Light and electron microscopic observations of fabrication, release, and fate of biphasic secretion granules produced by epididymal epithelial principal cells of the fan-throated lizardSitana ponticeriana cuvier

2006 ◽  
Vol 267 (6) ◽  
pp. 713-729 ◽  
Author(s):  
M.A. Akbarsha ◽  
V. Tamilarasan ◽  
B. Kadalmani
Keyword(s):  
Electron Microscopic ◽  
Principal Cells ◽  
Secretion Granules

scholarly journals Immunohistochemical localization of renin in the human kidney.

1982 ◽  
Vol 30 (5) ◽  
pp. 459-465 ◽  
Author(s):  
T Faraggiana ◽  
E Gresik ◽  
T Tanaka ◽  
T Inagami ◽  
A Lupo
Keyword(s):  
Plasma Renin Activity ◽  
Protein A ◽  
Electron Microscopic Observation ◽  
Human Kidney ◽  
Plasma Renin ◽  
Renin Activity ◽  
Afferent Arteriole ◽  
Epithelioid Cells ◽  
Electron Microscopic ◽  
Secretion Granules

By using an antiserum to purified human renal renin, renin was localized immunocytochemically in the human kidney under normal and various pathological conditions by the unlabeled antibody enzyme light microscope: (LM) and protein A-gold colloid electron microscope (EM) procedures. In the normal kidney, renin was confined to the epithelioid cells of the afferent arteriole of the juxtaglomerular apparatus (JGA). These cells were small and few, and always in the immediate neighborhood of the glomerulus. Fine structural analysis showed renin only in the secretion granules of the epitheloid cells. All granules within a given cell were stained with comparable intensity. In cases of renal artery stenosis (ischemic kidney) and of Bartter's syndrome, renin-positive epithelioid cells were larger, showed increased staining intensity, and were often found along the afferent arteriole at some distance from the glomerulus. Again, by electron microscopic observation, renin was seen only in secretion granules of epithelioid cells. In all of the above pathologic cases, plasma renin activity was very high. However, in the other nephropathies studied, renin staining in the kidney resembled that seen in normal kidneys, even when levels of plasma renin activity were quite high.

scholarly journals Identification of immunoreactive sites in bovine parathyroid cells to antibodies raised against the NH2-terminal sequence of parathyroid hormone.

1979 ◽  
Vol 27 (8) ◽  
pp. 1209-1214 ◽  
Author(s):  
W Limacher ◽  
P Wild ◽  
E Manser ◽  
H Lutz
Keyword(s):  
Parathyroid Hormone ◽  
Protein A ◽  
Electron Microscopic Level ◽  
Enzyme Linked Immunosorbent Assay ◽  
Staphylococcal Protein A ◽  
Terminal Sequence ◽  
Electron Microscopic ◽  
Secretion Granules ◽  
Parenchymal Cells ◽  
Bovine Parathyroid Hormone

The NH2-terminal sequence of bovine parathyroid hormone (1-84) was localized with different immunocytochemical methods on the light and electron microscopic level in bovine parathyroid glands and in isolated bovine parathyroid parenchymal cells. The peroxidase labeled staphylococcal protein A and the peroxidase anti-peroxidase method were found to be advantageous for light and electron microscopic localization, respectively. Reaction product was found light microscopically in the cytoplasma of the parenchymal cells and electron microscopically largely over the secretion granules of the parenchymal cells. The immunoreactive sites were subsequently identified to represent only intact parathyroid hormone (1-84) by gel electrophoresis derived enzyme linked immunosorbent assay.

scholarly journals A neonatal secretory protein associated with secretion granule membranes in developing rat salivary glands.

1991 ◽  
Vol 39 (12) ◽  
pp. 1693-1706 ◽  
Author(s):  
W D Ball ◽  
A R Hand ◽  
J E Moreira
Keyword(s):  
Acinar Cells ◽  
Secretory Protein ◽  
Postnatal Life ◽  
Type I ◽  
Secretion Granule ◽  
Electron Microscopic ◽  
Type Iii ◽  
Type I Cells ◽  
Secretion Granules ◽  
I Cells

In the perinatal submandibular gland, the secretion granules of Type I cells contain protein C (89 KD) and those of Type III cells have Bl-immunoreactive proteins (Bl-IP, 23.5-27.5 KD). In this report we used immunocytochemistry at the light and electron microscopic levels to describe the developmental distribution and localization of protein D (175 KD), which is secreted by both Type I and Type III cells. At its first appearance in Type I cells at 18 days and in Type III cells at 19 days post conception, protein D immunoreactivity (D-IR) is associated with secretion granule membranes; this is more pronounced in Type I than in Type III cells. In early postnatal life the label remains membrane associated, but as Type III cells differentiate into seromucous acinar cells, the lower level of label present in these cells is found in the granule content. Label is found associated with the membrane in secretion granules of Type I cells as long as these cells are identifiable in acini, and subsequent to this similarly labeled cells are seen in intercalated ducts. In the sublingual gland (SLG), D-IR is membrane associated in secretion granules of serous demilune cells, and is present in the secretion granule content in mucous acinar cells. D-IR is also found in the lingual serous (von Ebner's) glands, lacrimal gland, and tracheal glands, primarily in the ducts, where it is localized in the content of secretion granules.

Dynein and dynactin colocalize with AQP2 water channels in intracellular vesicles from kidney collecting duct

1998 ◽  
Vol 274 (2) ◽  
pp. F384-F394 ◽  
Author(s):  
David Marples ◽  
Trina A. Schroer ◽  
Nikolai Ahrens ◽  
Ann Taylor ◽  
Mark A. Knepper ◽  
...  
Keyword(s):  
Collecting Duct ◽  
Motor Protein ◽  
Cytoplasmic Dynein ◽  
Electron Microscopic Level ◽  
Electron Microscopic ◽  
Principal Cells ◽  
Intracellular Vesicles ◽  
Dynactin Complex ◽  
Intermediate Chains ◽  
Regulated Trafficking

We investigated whether the motor protein cytoplasmic dynein and dynactin, a protein complex thought to link dynein with vesicles, are present in rat renal collecting ducts and associated with aquaporin-2 (AQP2)-bearing vesicles. Immunoblotting demonstrated cytoplasmic dynein heavy and intermediate chains in kidney, with relative expression levels of inner medulla > outer medulla > cortex. In addition to being present in cytoplasmic fractions, dynein was abundant in membrane fractions enriched for intracellular vesicles. Dynactin was also abundant in membrane fractions enriched for intracellular vesicles. Furthermore, both dynactin and dynein were present in vesicles specifically immunoisolated using anti-AQP2 antibodies. Immunocytochemistry revealed labeling for dynein in the collecting duct principal cells with a pattern consistent with labeling of intracellular vesicles. Moreover, quantitative double immunogold labeling confirmed colocalization of AQP2 and dynein in the same vesicles at the electron microscopic level. Thus the microtubule-associated motor protein dynein and the associated dynactin complex are present in rat renal collecting duct principal cells and are associated with intracellular vesicles, including those bearing AQP2, consistent with the view that dynein and dynactin are involved in vasopressin-regulated trafficking of AQP2-bearing vesicles.

Ultrastructural Studies of the Femoral Tendon Cells in the Freshly Molted Cockroach Nymph

1969 ◽  
Vol 27 ◽  
pp. 254-255
Author(s):  
Martin Hagopian ◽  
David Spiro
Keyword(s):  
Endoplasmic Reticulum ◽  
Electron Microscopic ◽  
Ultrastructural Studies ◽  
Leucophaea Maderae ◽  
Large Numbers ◽  
Secretion Granules ◽  
Tendon Cells ◽  
Microscopic Studies ◽  
Characteristic Features ◽  
Oriented Parallel

In our electron microscopic studies of the freshly molted cockroach, Leucophaea maderae, the tendon (epidermal) cells in the nymph's femur show some characteristic features which have hitherto not been described. Within an hour of ecdysis the majority of tendon cells are attached to the cuticle and adjacent tendon cells; others are joined to the cuticle on one side and fastened to muscle on the opposite side; and some are apparently migrating free in the hemolymph. The tendon cells, whether adjacent to the cuticle or within the hemolymph, display very large numbers of microtubules and also have regions which contain rough endoplasmic reticulum and secretion granules (Fig. 1). The microtubules are oriented parallel to the myofilaments in underlying muscle cells.

Scanning Electron Microscopic study on chicken pituitary cells

1989 ◽  
Vol 47 ◽  
pp. 972-973
Author(s):  
S. Tai ◽  
C. Velasquez
Keyword(s):  
Cell Types ◽  
Secretory Cells ◽  
Specific Cell ◽  
Pituitary Cells ◽  
Electron Microscopic ◽  
3 Dimensional ◽  
Transmission Electron ◽  
Scanning Electron Microscopic Study ◽  
Secretion Granules ◽  
Pituitary Glands

The cytology and histology of the vertebrate pituitary glands have been studied extensively under light microscopy and transmission electron microscopy. These informations form the basis for the generally accepted concept that the specific cell types synthesize, store and release their particular hormones. These hormonal products are stored in membrane-bound secretion granules in the cytoplasm.Tanaka developed the 0 smium-DMS 0-0 smium (ODO) method which can remove the excess cytoplasmic matrices from the frozen-fractured surface of pre-fixed cells and revealed intracellular structures of many kind s of cells from liver, retina, etc. In this work, we have used the ODO method and Field Emission SEM to obtain 3-dimensional images of the fine structure of pituitary cells, as a new approach to have a better idea about the intracellular organization of the hormone secretory cells .Chicken pituitary glands were fixed in 0.5% glutaraldehyde in 0.2M phosphate buffer(pH=7.2) for ½ h; rinsed with the same buffer; postfixed in 0.5% OsO4 for another ½h. After been rinsed throughly, specimens were passed through 25% and 50% dimethyl sulfoxide(DMSO) solution for 30 minutes each.

Optogenetic study of central medial and paraventricular thalamic projections to the basolateral amygdala

2021 ◽  
Author(s):  
Nowrin Ahmed ◽  
Drew B Headley ◽  
Denis Pare
Keyword(s):  
Basolateral Amygdala ◽  
Feedback Inhibition ◽  
Thalamic Nuclei ◽  
Electron Microscopic ◽  
Local Circuit ◽  
Principal Cells ◽  
Axon Terminals ◽  
Microscopic Studies ◽  
The Impact

The central medial (CMT) and paraventricular (PVT) thalamic nuclei project strongly to the basolateral amygdala (BL). Similarities between the responsiveness of CMT, PVT, and BL neurons suggest that these nuclei strongly influence BL activity. Supporting this possibility, an electron microscopic study reported that in contrast with other extrinsic afferents, CMT and PVT axon terminals form very few synapses with BL interneurons. However, since limited sampling is a concern in electron microscopic studies, the present investigation was undertaken to compare the impact of CMT and PVT thalamic inputs on principal and local-circuit BL neurons using optogenetic methods and whole-cell recordings in vitro. Optogenetic stimulation of CMT and PVT axons elicited glutamatergic EPSPs or EPSCs in principal cells and interneurons, but they generally had a longer latency in interneurons. Moreover, after blockade of polysynaptic interactions with tetrodotoxin (TTX), a lower proportion of interneurons (50%) than principal cells (90%) remained responsive to CMT and PVT inputs. While the presence of TTX-resistant responses in some interneurons indicates that CMT and PVT inputs directly contact some local-circuit cells, their lower incidence and amplitude after TTX suggest that CMT and PVT inputs form fewer synapses with them than with principal BL cells. Together, these results indicate that CMT and PVT inputs mainly contact principal BL neurons such that when CMT or PVT neurons fire, limited feed-forward inhibition counters their excitatory influence over principal BL cells. However, CMT and PVT axons can also recruit interneurons indirectly, via the activation of principal cells, thereby generating feedback inhibition.

A Reproducible Selective Stain for Cardiac Sarcoplasmic Reticulum

1974 ◽  
Vol 32 ◽  
pp. 214-215
Author(s):  
R. A. Waugh ◽  
J. R. Sommer
Keyword(s):  
Complex System ◽  
Electron Microscope ◽  
Sarcoplasmic Reticulum ◽  
Transmission Electron Microscope ◽  
Electron Microscopic ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Transmission Electron

Cardiac sarcoplasmic reticulum (SR) is a complex system of intracellular tubules that, due to their small size and juxtaposition to such electron-dense structures as mitochondria and myofibrils, are often inconspicuous in conventionally prepared electron microscopic material. This study reports a method with which the SR is selectively “stained” which facilitates visualizationwith the transmission electron microscope.

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