TCDD alters the extracellular matrix and basal lamina of the fetal mouse kidney

Teratology ◽  
1987 ◽  
Vol 35 (3) ◽  
pp. 335-344 ◽  
Author(s):  
B. D. Abbott ◽  
K. S. Morgan ◽  
L. S. Birnbaum ◽  
R. M. Pratt
Keyword(s):  
Extracellular Matrix ◽  
Basal Lamina ◽  
Mouse Kidney ◽  
Fetal Mouse

Fine structure of the regressing interdigital membranes during the formation of the digits of the chick embryo leg bud

Development ◽  
1983 ◽  
Vol 78 (1) ◽  
pp. 195-209
Author(s):  
J. M. Hurle ◽  
M. A. Fernandez-Teran
Keyword(s):  
Extracellular Matrix ◽  
Fine Structure ◽  
Chick Embryo ◽  
Basal Lamina ◽  
Ultrastructural Study ◽  
Active Role ◽  
Epithelial Tissue ◽  
Complex Process ◽  
Cell Processes ◽  
Collagenous Material

There is recent evidence showing that in addition to the well-known mesenchymal necrotic mechanism involved in the disappearance of the interdigital membranes, the ectodermal tissue may also play an active role in the formation of the free digits of most vertebrates. Ultrastructural study of the regressing interdigital membrane of the chick leg revealed significant changes at the epitheliomesenchymal interface. Disruptions of the ectodermal basal lamina and an intense deposition of collagenous material were the most conspicuous changes observed in the extracellular matrix. In addition the basal ectodermal cells showed prominent cell processes projected into the mesenchymal core of the membrane, and mesenchymal macrophages appeared to migrate through the epithelial tissue to be detached into the amniotic sac. It is concluded from our results that the elimination of the interdigital membranes is a complex process requiring the interaction of all the tissue components of the membrane.

Effect of tunicamycin on maturation of fetal mouse lung

1993 ◽  
Vol 265 (3) ◽  
pp. L250-L259
Author(s):  
E. H. Webster ◽  
S. R. Hilfer ◽  
R. L. Searls ◽  
J. Kornilow
Keyword(s):  
Extracellular Matrix ◽  
Fetal Lung ◽  
Mouse Lung ◽  
Type I ◽  
Type Ii ◽  
Fetal Mouse ◽  
Type Ii Pneumocytes ◽  
Separate Control ◽  
Normal Controls

The mesodermal capsule of the fetal lung plays a role in differentiation of the respiratory region. It has been proposed for other epithelial organs that the mesodermal capsule influences development by modifying the basal lamina or the extended extracellular matrix. The effect could be on deposition or turnover of collagens, proteoglycans, and/or glycoproteins. This study tests the role of glycoproteins in differentiation of respiratory endings by inhibiting their synthesis with the antibiotic tunicamycin (TM). Lungs at 16 and 18 days gestation and 3 days after birth were cultured with TM and examined for morphological and biochemical differences from normal controls. With TM, alveolar regions did not expand properly and formed fewer type I pneumocytes, although type II pneumocytes were unaffected. The epithelium of untreated respiratory regions showed greater incorporation of radioactive mannose than the airways region or mesenchyme. This incorporation was diminished in TM, but the pattern persisted. Comparison with the results obtained with beta-xyloside suggested that differentiation of type I and type II pneumocytes is under separate control.

Ultrastructure of the Epidermis and Protonephridium of an Undescribed Species of Luridae (Platyhelminthes, Rhabdocoela)

1993 ◽  
Vol 41 (4) ◽  
pp. 415 ◽  
Author(s):  
K Rohde ◽  
NA Watson ◽  
A Faubel
Keyword(s):  
Extracellular Matrix ◽  
Single Cell ◽  
Basal Lamina ◽  
Dense Material ◽  
Undescribed Species ◽  
Single Row ◽  
Longitudinal Ribs ◽  
Capillary Walls

The epidermis of an undescribed species of Luridae possesses many large cavities filled with a medium-dense material, intraepidermal nuclei, glandular ducts, cilia with vertical and horizontal rootlets, surface microvilli, and a thick basal lamina. Cilia have narrow tips, the peripheral axonemal doublets lose one of the microtubules and, finally, whole doublets are lost near the tip. Flame bulbs have a single row of longitudinal ribs containing microtubules and connected by a 'membrane' apparently of extracellular matrix; cilia of flame bulbs possess cross-striated rootlets, and capillary walls are smooth. The nucleus of the protonephridium was observed near the tip of the flame bulb, along the capillary. It is not clear whether one perikaryon forms more than one flame bulb. The structure of the epidermal ciliary rootlets, the presence of intraepidermal nuclei, and flame bulbs composed of a single row of longitudinal ribs containing microtubules formed by a single cell are typical rhabdocoel characteristics.

scholarly journals Progressive Extracellular Matrix Disorganization in Chemically Induced Murine Oral Squamous Cell Carcinoma

2012 ◽  
Vol 2012 ◽  
pp. 1-7 ◽  
Author(s):  
B. Fuentes ◽  
J. Duaso ◽  
D. Droguett ◽  
C. Castillo ◽  
W. Donoso ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Squamous Cell Carcinoma ◽  
Oral Squamous Cell Carcinoma ◽  
Connective Tissue ◽  
Cell Carcinoma ◽  
Basal Lamina ◽  
Squamous Cell ◽  
Collagen I ◽  
Severe Dysplasia ◽  
Tumor Pathogenesis

Introduction. Oral squamous cell carcinoma (OSCC) is one of the ten most common cancers affecting the human population. Tumor pathogenesis implies a multistep process in which cells acquire features that enable them to become tumorigenic and ultimately malignant. The process of OSCC carcinogenesis can be reproduced in animal models, the OSCC induction with 4-nitroquinoline-1-oxide (4NQO) in mice is a widely used tool for studying tumor pathogenesis. Objective. The aim of the present study was to determine the progressive changes in basal lamina and connective tissue remodeling during 4NQO-induced OSCC carcinogenesis. Material and Methods. Samples were classified according to “International Histological Classification of tumors” in mild, moderate, and severe dysplasia and invasive carcinoma. Five samples of each pathologic entity and control healthy tongues were used. Immunohistochemical analysis of collagen IV as well as histochemical analysis of glycosylated molecules (PAS) and collagen I (Picro Sirius red) were performed. Results. During experimental-induced carcinogenesis by 4NQO a progressive basal lamina destruction and collagen I disorganization in adjacent connective tissue can be observed. Conclusion. Our results confirm previous studies that show alterations in extracellular matrix (ECM) in malignant lesions, validating the experimental carcinogenesis induced by 4NQO.

Ultrastructural identification of extracellular matrix and cell surface components during limb morphogenesis in man

Development ◽  
1975 ◽  
Vol 34 (1) ◽  
pp. 1-18
Author(s):  
Robert O. Kelley
Keyword(s):  
Extracellular Matrix ◽  
Cell Surface ◽  
Basal Lamina ◽  
Mesenchymal Cell ◽  
Ruthenium Red ◽  
Human Hand ◽  
Binding Characteristics ◽  
Limb Morphogenesis ◽  
Testicular Hyaluronidase

Development of the human hand plate (stages 16–17) has been analyzed with emphasis on differentiation of elements within the extracellular matrix and the composition of the mesenchymal cell surface. The epithelial—mesenchymal interface contains a basal lamina and a sublaminar matrix exhibiting: (a) collagen fibrils with characteristic 63–64 nm banding; (b) non-banded filaments, 10–15 nm in diameter; (c) ruthenium red-positive particles, 12–15 nm in diameter; and (d) attenuated threads, 3·5–5·0 nm in diameter which interconnect particles, fibrils, filaments and the basal lamina. Processes of mesenchymal cells penetrate this matrix network. In addition to staining with ruthenium red, components of basal laminae bind to ferritin-conjugated Concanavalin A, greatest binding being localized on the mesenchymal surface of the lamina. Asymmetry of binding is removed by incubation of exposed laminae with trypsin (5 µg/ml). Regional differences in these staining and binding characteristics within the subepithelial matrix have not been observed in the hand plate. However, precartilaginous extracellular zones deep within the plate are notably unstructured in comparison to the sublaminar region. Ruthenium red-positive materials at mesenchymal cell surfaces display sensitivity to testicular hyaluronidase, Pronase and trypsin but resist removal with neuraminidase and EDTA. These features of the substrate in situ may be important in the regulation of mesenchymal cell behavior during limb morphogenesis in man.

Expression of J1/tenascin in the crypt-villus unit of adult mouse small intestine: implications for its role in epithelial cell shedding

Development ◽  
1990 ◽  
Vol 109 (2) ◽  
pp. 313-321 ◽  
Author(s):  
R. Probstmeier ◽  
R. Martini ◽  
M. Schachner
Keyword(s):  
Extracellular Matrix ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Basal Lamina ◽  
Adult Mouse ◽  
Epithelial Cell Line ◽  
Intestinal Epithelial ◽  
Collagen Types ◽  
Numerous Microvillus ◽  
Cell Shedding

The localization of the extracellular matrix recognition molecule J1/tenascin was investigated in the crypt-villus unit of the adult mouse ileum by immunoelectron microscopic techniques. In the villus region, J1/tenascin was detected strongly in the extracellular matrix (ECM) between fibroblasts of the lamina propria. It was generally absent in the ECM at the interface between subepithelial fibroblasts and intestinal epithelium, except for some restricted areas along the epithelial basal lamina of villi, but not of crypts. These restricted areas corresponded approximately to the basal part of one epithelial cell. In J1/tenascin-positive areas, epithelial cells contacted the basal lamina with numerous microvillus-like processes, whereas in J1/tenascin-negative areas the basal surface membranes of epithelial cells contacted their basal lamina in a smooth and continuous apposition. In order to characterize the functional role of J1/tenascin in the interaction between epithelial cells and ECM, the intestinal epithelial cell line HT-29 was tested for its ability to adhere to different ECM components. Cells adhered to substratum-immobilized fibronectin, laminin and collagen types I to IV, but not to J1/tenascin. When laminin or collagen types I to IV were mixed with J1/tenascin, cell adhesion was as effective as without J1/tenascin. However, adhesion was completely abolished when cells were offered a mixture of fibronectin and J1/tenascin as substratum. The ability of J1/tenascin to reduce the adhesion of intestinal epithelial cells to their fibronectin-containing basal lamina suggests that J1/tenascin may be involved in the process of physiological cell shedding from the villus.

scholarly journals Components of Torpedo electric organ and muscle that cause aggregation of acetylcholine receptors on cultured muscle cells.

1984 ◽  
Vol 99 (2) ◽  
pp. 615-627 ◽  
Author(s):  
E W Godfrey ◽  
R M Nitkin ◽  
B G Wallace ◽  
L L Rubin ◽  
U J McMahan
Keyword(s):  
Extracellular Matrix ◽  
Basal Lamina ◽  
Acetylcholine Receptors ◽  
Active Component ◽  
Electric Organ ◽  
Muscle Cells ◽  
Insoluble Fraction ◽  
Lateral Migration ◽  
Cultured Myotubes ◽  
Torpedo Electric Organ

The synaptic portion of a muscle fiber's basal lamina sheath has molecules tightly bound to it that cause aggregation of acetylcholine receptors (AChRs) on regenerating myofibers. Since basal lamina and other extracellular matrix constituents are insoluble in isotonic saline and detergent solutions, insoluble detergent-extracted fractions of tissues receiving cholinergic input may provide an enriched source of the AChR-aggregating molecules for detailed characterization. Here we demonstrate that such an insoluble fraction from Torpedo electric organ, a tissue with a high concentration of cholinergic synapses, causes AChRs on cultured chick muscle cells to aggregate. We have partially characterized the insoluble fraction, examined the response of muscle cells to it, and devised ways of extracting the active components with a view toward purifying them and learning whether they are similar to those in the basal lamina at the neuromuscular junction. The insoluble fraction from the electric organ was rich in extracellular matrix constituents; it contained structures resembling basal lamina sheaths and had a high density of collagen fibrils. It caused a 3- to 20-fold increase in the number of AChR clusters on cultured myotubes without significantly affecting the number or size of the myotubes. The increase was first seen 2-4 h after the fraction was added to cultures and it was maximal by 24 h. The AChR-aggregating effect was dose dependent and was due, at least in part, to lateral migration of AChRs present in the muscle cell plasma membrane at the time the fraction was applied. Activity was destroyed by heat and by trypsin. The active component(s) was extracted from the insoluble fraction with high ionic strength or pH 5.5 buffers. The extracts increased the number of AChR clusters on cultured myotubes without affecting the number or degradation rate of surface AChRs. Antiserum against the solubilized material blocked its effect on AChR distribution and bound to the active component. Insoluble fractions of Torpedo muscle and liver did not cause AChR aggregation on cultured myotubes. However a low level of activity was detected in pH 5.5 extracts from the muscle fraction. The active component(s) in the muscle extract was immunoprecipitated by the antiserum against the material extracted from the electric organ insoluble fraction. This antiserum also bound to extracellular matrix in frog muscles, including the myofiber basal lamina sheath. Thus the insoluble fraction of Torpedo electric organ is rich in AChR-aggregating molecules that are also found in muscle and has components antigenically similar to those in myofiber basal lamina.

Immunoelectron microscopic localization of fibronectin in the smooth muscle layer of mouse small intestine.

1987 ◽  
Vol 35 (4) ◽  
pp. 411-417 ◽  
Author(s):  
K Kurisu ◽  
Y Ohsaki ◽  
K Nagata ◽  
T Kukita ◽  
H Yoshikawa ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Smooth Muscle ◽  
Small Intestine ◽  
Smooth Muscle Cells ◽  
Basal Lamina ◽  
Muscle Cells ◽  
Muscle Layer ◽  
Secretory Vesicle ◽  
Smooth Muscle Layer ◽  
Mouse Small Intestine

We studied the ultrastructural distribution of fibronectin in the smooth muscle layer of mouse small intestine with affinity-purified antibodies using the immunogold technique. Fibronectin was present over the pericellular area extending from the cell membrane to the extracellular matrix beyond the basal lamina. Distribution of the glycoprotein over the pericellular area was heterogeneous, i.e., it was localized more abundantly in the narrow space between smooth muscle cells, the gaps having a width of 60-80 nm where the two dense bands in adjacent cells matched each other. Such localization suggests that fibronectin contributes to cell adhesion. Within the basement membrane, gold label was localized both in lamina lucida and lamina densa, more densely in the latter than in the former. Fibronectin was also co-distributed with collagen fibers in the extracellular matrix. Within smooth muscle cells, gold particles were observed on rough endoplasmic reticulum and secretory vesicle-like structures. These results suggest that smooth muscle cells synthesize fibronectin and secrete it as a component of the basal lamina and extracellular matrix.

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