Seasonally dependent formation of protein-storage vacuoles in the inner bark tissues of Salix microstachya

1990 ◽  
Vol 68 (8) ◽  
pp. 1747-1755 ◽  
Author(s):  
John S. Greenwood ◽  
Cobi Demmers ◽  
Suzanne Wetzel

The inner bark tissues of temperate hardwoods often act in the temporary storage of reduced nitrogen as protein during the overwintering period. Electron microscopic studies reported here demonstrate the analogy between the protein-storage vacuoles of the inner bark tissues and protein bodies in seeds. Development of these organelles parallels that of protein body formation seen in many dicotyledonous seeds. Coincident with the synthesis and sequestering of specific proteins, the large central vacuoles of the phloem parenchyma cells are slowly replaced over a 3- to 4-week period with numerous smaller protein-storage vacuoles (protein bodies). These arise via the subdivision of the larger vacuole and subsequent filling of the smaller vacuoles with protein. During this process there is a proliferation of both free ribosomes and rough endoplasmic reticulum in the ground cytoplasm. Stacks of rough endoplasmic reticulum are present in the peripheral cytoplasm and surround the smaller vacuoles as proteinaceous material is deposited. Golgi complexes, although not numerous, are present in the ground cytoplasm during the filling of the protein storage vacuoles. Key words: protein-storage vacuoles, protein body development, Salix microstachya, hardening, nitrogen storage, dormancy onset.

Author(s):  
Ronald Lam ◽  
Mary Ellen McGowan

Although several electron microscopic studies of chordoma have been published, the origin of the chondroitin sulfate rich extracellular matrix is still not clear. Based on the ultrastructural similarities between the extracellular matrix, contents of the rough endoplasmic reticulum and cytoplasmic vacuoles, some authors assume that the two latter structures of chordoma cells contain mucosubstance. The intent of this study is to localize the sulfated glycosaminoglycans intracellularly in a chordoma, which provides cytochemical evidence of the origin of extracellular matrix.A sacrococcygeal chordoma from a 65 year old man was examined by electron microscopy after fixation in 2.5% gluta-raldehyde, 0.2% ruthenium red-glutaraldehyde, and pre-embedment staining with high iron diamine (HID), a method specific for sulfated glycoconjugates. Routine electron microscopic examination revealed stellate nonvacuolated and vacuolated “physaliferous” cells embedded in an abundant extracellular matrix. In general the chordoma cells possessed prominent Golgi complex, rough endoplasmic reticulum, mitochondria, glycogen and intermediate filaments.


1989 ◽  
Vol 67 (10) ◽  
pp. 2850-2856 ◽  
Author(s):  
Hari B. Krishnan ◽  
Jerry A. White ◽  
Steven G. Pueppke

Electrophoretic analysis of sorghum (Sorghum bicolor (L.) Moench) seed prolamines in the presence of sodium dodecyl sulfate reveals major proteins of 27 and 25 kDa and two other proteins of 18 and 12 kDa. Antibodies were raised against this prolamine fraction and used to examine the subcellular distribution of the proteins in developing sorghum seeds. Protein bodies in the starchy endosperm and subaleurone cells usually are round in cross section and contain darkly staining materials arranged in concentric rings. Protein bodies in the first two layers beneath the aleurone layer are irregular in shape and contain discrete pockets of light and dark staining inclusions. Prolamines were detected in both types of protein bodies by immunolabeling. Other oganelles, including Golgi complexes, mitochondria, and amyloplasts, were not labeled. The protein bodies, which have ribosomes attached to their surfaces, are directly connected to the rough endoplasmic reticulum. In some instances, this endoplasmic reticulum was specifically labeled with protein A – gold particles. Based on these observations, we suggest that the rough endoplasmic reticulum serves as the site of both synthesis and accumulation of sorghum prolamines.


Author(s):  
F. G. Zaki

Addition of lithocholic acid (LCA), a naturally occurring bile acid in mammals, to a low protein diet fed to rats induced marked inflammatory reaction in the hepatic cells followed by hydropic degeneration and ductular cell proliferation. These changes were accompanied by dilatation and hyperplasia of the common bile duct and formation of “gallstones”. All these changes were reversible when LCA was withdrawn from the low protein diet except for the hardened gallstones which persisted.Electron microscopic studies revealed marked alterations in the hepatic cells. Early changes included disorganization, fragmentation of the rough endoplasmic reticulum and detachment of its ribosomes. Free ribosomes, either singly or arranged in small clusters were frequently seen in most of the hepatic cells. Vesiculation of the smooth endoplasmic reticulum was often encountered as early as one week after the administration of LCA (Fig. 1).


Author(s):  
Sant S. Sekhon

Although there have been numerous studies concerning the morphogenetic changes accompanying the maturation of insect sperm, only a few deal with the sperm differentiation in the dragonflies. In two recent electron microscopic studies Kessel, has comprehensively treated the erlationship of microtubules to the nucleus and mid-piece structures during spermiogenesis in the dragonfly. The purpose of this study is to follow the sequential nuclear and cytoplasmic changes which accompany the differentiation of spermatogonium into a mature sperm during spermatogenesis in the dragonfly (Aeschna sp.).The dragonfly spermatogonia are characterized by large round nuclei. Loosely organized chromatin is usually unevenly distributed within the spermatogonial nuclei. The scant cytoplasm surrounding the nucleus contains mitochondria, the Golgi apparatus, elements of endoplasmic reticulum and numerous ribosomes (Fig. 1).


1962 ◽  
Vol 13 (1) ◽  
pp. 127-146 ◽  
Author(s):  
G. Adolph Ackerman

Electron microscopic studies of the bursa of Fabricius during the 15th and 16th day of embryonic development in the chick have shown the following findings in the submicroscopic structure of the cellular elements of the lympho-epithelial follicles. In the medulla, basal endodermal epithelial cells undergo mitosis and differentiation into lymphoblasts. During this transformation, there is a reduction in the amount of rough endoplasmic reticulum, an increase in the number or ribosomes, and frequently an enlargement of the Golgi complex. As lymphoblasts differentiate into medium lymphocytes there is a loss of endoplasmic reticulum, a reduction in the number of ribosomes and in the size of the Golgi complex, as well as a decrease in the number and size of mitochondria and in the size of the cell and nucleus. Cytoplasmic processes of reticular-epithelial cells extend between proliferating lymphocytic cells. Desmosomes connect stellate reticular-epithelial and basal epithelial cells but are not present in lymphocytic cells. Nuclear blebbing and vesiculation are frequently observed in the various cell forms of the developing lympho-epithelial nodules. Although lymphocytes and lymphocytopoietic activities in the cortex are sparse during this stage of embryonic development of the bursa, transitional forms between mesenchymal cells and lymphoblasts have been encountered. In addition, lymphoblasts and/or undifferentiated epithelial cells occasionally may pass through the basement membrane from the medulla into the cortical region of the developing nodule. That lymphocytes in the bursa of Fabricius originate from both endodermal and mesodermal derivatives during embryonic development appears to be consistent with both light and electron microscopic observations.


1995 ◽  
Vol 129 (2) ◽  
pp. 459-471 ◽  
Author(s):  
N Benlimame ◽  
D Simard ◽  
I R Nabi

Autocrine motility factor (AMF) is secreted by tumor cells and is capable of stimulating the motility of the secreting cells. In addition to being expressed on the cell surface, its receptor, AMF-R, is found within a Triton X-100 extractable intracellular tubular compartment. AMF-R tubules can be distinguished by double immunofluorescence microscopy from endosomes labeled with the transferrin receptor, lysosomes labeled with LAMP-2, and the Golgi apparatus labeled with beta-COP. AMF-R can also be separated from a LAMP-2 containing lysosomal fraction by differential centrifugation of MDCK cells and is found within a 100,000 g membrane pellet. By electron microscopic immunocytochemistry, AMF-R is localized predominantly to smooth vesicular and tubular membranous organelles as well as to a lesser extent to the plasma membrane and rough endoplasmic reticulum. AMF-R tubules have a variable diameter of 50-250 nm and can acquire an elaborate branched morphology. By immunofluorescence microscopy, AMF-R tubules are clearly distinguished from the calnexin labeled rough endoplasmic reticulum and AMF-R tubule expression is stable to extended cycloheximide treatment. The AMF-R tubule is therefore not a biosynthetic subcompartment of the endoplasmic reticulum. The tubular morphology of the AMF-R tubule is modulated by both the actin and microtubule cytoskeletons. In a similar fashion to that described previously for the tubular lysosome and endoplasmic reticulum, the linear extension and peripheral cellular orientation of the AMF-R tubule are dependent on the integrity of the microtubule cytoskeleton. The AMF-R tubule may thus form part of a family of microtubule-associated tubular organelles.


Author(s):  
Betty G. Uzman ◽  
Marjorie Kasac

Electron microscopic studies of human tumors have been correlated by phase microscopy of ∼1μ sections with conventional histopathology. In tumor nodules from patients with fibrosarcoma (Fig. 1), malignant histiocytosis, and Hodgkin's disease (Figs. 2, 3, 4); in leukemic cells infiltrating spleen and lymph node; and in one parotid secretory cell (case of acute myeloblastic leukemia) alterations of the granular endoplasmic reticulum have been observed. These structures (indicated by arrows) resemble moth-eaten membranous bodies continuous with the encircling (Figs. 1, 2) or contiguous (Figs. 3, 4) cisternal wall. As many as five such alveolate reticular regions have been observed in a single cell.


Author(s):  
Hiroshi Saito ◽  
Goro Asano ◽  
Kaoru Aihara ◽  
Katsunari Fukushi ◽  
Minoru Yoshida ◽  
...  

This short communication is dealt with the ultrastructural changes of the chief cells in insulin stimulus in chronic gastritic condition. The bio gastro-endoscopic biopsy was obtained and pepsin activity of the gastric juice was measured in respective cases. Regular insulin of 0.15U/kg was administrated intra-muscularly and in pre-administration of insulin, 10 minutes, 20 minutes and 30 minutes after administration, biopsied specimens were subjected for electron microscopic studies.In the pre-treated chief cells, extensive development of the cysternal structures of the granular endoplasmic reticulum in basal aspect of the cytoplasm and spherical or oval shaped, light homogeneous zymogen granules in supranuclear region and especially apical aspect of the cytoplasm were featured. Moreover, other type of the chief cells as the one characterized by their fragmented and saccular dilated granular endoplasmic reticulum in basal aspect of the cytoplasm, also exist.


1972 ◽  
Vol 20 (3) ◽  
pp. 220-224 ◽  
Author(s):  
A. HADDAD

Radioactive galactose was injected intravenously into rats and localized in thyroid follicular cells by electron microscopic radioautography at intervals ranging from 2.5 to 30 min after injection. The galactose label was mostly present in the Golgi apparatus at 2.5 min, with some of it in the adjacent rough endoplasmic reticulum. By 30 min, the label was found in apical vesicles and colloid. It was concluded that galactose is added to the carbohydrate side chains of incomplete thyroglobulin molecules during their travel through the cisternae of the endoplasmic reticulum into the Golgi apparatus; the uptake begins as this organelle is approached, but predominates within it. The thyroglobulin molecule which has thus been labeled is transported by the apical vesicles to the colloid.


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