scholarly journals Ultrastructural localization of glycoconjugates in human bronchial glands: the subcellular organization of N- and O-linked oligosaccharide chains.

1992 ◽  
Vol 40 (2) ◽  
pp. 265-274 ◽  
Author(s):  
M T Castells ◽  
J Ballesta ◽  
J F Madrid ◽  
J A Martínez-Menárguez ◽  
M Avilés
Keyword(s):  
Secretory Granules ◽  
Ultrastructural Localization ◽  
Lectin Histochemistry ◽  
Electron Microscopic Level ◽  
Binding Pattern ◽  
Electron Microscopic ◽  
Beta Elimination ◽  
Sugar Chains ◽  
Bronchial Glands ◽  
Peptide Region

We investigated the glycoconjugates of the human bronchial glands at light and electron microscopic level by means of lectin histochemistry in combination with neuraminidase digestion and beta-elimination reaction. Both direct and indirect techniques using lectin-peroxidase, lectin-gold, and glycoprotein-gold complexes were applied. The binding pattern of the six lectins (ConA, HPA, DSA, WGA, LEA, and PNA) used in the present study suggests that mucous and serous cells of human bronchial glands contain both N- and O-glycosylated proteins in the secretory granules. Asparagine-linked oligosaccharides containing Gal(beta-1,4) GlcNAc and Man residues were abundant in serous cells. The demonstration of both the terminal Neu 5Ac (alpha-2,3, or 6) Gal (beta-1,4) GlcNAc sequence in the N-linked oligosaccharides of mucous cells and the terminal disaccharide Gal (beta-1,4) GlcNAc in the N-linked oligosaccharide chains of serous cells suggests the existence of complex type sugar chains N-glycosidically linked to the peptide region of the glycoproteins. The binding pattern of the DSA and the neuraminidase-DSA sequence provides evidence for the existence of sialyltransferase activity in the forming mucous granules of mucous bronchial cells.

ULTRASTRUCTURAL MORPHOMETRY OF SPARSELY GRANULATED PROLACTIN CELL ADENOMAS OF THE HUMAN PITUITARY

1978 ◽  
Vol 89 (3) ◽  
pp. 521-529 ◽  
Author(s):  
D. J. McComb ◽  
K. Kovacs
Keyword(s):  
Endoplasmic Reticulum ◽  
Secretory Granules ◽  
Volume Density ◽  
Microscopic Level ◽  
Electron Microscopic Level ◽  
Prolactin Cells ◽  
Electron Microscopic ◽  
Human Pituitary ◽  
Hormone Synthesis ◽  
Highly Active

ABSTRACT Fifteen sparsely granulated prolactin-producing adenomas and 10 non-tumourous adenohypophyses, removed by surgical hypophysectomy, have been studied using morphometry at the electron microscopic level. Compared to non-tumourous prolactin cells, sparsely granulated adenomatous prolactin cells showed a significant decrease in diameter and volume density of secretory granules and an increased volume density of rough-surfaced endoplasmic reticulum and Golgi apparatus. The volume density of mitochondria remained unchanged. These results indicate that the cells of the adenoma are in a highly active functional state. It appears that the equilibrium between hormone synthesis, storage and release is altered in adenomatous prolactin cells.

scholarly journals Immunocytochemical localization of renin in kidneys and submandibular glands of SWR/J and C57BL/6J mice.

1980 ◽  
Vol 28 (10) ◽  
pp. 1113-1118 ◽  
Author(s):  
T Tanaka ◽  
E W Gresik ◽  
A M Michelakis ◽  
T Barka
Keyword(s):  
Submandibular Gland ◽  
High Strain ◽  
Secretory Granules ◽  
Juxtaglomerular Apparatus ◽  
Electron Microscopic Level ◽  
Epithelioid Cells ◽  
Electron Microscopic ◽  
Submandibular Glands ◽  
Morphometric Analyses ◽  
Convoluted Tubules

By using antibodies against highly purified submandibular gland renin, renin was localized immunocytochemically at the light and electron microscopic level in the submandibular glands and kidneys of adult male SWR/J and C57BL/6J mice. In accord with the data of Wilson et al. (Proc Natl Acad Sci USA 75:1185, 1977), renin was demonstrable only in the submandibular glands of SWR/J mice (high strain), where it was confined to the secretory granules of the granular convoluted tubules. In the kidneys of both strains, renin was confined to epithelioid cells of the juxtaglomerular apparatus. Electron microscopically immunostaining was restricted to the granules of the juxtaglomerular epitheliod cells. Morphometric analyses suggested that the kidney of the C57BL/6J mice contained more immunoreactive complexes per unit volume of cortex than SWR/J mice kidney. The data indicate that submandibular gland renin cross-reacts with kidney renin, but that genetic controls of these polypeptides in the two organs are independent.

scholarly journals Electron immunocytochemical localization of enkephalin-like material in catecholamine-containing cells of the carotid body, the adrenal medulla, and in pheochromocytomas of man and other mammals.

1982 ◽  
Vol 30 (7) ◽  
pp. 682-690 ◽  
Author(s):  
I M Varndell ◽  
F J Tapia ◽  
J De Mey ◽  
R A Rush ◽  
S R Bloom ◽  
...  
Keyword(s):  
Adrenal Medulla ◽  
Carotid Body ◽  
Secretory Granules ◽  
Microscopic Level ◽  
Electron Microscopic Level ◽  
Immunocytochemical Localization ◽  
Electron Microscopic ◽  
Antibody Technique ◽  
Dopamine Beta Hydroxylase ◽  
Carotid Bodies

Enkephalin-like immunoreactivity has been localized to electron-dense secretory granules of cat and piglet carotid bodies and adrenal medullae, horse adrenal medulla, and also to human adrenal medulla and pheochromocytomas using a gold-labeled antibody technique performed at the electron microscopic level. The same granules were also demonstrated to exhibit dopamine-beta-hydroxylase-like immunoreactivity, which suggests a granular colocalization of amines and peptides in catecholamine-storing cells.

scholarly journals Ultrastructural localization of guanylate cyclase in bone cells.

1991 ◽  
Vol 39 (4) ◽  
pp. 529-535 ◽  
Author(s):  
O Fukushima ◽  
C V Gay
Keyword(s):  
Plasma Membrane ◽  
Guanylate Cyclase ◽  
Bone Cells ◽  
Ultrastructural Localization ◽  
Microscopic Level ◽  
Electron Microscopic Level ◽  
Lead Citrate ◽  
Free Medium ◽  
Membrane Guanylate Cyclase ◽  
Electron Microscopic

Guanylyl imidodiphosphate (GMP-PNP) hydrolyzing enzyme activity as a means of detecting plasma membrane guanylate cyclase was demonstrated in osteoblasts of chicken tibial metaphysis using a lead citrate histochemical method at the electron microscopic level. Activity was not discerned in osteoclasts or osteocytes. The reaction product development was completely abolished when the sections were incubated with substrate-free or MnCl2-free medium. Guanylate-(beta, gamma-methylene) diphosphate (GMP-PCP) was a less effective substrate than GMP-PNP, and Mn++ was a stronger stimulator than Mg++. No reaction product was observed on the plasma membrane of osteoblasts when beta-glycerophosphate or p-nitrophenylphosphate was used as substrate instead of GMP-PNP. The results implicate guanylate cyclase as a significant effector of osteoblast regulation at the site of the plasma membrane.

scholarly journals Immunoelectron microscopic localization of estrogen receptor with monoclonal estrophilin antibodies.

1985 ◽  
Vol 33 (9) ◽  
pp. 915-924 ◽  
Author(s):  
M F Press ◽  
N A Nousek-Goebl ◽  
G L Greene
Keyword(s):  
Estrogen Receptor ◽  
Ultrastructural Localization ◽  
Microscopic Level ◽  
Electron Microscopic Level ◽  
Nuclear Staining ◽  
Cytoplasmic Localization ◽  
Electron Microscopic ◽  
Tissue Sections ◽  
Receptor Antibodies ◽  
Microscopic Techniques

The recent production of a series of monoclonal estrophilin (estrogen receptor) antibodies recognizing estrogen receptor derived from a wide variety of animals and target tissues permits the development of immunoelectron microscopic techniques for identifying estrogen receptor. We have determined suitable conditions for the ultrastructural localization of estrogen receptor in tissue sections. Localization of receptor was observed in the euchromatin, but not in the marginated heterochromatin or nucleoli of epithelial and stromal nuclei of human endometrium. Competition studies indicate that only estrogen receptor specifically inhibits nuclear staining. The absence of any specific cytoplasmic localization at the electron-microscopic level is consistent with earlier light-microscopic observations and suggests that the majority of the cellular pool of estrophilin exists in the nucleus of hormone-responsive cells.

Ultrastructural localization of soluble and insoluble 3H-methyl prednisolone as revealed by electron microscopic dry-mounting radioautography

1978 ◽  
Vol 36 (2) ◽  
pp. 40-41
Author(s):  
T. Nagata ◽  
K. Yoshida ◽  
S. Ohno ◽  
F. Murata
Keyword(s):  
Mouse Liver ◽  
Sodium Succinate ◽  
Ultrastructural Localization ◽  
Microscopic Level ◽  
Electron Microscopic Level ◽  
Electron Microscopic ◽  
Methyl Prednisolone ◽  
Freeze Dried ◽  
Emulsion Films

IntroductionSince the recent improvements in both techniques and development in equipments at our laboratory or others, the dry-mounting procedures for radioautography facilitated the wide application of them for the study of soluble compounds such as nucleic acid precursors, amino acids, carbohydrates, lipids and steroids at both the light and electron microscopic levels. The purpose of this paper is to demonstrate ultrastructural localization of both soluble and insoluble 3H-labeled methyl prednisolone, a synthetic corticosteroid, by means of dry-mounting procedure at the electron microscopic level.Materials and MethodsMouse liver slices obtained from a male mouse and cultured HeLa cells were pulse- labeled in vitro in Eagle's MEM containing 6α-methyl prednisolone-1,2-T sodium succinate (100μCi/ml) for 1 hour.Some specimens were quickly frozen in isopentane cooled to -160°C with liquid nitrogen and freeze-dried,fixed in osmium vapour, embedded in Epon, dry-sectioned and dry-mounted according to the procedure described previously, by means of wire loops using Sakura NR-H2 emulsion containing dioctyl sodium sulfosuc- cinate in order to prevent the emulsion films from bursting while they are air dried.

scholarly journals Immunocytochemical localization of renin in the submandibular gland of the mouse.

1978 ◽  
Vol 26 (10) ◽  
pp. 855-861 ◽  
Author(s):  
E Gresik ◽  
A Michelakis ◽  
T Barka ◽  
T Ross
Keyword(s):  
Submandibular Gland ◽  
Adult Mouse ◽  
Secretory Granules ◽  
Microscopic Level ◽  
Electron Microscopic Level ◽  
Light Microscopic Level ◽  
Electron Microscopic ◽  
Granular Convoluted Tubule ◽  
Enzyme Method ◽  
Unlabeled Antibody

Renin was localized in the submandibular gland of the adult mouse at light and electron microscopic levels by the unlabeled antibody enzyme method of Sternberger. At the light microscopic level, renin was confined to the granular convoluted tubule (GCT) segment of the gland with considerable variation among GCT cells in intensity of staining. Some GCT cells failed to stain for renin. The pattern of staining was the same in the gland of male and female mice, but in the glands of females GCT segments were smaller and less numerous. At the electron microscopic level, staining for renin was also confined to the GCT cells, and was localized exclusively to the secretory granules. The intensity of staining of the secretory granules within a given GCT cell varied; some cells contained only minimally reactive or negative secretory granules. All other organelles within the GCT cell, except condensing vacuoles, failed to stain.

scholarly journals Silver amplification of mercury sulfide and selenide: a histochemical method for light and electron microscopic localization of mercury in tissue.

1985 ◽  
Vol 33 (3) ◽  
pp. 219-228 ◽  
Author(s):  
G Danscher ◽  
B Møller-Madsen
Keyword(s):  
Secretory Granules ◽  
Silver Ions ◽  
Ultrastructural Localization ◽  
Photographic Emulsion ◽  
Metallic Silver ◽  
Mercury Chloride ◽  
Electron Microscopic ◽  
Silver Amplification ◽  
Selenium Treatment ◽  
Arch Environ Health

A method for light and electron microscopic demonstration of mercury sulfides and mercury selenides in mammalian tissue is presented. Silver ions adhering to the surface of submicroscopic traces of mercury sulfides or selenides in the tissue are reduced to metallic silver by hydroquinone. Physical development thereupon renders deposits of mercury sulfides or mercury selenide visible as spheres of solid silver. Examples of localization of mercury in the central nervous system and various organs from animals exposed to mercury chloride or methyl mercury chloride with or without additional sodium selenide treatment are presented. Selenium treatment results in a considerable increase in the amount of mercury that can be made visible by silver amplification. After mercury chloride treatment, most of the mercury is localized in lysosomes and is only rarely seen in secretory granules. After simultaneous selenium treatment, mercury is also found in nuclei of proximal tubule cells in the kidney and in macrophages. The "sulfide-osmium" method for ultrastructural localization of mercury suggested by Silberberg, Lawrence, and Leider (Arch Environ Health 19:7, 1969) and the light microscopic method using a photographic emulsion suggested by Umeda, Saito, and Saito (Jpn J Exp Med 39:17, 1969) have been experimentally analyzed and commented on.

scholarly journals Light and electron microscopic localization of ACTH and pro-opiomelanocortin-derived peptides in human developmental and neoplastic cells.

1984 ◽  
Vol 32 (8) ◽  
pp. 885-893 ◽  
Author(s):  
R Y Osamura ◽  
Y Tsutsumi ◽  
K Watanabe
Keyword(s):  
Pituitary Adenomas ◽  
Staining Pattern ◽  
Secretory Granules ◽  
Small Cell ◽  
Electron Microscopic Level ◽  
Positive Staining ◽  
Electron Microscopic ◽  
Ectopic Acth ◽  
Pituitary Glands ◽  
Electron Microscopic Localization

Oncofetal aspects of ACTH and pro-opiomelanocortin (POMC)-derived peptides were studied immunohistochemically at the light and electron microscopic level in human fetal pituitary glands, pituitary adenomas, and small-cell carcinoma of the lung. ACTH, beta-endorphin, and gamma-MSH were localized in the same cells of both fetal and adult pituitary, as well as in the above-mentioned neoplastic tissues. However, alpha-MSH was observed only in the early fetal pituitary, its concentration decreasing with advancing gestational age. The adult pituitary contained only a few alpha-MSH-positive cells. By immunoelectron microscopy, ACTH in the adult pituitary was localized exclusively in the secretory granules. In fetal pituitary at 9 weeks' gestation, ACTH was localized in the perinuclear spaces (PNS), cisternae of rough endoplasmic reticulum (RER), Golgi saccules, and secretory granules. The staining pattern of ACTH in these organelles varied from cell to cell. In fetal pituitaries of greater gestational ages, ACTH was localized in secretory granules. The pituitary adenomas mimicked the staining characteristics of the adult pituitary, i.e., negative or only very occasional alpha-MSH staining and localization of ACTH in the secretory granules. The ectopic ACTH-producing tumors showed a staining pattern similar to that of the early fetal pituitary, i.e., positive staining for alpha-MSH and the presence of ACTH in PNS and cisternae of RER.

scholarly journals Subcellular Localization of the TFF Peptides xP1 and xP4 in the Xenopus laevis Gastric/Esophageal Mucosa: Different Secretion Modes Reflecting Diverse Protective Functions

2020 ◽  
Vol 21 (3) ◽  
pp. 761 ◽  
Author(s):  
Heinz Schwarz ◽  
Werner Hoffmann
Keyword(s):  
Xenopus Laevis ◽  
Secretory Granules ◽  
Lectin Binding ◽  
Goblet Cells ◽  
Electron Microscopic Level ◽  
Esophageal Mucosa ◽  
Mucous Cells ◽  
Electron Microscopic ◽  
Gastric Mucous ◽  
Tff Peptides

The TFF peptides xP1 and xP4 from Xenopus laevis are orthologs of TFF1 and TFF2, respectively. xP1 is secreted as a monomer from gastric surface mucous cells and is generally not associated with mucins, whereas xP4 is a typical secretory peptide from esophageal goblet cells, and gastric mucous neck and antral gland cells tightly associated as a lectin with the ortholog of mucin MUC6. Both TFF peptides have diverse protective functions, xP1 as a scavenger for reactive oxygen species preventing oxidative damage and xP4 as a constituent of the water-insoluble adherent inner mucus barrier. Here, we present localization studies using immunofluorescence and immunoelectron microscopy. xP1 is concentrated in dense cores of secretory granules of surface mucous cells, whereas xP4 mixes with MUC6 in esophageal goblet cells. Of note, we observe two different types of goblet cells, which differ in their xP4 synthesis, and this is even visible morphologically at the electron microscopic level. xP4-negative granules are recognized by their halo, which is probably the result of shrinkage during the processing of samples for electron microscopy. Probably, the tight lectin binding of xP4 and MUC6 creates a crosslinked mucous network forming a stabile granule matrix, which prevents shrinkage.

Sign in / Sign up

Export Citation Format

Share Document