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PubMed1979

[Visualization of opiate receptors in the locus coeruleus of rats: high resolution radioautography after administration of a tritiated met-enkephalin analog].

Opiate receptor sites were visualized by high resolution radioautography in the locus coeruleus of the Rat following intraventricular injection of the met-enkephalin analogue FK 33-824 tritiated with a high specific activity (3H-FK). After administration of a tracer dose of 3H-FK, more than 75% of the radioactivity detected in the locus coeruleus is specifically bound to opiate receptor sites. These are distributed both between and inside neuronal perikarya. After administration of 3H-FK at high concentration, electron microscope radioautography shows the presence of specific opiate binding sites at the level of axo-somatic and axo-dendritic synaptic junctions. These synaptic binding sites could correspond to receptor sites for endogenous enkephalins.

Animals↗

PubMed1979

Ultrastructural radioautography and cytochemistry of lead absorption.

Lead is a universal environmental contaminant absorbed largely through the gastrointestinal tract by unknown mechanisms. Because lead absorption is influenced by iron content in the body and diet, we used ultrastructural radioautography and cytochemistry to study absorption of physiologic lead doses in the rat duodenal epithelial cell and compared these findings to those previously reported for iron absorption. Rat duodenal loops exposed in vivo to 210Pb for 1 minute demonstrated the majority of labels on the microvilli, terminal web, and apical cytoplasm. Specimens exposed to radiolead for 10 minutes demonstrated more abundant labeling with a relative increase in labeling of epithelial cell mitochondria, nuclei and basal cytoplasm, as well as phagocytic cells, endothelial cells, and circulating erythrocytes of the lamina propria. Timm's sulfide-silver method localized trace metals in epithelial cells. After administration of lead, a significant increase in staining was observed in microvilli, mitochondria, non-membrane-bound cytoplasm, and nuclear chromatin. The rapid appearance of absorbed lead in epithelial cell mitochondria and nuclei, as well as phagocytic cells in the lamina propria, was distinctly different from that reported for absorbed iron and suggests different mechanisms for the subcellular transport of these cations. The combination of radioautography and Timm's sulfide-silver staining provides the specificity and resolution needed for ultrastructural evaluation of lead absorption and should be useful in further studies of lead metabolism.

Animals↗

PubMed1983

[Histogenesis on the ovarian Leydig cell tumor--light microscopic dry-mounting radioautography for 3H-cholesterol and electron microscopic cytochemistry for 3 beta-hydroxysteroid dehydrogenase activity].

A case of a virilizing ovarian Leydig cell tumor in a 38 year-old woman with a markedly elevated plasma testosterone level was investigated using light microscopic dry-mounting radioautography and electron microscopic cytochemistry. Following total abdominal hysterectomy and bilateral salpingo-oophorectomy, the plasma testosterone level fell abruptly. Light microscopic dry-mounting radioautography for 3H-cholesterol showed silver grains mainly localized over the cytoplasm of the tumor cells. In the Leydig cell tumor there were three different cell types: Fibroblast-like cells, Leydig cells (steroid-secreting cells) and transitional cells (partially or incompletely differentiated Leydig cells). Reaction products for 3 beta-hydroxysteroid dehydrogenase activity were localized on tubular or lamellar cristae and inner membranes of the mitochondria, and on the membranes of smooth endoplasmic reticulum in the transitional cell as well as in the Leydig cell. From these facts, it is suggested that the Leydig cell tumor is derived from the fibroblast-like cell and the Leydig cell, already has a steroidogenic activity in secreting testosterone.

3-Hydroxysteroid Dehydrogenases↗

PubMed1995

Radioautography in cellular and molecular biology.

A general survey is presented on the most important applications of radioactive compounds as well on fresh as on fixed tissues, with and without immunological reactions, at light and electron microscopic levels. Its goal is to show their flexibility and their extended applications, in comparison with the non-radioactive methods. But radioautography applies as well to non-cellular aspects, such as electrophoretic and chromatographic techniques, permitting a complementary and even more detailed exploration of the molecules investigated at cellular levels. A rapid information is given on the exact denomination of the radioautographic methods, on hybridization in situ and in vitro, on the different blotting techniques used for DNA, RNA and proteins, on semi-quantitation and quantitation of DNA-RNA hybrids, on radioimmunodection by fluorography and on newer filmless radioautographic systems. The organ, body and pharmacological radioautographies belong to the nuclear medicine and have been evocated briefly.

Animals↗

PubMed1964

THE INCORPORATION AND FATE OF H3-TYROSINE IN THE HAIR CORTEX OF RATS OBSERVED BY RADIOAUTOGRAPHY.

The incorporation of H(3)-tyrosine into the protein of the cells in the cortex of rat hair has been investigated by radioautography. In growing hairs, radioactivity is found in the matrix, the upper bulb, and the whole of the keratogenous zone up to the fully keratinized part of the shaft, 10 and 30 minutes after an injection of labelled tyrosine. This is unequivocal evidence of protein synthesis at these sites. There is a very precise relationship between the end of protein synthesis and the hardening of the cortical cells at the top of the keratogenous zone. The way in which the silver grains of the radioautographs are clustered indicates that at 30 minutes after the injection the isotope is distributed more evenly in the matrix and upper bulb than in the top of the keratogenous zone. Possibly this reflects a difference, at these sites, in the cell components engaged in protein synthesis, or in the proteins being synthesized. The fully keratinized and hardened part of the hair was not radioactive at 10 and 30 minutes after the injection of H(3)-tyrosine. The rate at which the radioactivity moves into this region shows that the hair of rats grows 0.9 mm/24 hours. Comparison of the degree of radioactivity along the growing hair in the 30-minute, 12-hour, and 36-hour materials shows conclusively that protein accumulates in the cortical cells during their keratinization. An injection of a labelled amino acid does not behave as an ideal pulse dose; consequently, the grain density over the hair cortex at 36 hours is 100 per cent larger than would be expected if an ideal pulse dose situation existed.

Amino Acids↗

PubMed1977

Formation and turnover of plasma membrane glycoproteins in kidney tubules of young rats and adult mice, as shown by radioautography after an injection of 3H-fucose.

The formation and turnover of the glycoproteins of the plasma membrane have been investigated by quantitative radioautography in the kidney tubules of young rats and adult mice killed at various time intervals after an intravenous injection of 3H-fucose. In young (40 g) rats killed five to ten minutes after the injection, radioautographs of distal tubule cells show that the Golgi apparatus contained about 85% of the cell label. By 30 hours, only 8% of the label remained in this organnele, whereas 67% was in the plasma membrane, indicating that most of the label had migrated from Golgi apparatus to this membrane. Similarly, in proximal tubule cells, about 82% of the label was initially in the Golgi apparatus, but less than 2% remained at 30 hours, at which time 78% was in the plasma membrane. In the latter cells, the apical tubules and vacuoles became heavily labeled before the apical microvilli did and, therefore, may be involved in the transit of label from the Golgi apparatus to the microvillous membrane. The results are interpreted to mean that, in kidney tubule cells, the Golgi apparatus is the site of a continuous incorporation of fucose into glycoproteins and that these migrate to the plasma membrane. In fully formed cells, such a conclusion would imply a continuous turnover of plasma membrane glycoproteins. However, in the rapidly growing kidney of young rats many new cells are added daily, the growth of which might involve net addition as well as turnover of glycoproteins. Accordingly, the experiment has been repeated in adult mice, in which the cells are assumed to be fully formed. Furthermore, since turnover implies eventual decrease of incorporated label, some of the animals have been killed at longer intervals, up to 27 days after injection. In these adult mice, as in young rats, prompt Golgi uptake and subsequent migration of label to the plasma membrane were observed in distal and proximal tubules cells. With time the label content of the plasma membrane decreased gradually, and by 27 days had virtually disappeared. From grain counts, it is concluded that the mean half-life of glycoproteins in the apical membrane of distal tubule cells is about two days, whereas in both the apical and basal membranes of proximal tubule cells, it is slightly over three days.

Age Factors↗

PubMed1982

Radioautography of rat incisor dentin as a continuous record of the incorporation of a single dose of 3H-labeled proline and tyrosine.

After injection of labeled precursors such as 3H-proline or 3H-tyrosine into rats, the incisor dentin contains a continuous and stable record of precursor incorporation into labeled proteins. This record was visualized and quantitated with radioautography in order to evaluate the quantitative changes in enamel where newly secreted proteins randomize with older proteins and both are eventually lost. Up to 4 hours after injection, the pulse-dose was incorporated as a highly labeled band of predentin. The band was entirely within calcified dentin at 2 days and was further removed from new predentin by 4 and 8 days. Dentin which formed proximal to the heavily labeled band contained an amount of radioactivity reflecting the level of labeled precursor available at that time. A standardizing factor for experimental error was obtained by quantitating the reaction in the heavily labeled band, and a post-pulse incorporation factor was determined from the amount of radioactivity added per day as weakly labeled dentin. The variation within the heavily labeled band was assumed to reflect experimental error. The number of grains in the bands were averaged from 4 hours to 8 days to give the standardizing factor. This was multiplied by the ratio of enamel to dentin counts in the same section to obtain a corrected enamel count. In this way the coefficient of variation was improved from a high of 17.2% in uncorrected enamel counts to 2.4% in corrected counts. The post-pulse incorporation factor was higher with tyrosine than with proline. With proline it amounted to 5% increase per day from 1 to 4 days and 2.5% per day from 4 to 8 days after injection. In addition, with 3H-proline the incorporation into predentin increased from 30 minutes to 4 hours. With tyrosine, the counts increased from 30 minutes to 1 hour, but decreased by nearly one third from 1 to 4 hours. This was interpreted as a loss of short-lived matrix proteins including procollagen peptides produced during conversion from procollagen to tropocollagen in the predentin.

Animals↗

PubMed1984

Influence of colchicine and vinblastine on the intracellular migration of secretory and membrane glycoproteins: II. Inhibition of secretion of thyroglobulin in rat thyroid follicular cells as visualized by radioautography after 3H-fucose injection.

Young (40 gm) rats were given a single intravenous injection of colchicine (4.0 mg) or vinblastine (2.0 mg). At 10 min after colchicine and 30 min after vinblastine administration, the rats were injected with 3H-fucose. Control rats received 3H-fucose only. All rats were sacrificed 90 min after 3H-fucose injection and their tissues processed for radioautography. In thyroid follicular cells of control animals, at this time interval, 57% of the total label was associated with colloid and secretory vesicles in the apical cytoplasm while 27% was localized in the Golgi apparatus and neighboring vesicles. In experimental animals, the proportion of label in colloid and apical vesicles was reduced by more than 69% after colchicine and more than 83% after vinblastine treatment. The proportion of label in the Golgi region, on the other hand, increased by more than 125% after colchicine and more than 179% after vinblastine treatment. Within the Golgi region, the great majority of the label was associated with secretory vesicles which accumulated adjacent to the trans face of the Golgi stacks. It is concluded that the drugs do not interfere with passage of newly synthesized thyroglobulin from the Golgi saccules to nearby secretory vesicles, but do inhibit intracellular migration of these vesicles to the cell apex. In most cells the number of vesicles in the apical cytoplasm diminished, but this was not always the case, suggesting that exocytosis may also be partially inhibited. The loss of microtubules in drug-treated cells suggests that the microtubules may be necessary for intracellular transport of thyroglobulin.

Animals↗

PubMed1984

Influence of colchicine and vinblastine on the intracellular migration of secretory and membrane glycoproteins: III. Inhibition of intracellular migration of membrane glycoproteins in rat intestinal columnar cells and hepatocytes as visualized by light and electron-microscope radioautography after 3H-fucose injection.

In the first paper of this series (Bennett et al., 1984), light-microscope radioautographic studies showed that colchicine or vinblastine inhibited intracellular migration of glycoproteins out of the Golgi region in a variety of cell types. In the present work, the effects of these drugs on migration of membrane glycoproteins have been examined at the ultrastructural level in duodenal villous columnar cells and hepatocytes. Young (40 gm) rats were given a single intravenous injection of colchicine (4.0 mg) or vinblastine (2.0 mg). At 10 min after colchicine and 30 min after vinblastine administration, the rats were injected with 3H-fucose. Control rats received 3H-fucose only. All rats were sacrificed 90 min after 3H-fucose injection and their tissues processed for radioautography. In duodenal villous columnar cells, 3H-fucose labeling of the apical plasma membrane was reduced by 51% after colchicine and by 67% after vinblastine treatment; but there was little change in labeling of the lateral plasma membrane. Labeling of the Golgi apparatus increased. This suggests that labeled glycoproteins destined for the apical plasma membrane were inhibited from leaving the Golgi region, while migration to the lateral plasma membrane was not impaired. In hepatocytes, labeling of the sinusoidal plasma membrane was reduced by 83% after colchicine and by 85% after vinblastine treatment. Labeling of the lateral plasma membrane also decreased, although not so dramatically. Labeling of the Golgi apparatus and neighboring secretory vesicles increased. This indicates that the drugs inhibited migration of membrane glycoproteins from the Golgi region to the various portions of the plasma membrane. Accumulation of secretory vesicles at the sinusoidal front suggests that exocytosis may also have been partially inhibited. In both cell types, microtubules almost completely disappeared after drug treatment. Microtubules may, therefore, be necessary for intracellular transport of membrane glycoproteins, although the possibility of a direct action of these drugs on Golgi or plasma membranes must also be considered.

Animals↗

PubMed1988

Phosphoprotein synthesis and secretion by odontoblasts in rat incisors as revealed by electron microscopic radioautography.

The secretory pathway of dentin phosphoproteins in rat incisors was studied by electron microscopic radioautography after the injection of 3H-serine, and the results were compared with those using 3H-proline as a tracer. Five min after injection of 3H-serine, radioactivity was found in the rough endoplasmic reticulum. At 10 min, silver grains were observed over the spherical portions of the cisface of the Golgi apparatus. At 20 min after injection, silver grains were seen over the cylindrical portions of the transface of the Golgi apparatus. The secretory granules showed the strongest reaction from 20 min to 1 hr. At 45 min, a significant labeled band appeared at the mineralization front. At 1 hr, the labeling at the mineralization front began to appear in the mineralized dentin, and after 12 hr this labeled band was located within the mineralized dentin. The pathway of 3H-proline was essentially the same as that of 3H-serine, but 3H-proline moved more slowly than 3H-serine, especially in transit from the rough endoplasmic reticulum to the Golgi apparatus. Secretory granules were heavily labeled from 30 min to 1 hr after injection of 3H-proline; no labeling was found at the mineralization front at 45 min. The labeling seen initially over the predentin was over the mineralized dentin no earlier than 6 hr after injection. The labeling pattern with 3H-serine is closely related to the localization of phosphoproteins, whereas the pattern with 3H-proline reflects the production of collagen rather than of phosphoproteins. The present radioautographic results indicate that dentin phosphoproteins are related to secretory granules and are secreted by odontoblasts at the mineralization front and also that phosphoproteins are involved in the process of mineralization of the circumpulpal dentin.

Animals↗

PubMed1979

Synthesis of secretory and plasma membrane glycoproteins by striated duct cells of rat salivary glands as visualized by radioautography after 3H-fucose injection.

The ability of the striated ducts of rat salivary glands to incorporate 3H-fucose into glycoprotein was studied by light and electron microscope radioautography. At 3.5 to 20 minutes after intravenous injection, the majority of the radioautographic grains in the ducts of the parotid gland were localized to the Golgi apparatus. By 40 minutes, the percentage of grains over the Golgi apparatus had decreased; a corresponding increase in grains occurred over small (0.1-0.4 micrometer) apical granules and the highly infolded basal and lateral plasma membranes. By two hours, less than 10% of the label was associated with the Golgi apparatus, while 26% and 28% were attributed to the apical granules and plasma membrane, respectively. By 8 to 12 hours after injection, the number of grains over the apical cytoplasm had decreased, suggesint luminal discharge of the apical granules. In contrast, the basal and lateral plasma membranes remained labeled up to 30 hours after injection as judged by the distribution of grains in light microscope radioautographs. Mitochondria appeared capable of independent incorporation of fucose, accounting for about 20% of the grains from ten minutes to two hours after injection. Comparable results were obtained in the striated ducts of the submandibular and sublingual glands. These results indicate that the striated duct cells readily incorporate 3H-fucose into newly-synthesized glycoproteins. A portion of these are secretory glycoproteins which are packaged and stored in the apical granules, and a portion are membrane glycoproteins which are incorporated into the extensive plasma membrane of these cells.

Animals↗

PubMed1982

Cell flux through S phase in the mouse duodenal epithelium determined by cell sorting and radioautography.

An accumulation of cells in early S phase was observed in normal mouse duodenal epithelium studied with flow cytometry (Cheng and Bjerknes, 1982). To determine if this accumulation of cells was the result of a lower rate of DNA synthesis, animals were given a single injection of 3H-thymidine and the epithelium collected one hour later. The epithelium was processed for flow cytometry. Seven sort windows were established in different portions of the DNA histogram. Cells from each window were sorted onto glass slides that were then processed for radioautography. The number of silver grains over the nuclei of each sorted population was counted. It was found that cells in early S phase had significantly fewer grains over their nuclei than did mid- or late-S phase cells. We conclude that the accumulation of cells in early S phase is due, at least in part, to a lower rate of DNA synthesis in early than in mid or late S phase.

Animals↗

PubMed1986

The effect of streptozotocin on the secretory activity of ameloblasts in rat incisor as revealed by radioautography after 3H-proline administration.

The effect of a diabetogenic dose of streptozotocin on the secretory activity of ameloblasts was investigated in the rat incisor by radioautography. One group of male Sprague-Dawley rats was injected intravenously with streptozotocin in citrate buffer (pH 4.5). One hour later, this group was again injected intravenously with 3H-proline (2 mCi/kg). A control group of animals was injected with 3H-proline only. All the animals were sacrificed in groups of three at 5 min, 1 h, 2 h, 4 h and 8 h after 3H-proline injection by perfusion with 3% phosphate-buffered formaldehyde followed by an additional perfusion with 2.5% phosphate-buffered glutaraldehyde. The incisors were extracted with the jaws, demineralized, and prepared for radioautographic observations and analysis. The principal effects of streptozotocin were as follows: There was an inhibition of 3H-proline incorporation into the secretory ameloblasts at 5 min after injection. This was followed by a larger uptake and a slower passage of the label out of the cells into the enamel matrix than that seen in the control sample. Finally, there was a slower secretion of labeled proteins out of Tomes' processes between 1 and 4 h after injection. Therefore, streptozotocin had a temporary inhibitory effect on the incorporation and secretion of 3H-proline by the secretory ameloblasts of the rat incisor. This effect was present for about 4 h and was completely reversed 9 h after streptozotocin injection.

Ameloblasts↗

PubMed1986

Dynamic features of duct epithelial cells in the mouse pancreas as shown by radioautography following continuous 3H-thymidine infusion.

The possibility of turnover of the epithelial duct cells was examined in the adult mouse pancreas by radioautography following continuous administration of 3H-thymidine for periods varying from 1 h to 60 days. One hour after an injection of 3H-thymidine, the label observed in small and large ducts was low but increased with the duration of the continuous infusion of 3H-thymidine and reached a level of about 67% cells labeled after 60 days. The rate of duct cell labeling was estimated from the regression line of the labeling index vs. time in four types of ducts classified according to their inner diameter and the presence of the adventitia and was given as 0.60% cells per day in small (adventitia-free) ducts (phi 4-12 micron), 0.89%, 1.02%, and 1.23% cells per day in large (adventitia-including) ducts (phi 15-29, 30-49, and 50-160 micron respectively). In contrast, the labeling index of aciner cells after a 60-day infusion indicated an addition of only 0.02-0.07% per day, and that of islet cells 0.14-0.22% per day. It is known that most parenchymal cells belong to either expanding or renewing cell populations. The acinar cells of the pancreas have been shown to constitute an expanding population, a conclusion confirmed by the low addition of cells observed in the present work. However, the relatively high rate of cell addition in the duct epithelia indicates that they may turn over in a period of 2.7 months in the case of large ducts and 5.6 months in the case of small ducts.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1986

In vivo demonstration by radioautography of binding sites for insulin in liver, kidney, and calcified tissues of the rat.

An in vivo binding assay using radioautography was employed to visualize insulin receptors in rat tissues. Two and one-half minutes after the intravenous injection of 125I-insulin, free hormone was separated from bound hormone by whole body perfusion with lactated Ringer's solution followed by perfusion with glutaraldehyde. The localization of bound hormone, fixed in situ by perfusion with glutaraldehyde, was determined. Nonspecific binding of labeled insulin was noted in the proximal convoluted tubules of the kidney cortex, prebone and adjacent bone, predentin and adjacent dentin, and enamel. Specific binding sites were observed at the periphery of hepatocytes, over osteoblasts, and in relation to the endothelial cells of fenestrated capillaries within the papillary layer of the maturation zone of the incisors.

Animals↗

PubMed1986

Osteodentin formation in rat incisor as visualized by radioautography after 3H-proline administration.

Osteodentin formation was studied in rat incisor pulp after adriamycin administration. Male Sprague Dawley rats (100 +/- 5 gm) were injected intravenously with adriamycin (5 mg/kg body weight), and after 7 days they were again injected intravenously with 3H-proline (3 microCi/gm). These animals were killed in groups of three from 5 minutes to 4 hours after proline injection by perfusion with 3% phosphate-buffered formaldehyde followed by 2.5% phosphate-buffered glutaraldehyde. Control animals injected with only physiological saline, and 7 days later with 3H-proline (3 microCi/gm), and were killed at the same time intervals. Radioautography on sections showing osteodentin formation revealed that at 5 minutes after 3H-proline injection the labeling was located over the cells associated with the osteodentin matrix. At 1 hour after injection the labeling was located over the cells and the matrix, while at 4 hours the labeling was seen only over the matrix. It therefore appears that at least a proline-containing component of the osteodentin matrix is synthesized and secreted by the cells associated with it.

Animals↗

PubMed1986

The distribution of 3H-proline in alveolar bone of the mouse as seen by radioautography.

Previous studies of the turnover of alveolar bone collagenous proteins have devoted little attention to the variable patterns in this process caused by bone remodeling. The present study seeks to document changes resulting from physiologic tooth movements in the incorporation and removal of the 3H-proline label within the interdental septum of alveolar bone. One week following 3H-proline injection, three zones could be distinguished: the appositional band, new bone, and old bone. Radioautography demonstrated that formation of new bone on the distal wall of the septum entrapped fibers of the periodontal ligament to create Sharpey's fibers. At the alveolar crest, new bone entrapped transseptal fibers to form transalveolar Sharpey's fibers. Grain counts were made within each area and over the total septum and were compared statistically. The data strongly suggested regional variations in protein remodeling. Counts from old and new bone were significantly different from the total septum or the appositional band (P less than .001). Regression lines were drawn to represent incorporation and removal of the isotope; slopes were calculated and compared statistically. The rate of incorporation and removal was significantly greater in the appositional band and in the total septum in comparison to old bone (P less than .001). The rates of incorporation and removal in the appositional band, old bone, and total septum were significantly different (P less than .001). Half-life of the labeled protein of old bone was 16.78 weeks; in the appositional band, 7.66 weeks; and in the total septum, 7.64 weeks. These data suggest that regional variations in collagen remodeling must be considered in a study of interdental bone and that the total septal grain counts are not indicative of the remodeling in the component zones.

Alveolar Process↗

PubMed1988

Effect of colchicine on the transport of precursor enamel protein in secretory ameloblasts studied by 3H-proline radioautography in vitro.

The incorporation of 3H-proline into the secretory ameloblasts of rat molar tooth germs cultured with or without colchicine was studied by light and electron microscope radioautography to determine the function of microtubules in the transport of precursor enamel protein from the rough-surfaced endoplasmic reticulum (rER) to the Golgi cisternae. The grain counts over the transitional vesicles, which accumulated in various cellular regions with colchicine treatment, continued to increase with chase time, unlike in controls. At 30 and 90 min chase, these counts were significantly higher than in controls. Moreover, the total grain count over the organelles (rER, pale granules, and transitional vesicles), which are positioned before the Golgi cisternae in the synthetic pathway, maintained a significantly higher level at 90 min chase in colchicine-treated tooth germs than in controls. The transport of synthesized protein to the Golgi cisternae via transitional vesicles was suppressed in colchicine-treated tooth germs. Some grains appeared with time over pale granular materials that appeared in the intercellular spaces of secretory ameloblasts with colchicine treatment. However, at each chase period, the grain count over pale granular materials was not so high as the count over the enamel in control. The present results indicate that colchicine affects the transport of newly synthesized protein from the rER to the Golgi cisterna via transitional vesicles, probably by interfering with the oriented transport related to microtubular function. It is suggested that the microtubular system may be concerned with the movement of the transitional vesicles.

Ameloblasts↗