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Information on ductal differentiation in the developing rat parotid gland is sparse. Striated and excretory ducts are rich in a number of enzymes related to ion movement. The objective of this investigation was to delineate histochemically the chronology of two of these, ouabain-sensitive Na(+),K(+)-ATPase and NADH-DE, in the developing rat parotid gland. Parotid glands were excised from rats at representative ages from 20 days in utero to 42 days. Enzyme histochemistry was performed on air-dried frozen sections. For Na(+), K(+)-ATPase, some sections also were fixed in phosphate-buffered formalin. Ouabain blocked Na(+),K(+)-ATPase activity, and neither enzyme reacted without substrate. Weak Na(+),K(+)-ATPase reactions were initially seen in unfixed sections at 1 day, and increased steadily to the adult pattern of strong (concentrated basolaterally) in striated ducts and excretory ducts, respectively, and weak to modest (diffuse) in acini and intercalated ducts at 28 days. In fixed sections, localization was sharper but the reaction was somewhat reduced. NADH-DE was modest in terminal buds and ducts before birth, then progressively changed to the adult pattern of weak in acini and intercalated ducts and strong (concentrated basally and luminally) in striated and excretory ducts at 28 days. As demonstrated by enzyme histochemistry of Na(+),K(+)-ATPase and NADH-DE, differentiation of rat parotid striated ducts and excretory ducts occurs mainly between birth and 28 days. Anat Rec 256:72-77, 1999. Published 1999 Wiley-Liss, Inc.
Anat Rec 1999 09 01
PMID:Enzyme histochemical localization of Na(+),K(+)-ATPase and NADH-DE in the developing rat parotid gland. 1045 87

Arterial hypertension produces changes along the vascular tree. However, there are few reports on its effect on human muscle capillaries. This study demonstrates the effects of essential hypertension on the capillaries of human quadriceps muscle. Muscle biopsy was taken from quadriceps femoris in eight men with recent diagnosis of essential hypertension, without treatment. Biopsies were also taken from eight normotensive men and were used as controls. Fiber types were classified by ATPase reaction, capillaries counted in alpha-amylase-PAS stained sections and ultrastructure studied by conventional methods of transmission electron microscopy. No changes were found in capillaries or muscle fiber types by histochemical methods. However, electron microscopy revealed abnormal capillaries with endothelial cells infoldings into the lumen, as well as occluded or degenerated capillaries. In some cases the endothelial cell area covered by pericytes was increased. Basement membrane of capillaries was frequently increased in width, sometimes irregularly, and in other instances it was reduplicated. In transversely sectioned capillaries lumen diameter was reduced and wall thickness was increased, although total diameter was unchanged. In hypertensive patients the finding of some degenerated capillaries adjacent to muscle fibers could be interpreted as the beginning of a process of rarefaction. Some capillaries showed morphological changes, and the ratio wall thickness/lumen was increased.
Anat Rec 1999 12 01
PMID:Capillary changes in skeletal muscle of patients with essential hypertension. 1058 28

The genioglossus (GG) muscle is divided into horizontal and oblique compartments that are the main protrusor and depressor muscles of the tongue, respectively. In humans the GG plays an important role in speech articulation, swallowing, and inspiratory dilation of the pharynx. At present, little is known about the neuromuscular specializations of the GG in any mammal. This study examined the specializations of these compartments in the canine tongue using a variety of anatomical and histochemical techniques. Six canine GG muscles were sectioned and stained for myofibrillar ATPase to study muscle fiber types; five whole-mount GG muscles were stained for acetylcholinesterase (AChE) to study the distribution of motor endplates; and eight whole mount GG muscles were processed with Sihler's stain to study the entire nerve supply pattern. In addition, the arrangement of muscle fibers of the GG within the tongue was also determined (N = 3). The most notable difference between the compartments of the GG was their proportions of fast and slow twitch muscle fibers: the horizontal compartment contained 64% slow twitch muscle fibers compared to 41% in the oblique compartment. In addition, although the oblique compartment appeared to be grossly homogeneous, it could be divided into thirds by significant differences in the percentages of slow twitch fibers: posterior (23%), middle (15%), and anterior (56%; P < 0.05). The muscle fibers of the oblique GG within the tongue were found to be divided into medial and lateral layers that run vertically and transversely, respectively. The nerve supply to each third of the oblique GG formed a plexus with the anterior third being the densest. The innervation pattern of the oblique GG was also notable as terminal nerve branches coursing parallel to the muscle fascicles gave off perpendicular secondary branches along each motor endplate band. These secondary nerve branches connected the primary nerves and formed a regularly spaced grid throughout the compartment. Evidently, the two compartments of the GG exhibited different anatomical specializations. The horizontal had a slow muscle fiber profile and simple innervation pattern; these qualities are possibly related to its single force vector and respiratory related activity. The oblique compartment had a relatively fast muscle fiber profile with evidence for three separate functional subdivisions. The most anterior part was noticeably different, and was presumably specialized for fine motor control of the tip of the tongue. The vertically oriented fibers of the oblique GG within the tongue body may function as a midline depressor of the tongue, whereas its transversely oriented fibers could play a role in narrowing the tongue during other motor tasks.
Anat Rec 2000 11 01
PMID:Neuromuscular specializations of the pharyngeal dilator muscles: II. Compartmentalization of the canine genioglossus muscle. 1106 41

Brefeldin-A (BFA) is a specific and potent inhibitor of the intracellular transport of clathlin-uncoated transitional vesicles from the cisterns of rough-surfaced endoplasmic reticulum (RER) to the Golgi lamellae. This study was designed to clarify the effects of BFA on ultrastructure, subcellular localization of vacuolar-type H+-ATPase and a lysosomal cysteine proteinase, cathepsin K, in cultured osteoclasts and their resorptive function. H+-ATPase and cathepsin K are the most important enzymes for decalcification of apatite crystals and degradation of type-I collagen, respectively. In control cultures without BFA, osteoclasts were structurally characterized by the development of broad ruffled borders and clear zones, and formed many resorption lacunae in cocultured dentine slices. In BFA-treated cultures, osteoclasts lacked ruffled borders, and the cytoplasm was filled with regular-size and extremely large pale vacuoles over 2 microm in diameter, which were produced by fusion of adjacent vacuoles. BFA did not, however, inhibit clear zone formation and adhesion of osteoclasts to dentine slices. Resorption lacuna formation was markedly diminished by BFA treatment. Although H+-ATPase and cathepsin K were strongly expressed in osteoclast ruffled borders in control cultures, BFA treatment altered the subcellular localization and decreased the expression of these molecules. In BFA-treated cultures, H+-ATPase immunoreaction in osteoclasts was observed along the limiting membranes of some, but not all, regular-size pale vacuoles, but neither in extremely large vacuoles nor along the smooth plasma membranes facing the dentine slices. Similarly, cathepsin K was localized within lysosomes and some regular-size pale vacuoles, but its secretion toward the dentine slices through the ruffled borders was strongly inhibited by BFA treatment. These results suggest that 1.) formation of the osteoclast ruffled borders and their resorptive function are closely associated with the intracellular transport of these molecules from the RER cisterns and the Golgi lamellae to the ruffled borders, and 2.) both H+-ATPase and cathepsin K are selectively transported to the ruffled border membranes by pale vacuoles.
Anat Rec 2001 06 01
PMID:Effects of brefeldin-A: potent inhibitor of intracellular protein transport on ultrastructure and resorptive function of cultured osteoclasts. 1136 Feb 30

The primary focus of this study was the accurate classification of limb skeletal muscle fiber types in adult goats (Capra hircus) according to the myosin heavy chain (MHC) isoform they express. Combined methodologies of gel electrophoresis, immunoblotting, immunohistochemistry, myofibrillar ATPase (mATPase), and quantitative metabolic enzyme histochemistry of M. semitendinosus samples were developed. Three MHCs were identified and tentatively designated as types I, IIA, and IIX. Five fiber types were defined immunohistochemically according to their MHC content: I, I+IIA, IIA, IIAX, and IIX. The hybrid fast-twitch fibers (IIAX) totaled 21% of the fiber population analyzed. The three major pure fibers (I, IIA, and IIX) could be objectively separated upon the basis of their mATPase activities after acid and alkaline preincubations. The prominent number of hybrid fibers, however, could not be delineated with these mATPase methods. Metabolic and size properties of muscle fibers varied according to their MHC content, but overlapped the full range of muscle fiber phenotypes. These integrated data demonstrate that type II skeletal muscle fibers of small ruminants have been misclassified in previous studies. The immunohistochemical approach developed in the present study offers new prospects for muscle fiber typing in caprine experimental studies and meat production technologies.
Anat Rec 2001 11 01
PMID:Limb myosin heavy chain isoproteins and muscle fiber types in the adult goat (Capra hircus). 1159 10

To investigate the cellular mechanisms of physiological root resorption in human deciduous teeth, the authors examined the immunocytochemical localization of vacuolar-type H+-ATPase, a lysosomal cysteine proteinase, cathepsin K, matrix metalloproteinase-9 (MMP-9), and receptor activator of NFKB ligand (RANKL) in odontoclasts. H+-ATPase, cathepsin K, and MMP-9 are the most important enzymes for decalcification of apatite crystals and degradation of type-I collagen. In addition, RANKL is one of the key regulatory molecules in osteoclast formation and functions. Odontoclasts developed extensive ruffled borders and clear zones apposed to the resorbing root dentine surfaces. On immunoelectron microscopy, the expression of vacuolar-type H+-ATPase was detected along the limiting membranes of pale vacuoles and the ruffled border membranes of odontoclasts. Cathepsin K in odontoclasts was localized within pale vacuoles, lysosomes, the extracellular canals of ruffled borders, and the underlying resorbing dentine surfaces. MMP-9 localization in odontoclasts was similar to those of cathepsin K. RANKL was detected in both mononuclear stromal cells and odontoclasts located on resorbing dentine surfaces. These results suggest that (1) odontoclasts are directly involved in decalcification of apatite crystals by active extrusion of proton ions mediated by H+-ATPase and (2) extracellular degradation of dentine type-I collagen by both cathepsin K and MMP-9, and (3) odontoclast differentiation and activity are regulated, at least in part, by RANKL, possibly produced by mononuclear stromal cells and odontoclasts themselves in the resorbing tissues. Thus, the cellular mechanisms of physiological root resorption appear to be quite similar to those of osteoclastic bone resorption.
Anat Rec 2001 11 01
PMID:Immunolocalization of vacuolar-type H+-ATPase, cathepsin K, matrix metalloproteinase-9, and receptor activator of NFkappaB ligand in odontoclasts during physiological root resorption of human deciduous teeth. 1159 12

The inferior pharyngeal constrictor (IPC) muscle functions during swallowing, respiration, and vocalization. The most-caudal portion of the IPC is believed to be part of the functional upper esophageal sphincter (UES). We hypothesized that the caudal fibers of the human IPC may have enzyme-histochemical characteristics similar to those of the cricopharyngeus muscle, a major component of the UES. In this study, human IPC muscles obtained from autopsy were studied using Sihler's stain to examine innervation patterns, and using myofibrillar ATPase, NADH tetrazolium reductase (NADH-TR), and succinic dehydrogenase (SDH) techniques to investigate the distribution and oxidative capacity of the slow- (type I) and fast- (type II) twitch fibers in the muscle. The results showed that the human IPC consists of at least two neuromuscular compartments (NMCs): rostral and caudal. Each of the NMCs was innervated by a separate nerve branch derived from the pharyngeal branch of the vagus nerve. The rostral NMC is faster (39% type I, 61% type II) than the caudal NMC (70% type I, 30% type II). In addition, two histochemically-delineated fiber layers were identified in the human IPC: a slow inner layer (SIL) with predominantly type I fibers (66%), and a fast outer layer (FOL) with predominantly type II fibers (62%) (P < 0.01). However, the dimensions of both fiber layers and proportions of the muscle fiber types varied with the NMCs. Specifically, the ratio of the thickness of the SIL to FOL was approximately 2:1 for the caudal NMC and approximately 1:2 for the rostral NMC, respectively. In the SIL the type I fibers accounted for 84% for the caudal NMC and 69% and 44% for the lower and upper portions of the rostral NMC. In contrast, the type II fibers in the FOL accounted for 46% for the caudal NMC and 67% and 74% for the lower and upper portions of the rostral NMC, respectively (P < 0.01). The caudal NMC of the IPC shared histochemical characteristics with the cricopharyngeus muscle, in that it contained predominantly slow oxidative fibers. Overall, the caudal NMC and the SIL in the IPC had high NADH-TR and SDH activities. However, different patterns of oxidative enzyme activity were identified in both type I and type II fibers. This study provided histochemical evidence for the concept that the caudal NMC within the IPC contributes to the functional UES. In addition, the two histochemically-defined fiber layers in the IPC may be a specialized adaptation in humans to enable different upper-airway functions during respiration, swallowing, and speech.
Anat Rec 2001 12 01
PMID:Neuromuscular compartments and fiber-type regionalization in the human inferior pharyngeal constrictor muscle. 1174 92

The lateral wall of the dog cochlear duct was investigated by classical staining and immunohistochemistry for NaK/ATPase beta2 isoform, cytokeratins (Cks), vimentin, nestin, and S100A6 during the postnatal cochlear maturation, i.e., from birth to postnatal day 110. The dog stria vascularis was immature at birth. Fine melanin granules were evident in the stria from the second week of life, and melanin concentration increased drastically beyond the first month. The marginal cells were NaK/ATPase- and Ck-positive; intermediate cells were either nestin- and S100A6-positive or vimentin-positive; the basal cells were vimentin-positive; the capillary endothelium showed vimentin and nestin labeling; the cell layer underlying the stria was nestin-positive. The fibrocytes of the spiral ligament and spiral prominence expressed nestin and vimentin. The epithelial cells overlaying the spiral prominence and the external sulcus were Ck-positive, and transiently nestin- and vimentin-positive. Double immunolabeling, for S100A6 and either nestin, vimentin, or NaK/ATPase, and for nestin and vimentin suggested the presence of two distinct intermediate cell types. The results enabled us to differentiate the cell types forming the lateral wall of the dog cochlear duct, and to follow their postnatal maturation. This study may form a basis for future investigations about spontaneous cochleosaccular degeneration in dogs. This species is an important companion animal, and a possible model for the study of comparable diseases in humans.
Anat Rec A Discov Mol Cell Evol Biol 2003 Jan
PMID:Postnatal maturation of the dog stria vascularis-- an immunohistochemical study. 1249 92

We report the effects of specific and potent inhibitors of vacular-type H(+)-ATPase and lysosomal cysteine proteinases, cathepsins, on the ultrastructure, expression of these enzymes, and resorptive functions of cultured osteoclasts. Osteoclasts were formed by co-culture of marrow cells and calvarial primary osteoblasts of ddY mice. Formed osteoclasts were cultured on dentine slices for 6-48 hr with either an H(+)-ATPase inhibitor, bafilomycin A1, or a cysteine proteinase inhibitor, E-64. In control cultures with no additive, osteoclasts were structurally characterized by the development of ruffled borders and clear zones, and formed many resorption lacunae on dentine slices. Both H(+)-ATPase and cathepsin K were strongly expressed in the ruffled borders of these osteoclasts. In bafilomycin A1-treated cultures, osteoclasts lacked ruffled borders, and resorption lacuna formation was markedly diminished. This effect of bafilomycin A1 on osteoclast structure was reversible by removal of the compound. Bafilomycin A1 treatment altered the subcellular localization and decreased the expression of H(+)-ATPase molecules. H(+)-ATPase expression was observed throughout the cytoplasm, but not along the plasma membranes facing dentine slices. On the other hand, E-64 treatment did not affect the ultrastructure of osteoclasts and the expression of enzyme molecules. Although E-64 showed no effect on demineralization of dentine slices, it dose-dependently reduced resorption lacuna formation. Our results suggest that 1) bafilomycin A1 dose-dependently inhibits resorption lacuna formation via inhibition of ruffled border formation, 2) H(+)-ATPase expression is closely associated with the cytoskeleton of osteoclasts, and 3) E-64 treatment decreases the depth of resorption lacunae, by inhibition of secreted cathepsin K activity, but does not impair ruffled border formation and the associated expression of H(+)-ATPase and cathepsin K in osteoclasts.
Anat Rec A Discov Mol Cell Evol Biol 2003 Feb
PMID:Specific biological functions of vacuolar-type H(+)-ATPase and lysosomal cysteine proteinase, cathepsin K, in osteoclasts. 1252 90

This short review discusses changes in the fibre type distribution, myosin heavy chain isoform composition and histological appearance of the very elderly human skeletal muscle. Point of origin of the discussion comes from data that we have obtained from muscle biopsies from the vastus lateralis muscle of a group of frail very elderly subjects (age: 88 +/- 3 years, range 85-97). Myosin heavy chain composition of muscle homogenates and single fibres, fibre type distribution, fibre size and capillary density were examined and compared with muscle biopsies from the young vastus lateralis muscle. Histological preparations of the muscle biopsies from our elderly subjects showed extended "grouping" (Nygaard & Sanchez, Anat Rec 1992: 202: 451-459) of the fibre types as well as significant changes in the appearance and size of the individual muscle fibres. On average, the fibre type composition of our very elderly subjects do not seem to be different to what is observed in a corresponding young group when examined with ATPase histochemistry. Likewise, the MHC composition of the muscle homogenates is comparable to what is observed in young subjects. Nevertheless, a detailed examination of the MHC composition of single fibres from the old subjects revealed that the most prominent phenotype was fibres co-expressing MHC I and MHC IIA. This is very different from what is observed in the young muscle. Detailed investigation of longitudinally cut fibres indicated that some fibres in the very old muscle, in contrast to the young muscle, switch fibre type along the length of the fibre or contain areas or nuclear domains in which the MHC expression is different from the remaining part of the fibre.
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PMID:Muscle fibre type adaptation in the elderly human muscle. 1253 16


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