scholarly journals Biophysical Properties of the Basal Lamina: A Highly Selective Extracellular Matrix

Author(s):  
Fabienna Arends ◽  
Oliver Lieleg
Development ◽  
1983 ◽  
Vol 78 (1) ◽  
pp. 195-209
Author(s):  
J. M. Hurle ◽  
M. A. Fernandez-Teran

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.


2019 ◽  
Vol 30 (7) ◽  
pp. 838-850 ◽  
Author(s):  
Mengdie Wang ◽  
James P. Hinton ◽  
Jaime M. C. Gard ◽  
Joe G. N. Garcia ◽  
Beatrice S. Knudsen ◽  
...  

Integrin α6β4 is an essential, dynamic adhesion receptor for laminin 332 found on epithelial cells, required for formation of strong cell–extracellular matrix (ECM) adhesion and induced migration, and coordinated by regions of the β4C cytoplasmic domain. β4E, a unique splice variant of β4 expressed in normal tissue, contains a cytoplasmic domain of 231 amino acids with a unique sequence of 114 amino acids instead of β4C’s canonical 1089 amino acids. We determined the distribution of α6β4E within normal human glandular epithelium and its regulation and effect on cellular biophysical properties. Canonical α6β4C expressed in all basal cells, as expected, while α6β4E expressed within a subset of luminal cells. α6β4E expression was induced by three-dimensional culture conditions, activated Src, was reversible, and was stabilized by bortezomib, a proteasome inhibitor. α6β4C expressed in all cells during induced migration, whereas α6β4E was restricted to a subset of cells with increased kinetics of cell–cell and cell–ECM resistance properties. Interestingly, α6β4E presented in “ringlike” patterns measuring ∼1.75 × 0.72 microns and containing actin and CD9 at cell–ECM locations. In contrast, α6β4C expressed only within hemidesmosome-like structures containing BP180. Integrin α6β4E is an inducible adhesion isoform in normal epithelial cells that can alter biophysical properties of cell–cell and cell–ECM interactions.


1993 ◽  
Vol 41 (4) ◽  
pp. 415 ◽  
Author(s):  
K Rohde ◽  
NA Watson ◽  
A Faubel

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.


2020 ◽  
Vol 7 (4) ◽  
pp. 124 ◽  
Author(s):  
Jun Yang ◽  
Gokhan Bahcecioglu ◽  
Pinar Zorlutuna

Emerging evidence has shown multiple roles of the tumor microenvironment (TME) components, specifically the extracellular matrix (ECM), in breast cancer development, progression, and metastasis. Aside from the biophysical properties and biochemical composition of the breast ECM, the signaling molecules are extremely important in maintaining homeostasis, and in the breast TME, they serve as the key components that facilitate tumor progression and immune evasion. Extracellular vesicles (EVs), the mediators that convey messages between the cells and their microenvironment through signaling molecules, have just started to capture attention in breast cancer research. In this comprehensive review, we first provide an overview of the impact of ECM in breast cancer progression as well as the alterations occurring in the TME during this process. The critical importance of EVs and their biomolecular contents in breast cancer progression and metastasis are also discussed. Finally, we discuss the potential biomedical or clinical applications of these extracellular components, as well as how they impact treatment outcomes.


2012 ◽  
Vol 2012 ◽  
pp. 1-7 ◽  
Author(s):  
B. Fuentes ◽  
J. Duaso ◽  
D. Droguett ◽  
C. Castillo ◽  
W. Donoso ◽  
...  

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.


Teratology ◽  
1987 ◽  
Vol 35 (3) ◽  
pp. 335-344 ◽  
Author(s):  
B. D. Abbott ◽  
K. S. Morgan ◽  
L. S. Birnbaum ◽  
R. M. Pratt

Development ◽  
1975 ◽  
Vol 34 (1) ◽  
pp. 1-18
Author(s):  
Robert O. Kelley

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.


Development ◽  
1990 ◽  
Vol 109 (2) ◽  
pp. 313-321 ◽  
Author(s):  
R. Probstmeier ◽  
R. Martini ◽  
M. Schachner

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.


1984 ◽  
Vol 99 (2) ◽  
pp. 615-627 ◽  
Author(s):  
E W Godfrey ◽  
R M Nitkin ◽  
B G Wallace ◽  
L L Rubin ◽  
U J McMahan

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.


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