The relationships of the lateral pterygoid muscle within the infratemporal fossa were observed by conventional dissections and by examination of specimens sectioned in the horizontal and frontal planes. The following less well-known features were noted. At the origins of the superior and inferior heads there are regions in which the fibres are interlaced or closely overlapped by fibres of either the temporalis muscle or the medial pterygoid muscle. Fibres of the superior head insert not only into the meniscus of the temporomandibular joint, but also into the pterygoid fovea at the neck of the mandibular condyle. Specimens sectioned through the origin of the inferior head of the muscle show internal tendon lamellae consistent with a pennate structure. Electromyographic (EMG) activity was recorded in five healthy subjects using concentric needle and fine-wire electrodes. Strong to very strong activity was consistently observed in the superior head during clenching and tooth gnashing. The inferior heads were silent or had negligible to slight activity most of the time during ipsilateral movements or clenching, but were co-activated bilaterally, with strong to very strong activity during jaw opening, protrusion, swallowing, tooth gnashing and during passive retrusion. They showed marked activity unilaterally during contralateral movements.
Subcultivated rat lingual epithelial cells when grown on collagen gels at a liquid-gas interface achieve a highly ordered state that closely resembles the parent tissue. Three distinct cell layers are present; basal, spinous, and keratinized. Basal cells are cuboidal in shape and form a complex interface with the underlying collagen fibrils. Spinous cells form a layer 5-10 cells thick and, with the exception of keratohyalin granules, possess an organellar complement identical with native cells, including membrane-coating granules. The keratinized cell layer increases in thickness as a function of time spent in culture. Forty or more plies of terminally differentiated cells are observed following a 30-day culture period. Terminally differentiated cells while retaining pycnotic nuclei and some other organellar debris are principally envelope-enclosed squames filled with tonofilaments. Keratinization is a continuing process which occurs simultaneously across the full expanse of the culture surface. The high degree of tissue organization observed appears to be the result of feeding the cultures from the undersurface.
Administration of the j3-adrenergic drug, isoproterenol (IPR), affects the release of 98% of stored amylase from rat parotid gland acinar cells . A period of 6 h elapses from the onset of secretion to the maximum [14C]phenylalanine (Phe) incorporation into total protein and amylase . 10 h after IPR administration the rate of [ 14C]Phe incorporation into total protein was no longer elevated above that of control . Incorporation into amylase, however, remained elevated above the control by 2 .3 times . This latent period may reflect :(a) reduced amounts of available ATP which occurs as a result of the process of secretion as well as (b) the time required for reorganization of cellular organelles and membranes after secretion. The latent period after IPR-induced secretion appears similar to the latent period which has recently been reported to occur after physiologic release of amylase from the parotid gland during the diurnal feeding cycle of the rat . These observations support the existence of a positive feedback system operant in the parotid acinar cell linking the release of secretory proteins with their synthesis . The period of greatest protein synthesis is, however, temporally dissociated from the secretory process .
The collagen fibrils of human or guinea pig dermis when exposed to the denaturing agents, urea or guanidine-HC1, dissociated into smaller, disparate subunits, probably aggregates of microfibrils. The process of dissociation demonstrates that the fibrils are assembled helically. Initially, diagonal clefts appear on the surface of the fibril. These clefts are surface manifestations of a spirally oriented, internal space. Continued exposure to these denaturants resulted in progressive dissociation of the fibril into helically oriented subunits. It is suggested that water-miscible compounds such as glycols or hydroxypropyl methacrylate, in addition to the urea-guanidinium class of denaturants used in this study, affect the observed fbrillar changes through the disruption of hydrogen bonds between the microfibrils making up the fibril. Such a mode of action may explain why freeze-fractured or '~inert embedded" collagen demonstrates helical organization while other, more conventional methods of tissue processing do not. Further support for the proposed mode of action of these dissociative agents was provided by the observation that mature collagen, in which extensive intra-and intermolecular covalent crosslinks are present, is more resistant to dissociation than newly formed collagen.
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