title: Electron microscopical study of non-specific cholinesterase activity in simple lamellar corpuscles of glabrous skin from cat rhinarium: a histochemical evidence for the presence of collagenase-sensitive molecular forms and their secretion.
abstract: The distribution of nCHE activity was studied histochemically in simple lamellar corpuscles (SLCs) of glabrous skin from cat rhinarium. The Schwann cells forming myelin sheaths in preterminal part of SCLs exhibited no positive reaction for nCHE activity. Prevalent reaction product was localized extracellularly in the inne core enveloping terminal portion of unmyelinated sensory axon. A dot-like shaped reaction product was deposited in the basal lamina of the inner core cells and their cytoplasmic lamellae or was scattered in enlarged interlamellar spaces. Only small amount of fine end product was found to be associated with the plasma membrane of inner core lamellae. Fine reaction product for nCHE activity was consistently localized in perinuclear and rER cisternae and saccules of the Golgi apparatus of inner core cells. Some vesicles around rER and the Golgi apparatus, ones beneath the plasma membrane, and tubular-like cisternal profiles oriented towards the surface contained nCHE end product, as well. The intracellular and extracellular localization of nCHE reaction product suggests that this enzyme behaves in cat SLCs as a secreted rather than as an integral membrane protein. A large amount of dot-like reaction product in the interlamellar spaces disappeared if the skin sections were treated with collagenase before incubation in the medium for histochemical detection of nCHE activity. The decrease of nCHE end product in SLCs of the skin sections after collagenase digestion was corroborated by means of light microdensitometer and electrometrical measurement. The histochemical detection and electrometrical measurement revealed that the majority of the reaction product in the interlamellar spaces of inner core corresponds with the nCHE molecules sensitive to collagenase treatment and they are probably counted among asymmetrical molecular forms.
authors.affiliation: Department of Anatomy, Medical Faculty, Purkynĕ University Brno, Czechoslovakia.
authors.forename: P
authors.initials: P
authors.lastname: Dubový
mesh_terms: D000818:Animals; D002415:Cats / Q000033:anatomy & histology / Q000378:metabolism*; D002802:Cholinesterases / Q000032:analysis*; D004721:Endoplasmic Reticulum / Q000201:enzymology; D005260:Female; D006056:Golgi Apparatus / Q000201:enzymology; D006651:Histocytochemistry; D008297:Male; D008465:Mechanoreceptors / Q000201:enzymology* / Q000648:ultrastructure; D003012:Microbial Collagenase / Q000494:pharmacology; D008854:Microscopy, Electron; D009666:Nose; D012867:Skin / Q000201:enzymology
chemical_list: D002802:Cholinesterases; D003012:Microbial Collagenase