Apical cytoplasm

About: Apical cytoplasm is a research topic. Over the lifetime, 1080 publications have been published within this topic receiving 36131 citations.

The epithelium of the excretory duct of the human submandibular gland: a transmission and scanning electron microscopic study.

Abstract: The duct of the human submandibular gland (Wharton) is lined by a pseudostratified epithelium consisting of principal and basal cells. Scattered among them are a few goblet and ciliated cells. The principal cells are columnar in shape with many mitochondria, numerous dense bodies and a central nucleus with some indentations. Their apical cytoplasm shows a number of clear vesicles, some of which are reactive to silver and are extruded by exocytosis into the lumen. Other vesicles, which are unreactive, may represent the products of the absorption process. A mechanism of apocrine secretion is also observed in the principal cells. Thus, with regard to its functions, the duct of the human submandibular gland modifies the composition of saliva by adding a secretory component to it. This latter material is derived from the goblet cells but chiefly from merocrine (exocytosis) and apocrine secretion of principal cells.

Identification of a Member of a New RNase A Family Specifically Secreted by Epididymal Caput Epithelium

Abstract: In this study, we purified the first member of a new ribonuclease (RNase) A family from fluid of the proximal caput of the boar epididymis. This protein, named ‘‘Train A,’’ is the most abundant compound secreted in the anterior part of the boar epididymis. After 2D electrophoresis, it is characterized by more than 10 isoforms ranging in size from 26 to 33 kDa and pI from 5 to 8.5. Several tryptic peptides were N-terminal sequenced, and an antiserum against one of these peptides was obtained. The protein was immunolocalized in the epididymal epithelium of the proximal caput, especially in the Golgi zone and the apical cytoplasm of the principal cells. In the lumen, spermatozoa were negative but droplets of reaction product were observed within the lumen. Full lengths of Train A cDNA were obtained from a lgt11 boar caput epididymis library and sequenced. The deduced protein is composed of 213 amino acids, including a 23-amino acid peptide signal and a potential N-glycosylation site. The mRNA of this protein has been retrieved and partially sequenced in the bull, horse, and ram, and homologous cDNA is found in databanks for the rat, mouse, and human. All the sequences are highly conserved between species. This protein and its mRNA are male-specific and exclusively expressed in the proximal caput of the epididymis, the only site where they have been found. Train A presents an RNase A family motif in its sequence. The RNase A family is a group of several short proteins (20‐14 kDa) with greater and lesser degrees of ribonucleolytic activity and with supposed different roles in vivo. However, the presence of a long-conserved N-terminal specific sequence and the absence of RNase catalytic site for Train A indicate that Train A protein is a member of a new family of RNase A.

Helical structure in the apical tubules of several absorbing epithelia. Kidney proximal tubule, visceral yolk sac and ductuli efferentes.

Abstract: Unique and highly ordered structures were discovered in the so-called apical tubules of several absorbing epithelia (kidney proximal tubule, visceral yolk sac and ductuli efferentes) fixed in situ with a mixture of formaldehyde, glutaraldehyde and osmium tetroxide. The apical tubules were especially numerous in the apical cytoplasm, in addition to the invaginations of the apical plasma membrane, newly formed endocytic vesicles and large endocytic vacuoles. They showed a cylindrical structure (∼80 nm in diameter) limited by a smooth membrane. Helically wound parallel rows of particles (∼11 nm in diameter) were found in the apical tubules in close proximity to their limiting membrane. The structure of the helix was determined by following the rows through serial sections and semithin sections, and was found to be a left-handed quadruple helix. These particles surround an electron-lucent cylinder (∼35 nm in diameter), containing at its center a single row of particles (∼9 nm in diameter). The apical tubules with the luminal specializations were not seen in continuity with the apical plasma membrane, but were frequently connected with the large endocytic vacuoles, which were present in the deeper levels of the apical cytoplasm. From these observations, it is suggested that the apical tubules are not derivatives of the apical plasma membrane; rather, they represent an intracellular compartment, which is morphologically related to the large endocytic vacuoles.

Intracellular transport and secretion of fibroin in the posterior silk gland of the silkworm Bombyx mori.

Abstract: Intracellular transport and secretion of fibroin in the posterior silk gland cells of the silkworm, Bombyx mori, were investigated in relation to the radial microtubule and circular microtubule-microfilament systems of the cells. The silk glands were pulse-labelled for 3 min with [3H]glycine in vitro and then chased in media containing excess cold glycine and in some cases antimitotic reagents (colchicine or vinblastine) or cytochalasin (B or D), and the flow of the label in the glands was investigated by radioautography. It was revealed that the label initially located over the rough endoplasmic reticulum subsequently moves to the Golgi bodies to be condensed there. The secretory granules of fibroin or fibroin globules thus formed are transported via the radial microtubule system to the apical cytoplasm to be secreted there under some regulation by the circular microtubule-microfilament system. In the presence of colchicine or vinblastine, the secretion of fibroin was suppressed an marked accumulation of fibroin globules in the Golgi regions was observed, while in the presence of cytochalasin B or D the secretion was accelerated and extensive invagination of the luminal surface, which was probably due to the serial exocytosis of fibroin globules, was observed. These results suggest that the radial microtubule system and the circular microtubule-microfilament system are responsible for intracellular transport of fibroin globules from Golgi bodies to the apical cytoplasm and secretion by exocytosis at the luminal surface, respectively.