Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.7 (acetylcholinesterase)
 28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The behavior of host and donor cell lines in human split-thickness skin grafts onto nude mice was studied by in situ hybridization (ISH) using genomic DNAs as probes, and immunohistochemically with species-specific or cross-species specific antibodies, at different stages ranging from day 3 to more than 1 year following grafting. Changes in the graft vascular and interstitial extracellular matrix were also assessed using species-specific or cross-species specific antibodies to human or murine type I, III, and IV collagens. Finally, transplant reinnervation was investigated using antibodies to various nerve cytoplasmic antigens and the thiocholine method to demonstrate acetylcholinesterase. Using these methods we were able to show the following: (1) the graft epidermis that is not replaced by mouse keratinocytes is progressively colonized by recipient Langerhans cells (LCs); (2) revascularization of the grafts begins soon by inoculation of the graft vessels with the host microcirculatory bed, and mouse endothelial cells growing into preexisting human capillary tubes produce a new basement membrane, prior to the replacement of the original one; (3) within 3-5 days following grafting, mouse fibroblasts migrate into the graft dermis. The density of the human and murine fibroblast populations then progressively increases. Characterization of the interstitial collagens identifies both human and murine type I and III collagens. Production of type III collagens decreases during the progression of fibrogenesis while human type I collagen becomes the predominant matrix protein; (4) transplant reinnervation is deficient, and neurites growing into severed graft nerve trunks were never detected.
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PMID:Host-donor interactions in healing of human split-thickness skin grafts onto nude mice: in situ hybridization, immunohistochemical, and histochemical studies. 158 62

Previous studies have indicated that the asymmetric form of acetylcholinesterase is localized in the basement membrane zone of the neuromuscular junction. We find that the collagenous subunit of the enzyme is required for interactions with basement membrane components. Acetylcholinesterase (the A12 form) binds best to the basement membrane heparan sulfate proteoglycan and type V collagen, to a lesser extent to laminin, fibronectin, and type I collagen, but not to type IV collagen. In addition, the purified A12 enzyme as prepared from electric eel is associated with a heparan sulfate-like component which appears to be responsible for the aggregation of the enzyme at low ionic strength. We observed that the purified form of the enzyme reacted with antibodies to type V collagen, and to a lesser extent with anti-type I collagen antibody, but not with anti-type IV collagen antibody. These data suggest that the collagenous subunit of the enzyme may have some similarity to type V collagen and that the interaction of the collagenous subunit with a heparan sulfate proteoglycan may be involved in its binding to basement membrane in the neuromuscular junction.
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PMID:Interactions of asymmetric forms of acetylcholinesterase with basement membrane components. 686 10

Unlabeled collagenous proteins were quantified as inhibitors of binding of native, soluble, radioiodinated type I collagen to the fibroblast surface. Collagen types IV, V a minor cartilage isotype (1 alpha 2 alpha 3 alpha), and the collagenlike tail of acetylcholinesterase did not inhibit binding. Collagen types II and III behaved as competitive inhibitors of type I binding. Denaturation of native collagenous molecules exposed cryptic inhibitory determinants in the separated constituent alpha chains. Inhibition of binding by unlabeled type I collagen was not changed by enzymatic removal of the telopeptides. Inhibitory determinants were detected in cyanogen bromide-derived peptides from various regions of helical alpha 1 (I) and alpha 1(III) chains. The aminoterminal propeptide of chick pro alpha 1(I) was inhibitory for binding, whereas the carboxyterminal three-chain propeptide fragment of human type I procollagen was not. The data are discussed in terms of the proposal that binding to surface receptors initiates the assembly of periodic collagen fibrils in vivo.
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PMID:Binding of soluble type I collagen to fibroblasts: specificities for native collagen types, triple helical structure, telopeptides, propeptides, and cyanogen bromide-derived peptides. 715 46

A quantitative morphometric evaluation of the intramural plexus of the urinary bladder of adult and aged guinea-pigs was performed by histological analysis, scanning electron microscopy, and hystochemical methods, such as NADH-diaphorase and acetylcholinesterase (AChE). The round or oval shaped intramural neurons were revealed among the bundles of the smooth detrusor muscle in clusters containing a variable number of cells in the groups. In both adult control and aged animals, the ganglia were enveloped by a ganglionar capsule of connective tissue mainly composed of type I collagen fibers. The number of neurons NADH-diaphorase positives estimated in the intramural plexus was 1433+/-187.71 and 1107+/-120.67 in the adult control and aged groups, respectively. The perikaryon areas of the NADH-diaphorase neurons reactives ranged from 216.40 to 1809.30 microm(2) in adult control group and from 198.20 to 2096.25 microm(2) in aged group. The nuclear area showed an increase in aged animals. The number of AChE-positive neurons estimated in the intramural plexus was 3294.67+/-415 microm(2) in the adult control group and 1960.33+/-526 microm(2) in the aged group, showing a significant decrease in the latter group. This age-related morphological change in intramural neurons may contribute to changes in urinary bladder activities in the elderly.
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PMID:Age-related changes in urinary bladder intramural neurons. 1744 14