PMA (40 weeks after term age) and compared to data from two adults. Motor endplates were stained by a combined acetylcholinesterase stain. Innervation patterns and motor endplate morphology were studied and the sizes of endplates were measured. As a main result of our study polyneural innervation of the psoas muscle remains at a level of about 2 endings per endplate (range 1-5 terminals) until 18-25 weeks PMA and decreases thereafter. From 52 weeks PMA (12 weeks post term) onwards, muscle fibres are predominantly mononeurally innervated. During development the morphology of the terminal patterns of the nerve endings becomes more complex and the size of endplates increases, implying that the adult pattern of muscle innervation is reached at the age at which a major functional transformation in the neurobehavioural repertoire occurs (i.e. the end of the second and the beginning of the third month.
To explore the possibility that overproduction of neuronal acetylcholinesterase (AChE) confers changes in both cholinergic and morphogenic intercellular interactions, we studied developmental responses to neuronal AChE overexpression in motoneurons and neuromuscular junctions of AChE-transgenic mice. Perikarya of spinal cord motoneurons were consistently enlarged from embryonic through adult stages in AChE-transgenic mice. Atypical motoneuron development was accompanied by premature enhancement in the embryonic spinal cord expression of choline acetyltransferase mRNA, encoding the acetylcholine-synthesizing enzyme choline acetyltransferase. In contrast, the mRNA encoding for neurexin-Ibeta, the heterophilic ligand of the AChE-homologous neuronal cell surface protein neuroligin, was drastically lower in embryonic transgenic spinal cord than in controls. Postnatal cessation of these dual transcriptional responses was followed by late-onset deterioration in neuromotor performance that was associated with gross aberrations in neuromuscular ultrastructure and with pronounced amyotrophy. These findings demonstrate embryonic feedback mechanisms to neuronal AChE overexpression that are attributable to both cholinergic and cell-cell interaction pathways, suggesting that embryonic neurexin Ibeta expression is concerted in vivo with AChE levels and indicating that postnatal changes in neuronal AChE-associated proteins may be involved in late-onset neuromotor pathologies.