Extracellular matrix and morphogenesis in cnidarians: a tightly knit relationship

2019 ◽  
Vol 63 (3) ◽  
pp. 407-416 ◽  
Author(s):  
Bruno Gideon Bergheim ◽  
Suat Özbek
Keyword(s):  
Extracellular Matrix ◽  
Epithelial Cell ◽  
Basement Membrane ◽  
Genetic Manipulation ◽  
Body Plan ◽  
Body Axis ◽  
Basic Composition ◽  
Cell Layers ◽  
Simple Body ◽  
Matrix Components

Abstract Cnidarians, members of an early-branching metazoan phylum, possess an extracellular matrix (ECM) between their two epithelial cell layers, called the mesoglea. The cnidarian ECM, which is best studied in Hydra, contains matrix components reflective of both interstitial matrix and basement membrane. The identification of core matrisome components in cnidarian genomes has led to the notion that the basic composition of vertebrate ECM is of highly conserved nature and can be traced back to pre-bilaterians. While in vertebrate classes ECM factors have often diverged and acquired specialized functions in the context of organ development, cnidarians with their simple body plan retained direct links between ECM and morphogenesis. Recent advances in genetic manipulation techniques have provided tools for systematically studying cnidarian ECM function in body axis patterning and regeneration.

scholarly journals Expression of extracellular matrix components is regulated by substratum.

1990 ◽  
Vol 110 (4) ◽  
pp. 1405-1415 ◽  
Author(s):  
C H Streuli ◽  
M J Bissell
Keyword(s):  
Extracellular Matrix ◽  
Epithelial Cells ◽  
Basement Membrane ◽  
Type I Collagen ◽  
Basement Membranes ◽  
Type I ◽  
Collagen Gels ◽  
Extracellular Matrix Components ◽  
Matrix Components ◽  
Cells Cultured

Reconstituted basement membranes and extracellular matrices have been demonstrated to affect, positively and dramatically, the production of milk proteins in cultured mammary epithelial cells. Here we show that both the expression and the deposition of extracellular matrix components themselves are regulated by substratum. The steady-state levels of the laminin, type IV collagen, and fibronectin mRNAs in mammary epithelial cells cultured on plastic dishes and on type I collagen gels have been examined, as has the ability of these cells to synthesize, secrete, and deposit laminin and other, extracellular matrix proteins. We demonstrate de novo synthesis of a basement membrane by cells cultured on type I collagen gels which have been floated into the medium. Expression of the mRNA and proteins of basement membranes, however, are quite low in these cultures. In contrast, the levels of laminin, type IV collagen, and fibronectin mRNAs are highest in cells cultured on plastic surfaces, where no basement membrane is deposited. It is suggested that the interaction between epithelial cells and both basement membrane and stromally derived matrices exerts a negative influence on the expression of mRNA for extracellular matrix components. In addition, we show that the capacity for lactational differentiation correlates with conditions that favor the deposition of a continuous basement membrane, and argue that the interaction between specialized epithelial cells and stroma enables them to create their own microenvironment for accurate signal transduction and phenotypic function.

scholarly journals Resolution and limitations of the immunoperoxidase procedure in the localization of extracellular matrix antigens.

1983 ◽  
Vol 31 (7) ◽  
pp. 945-951 ◽  
Author(s):  
P J Courtoy ◽  
D H Picton ◽  
M G Farquhar
Keyword(s):  
Extracellular Matrix ◽  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Cationized Ferritin ◽  
Anionic Sites ◽  
Double Labeling ◽  
Extracellular Matrix Components ◽  
Matrix Components ◽  
Indirect Immunoperoxidase ◽  
Labeling System

A double labeling system was used to test the resolution of the indirect immunoperoxidase procedure in the localization of extracellular matrix components. A recognizable antigen, cationized ferritin, was first implanted at specific anionic sites (approximately 60 nm periodicity) in the lamina rara interna and externa of the glomerular basement membrane (GBM) and subsequently localized by immunoperoxidase. The coincidence between the location of reaction product and the ferritin clusters was assessed. When the amount of immunoadsorbed peroxidase and time of exposure to the 3,3'-diaminobenzidine (DAB)-containing medium were limited, discrete deposits of reaction product were observed around individual ferritin clusters. When immunolabeling was increased, the whole GBM was stained, and DAB staining was also found along the endothelial plasmalemma and the epithelial plasmalemma at the base of the foot processes at some distance (greater than 100 nm) from the ferritin clusters in the laminae rarae. These findings indicate that oxidized DAB reaction product can diffuse over long distances and be reabsorbed onto cell membranes. Even under limited incubation conditions some diffusion of DAB reaction product was encountered. The value and limitations of the DAB-peroxidase procedures are discussed.

scholarly journals Distinctive populations of basement membrane and cell membrane heparan sulfate proteoglycans are produced by cultured cell lines.

1987 ◽  
Vol 105 (1) ◽  
pp. 529-539 ◽  
Author(s):  
J L Stow ◽  
M G Farquhar
Keyword(s):  
Extracellular Matrix ◽  
Cell Membrane ◽  
Basement Membrane ◽  
Heparan Sulfate ◽  
Cultured Cells ◽  
Cell Types ◽  
Heparan Sulfate Proteoglycans ◽  
Cell Layers ◽  
The Media ◽  
Membrane Type

We have investigated the nature and distribution of different populations of heparan sulfate proteoglycans (HSPGs) in several cell lines in culture. Clone 9 hepatocytes and NRK and CHO cells were biosynthetically labeled with 35SO4, and proteoglycans were isolated by DEAE-Sephacel chromatography. Heterogeneous populations of HSPGs and chondroitin/dermatan proteoglycans (CSPGs) were found in the media and cell layer extracts of all cultures. HSPGs were further purified from the media and cell layers and separated from CSPGs by ion exchange chromatography after chondroitinase ABC digestion. In all cell types, HSPGs were found both in the cell layers (20-70% of the total) as well as the medium. When the purified HSPG fractions were further separated by octyl-Sepharose chromatography, very little HSPG in the incubation media bound to the octyl-Sepharose, whereas 40-55% of that in the cell layers bound and could be eluted with 1% Triton X-100. This hydrophobic population most likely consists of membrane-intercalated HSPGs. Basement membrane-type HSPGs were identified by immunoprecipitation as a component (30-80%) of the unbound (nonhydrophobic) HSPG fraction. By immunofluorescence, basement membrane-type HSPGs were distributed in a reticular network in Clone 9 and NRK cell monolayers; by immunoelectron microscopy, these HSPGs were localized to irregular clumps of extracellular matrix located beneath and between cells. The cells did not produce a morphologically recognizable basement membrane layer under these culture conditions. When membrane-associated HSPGs were localized by immunoelectron microscopy, they were found in a continuous layer along the cell membrane of all cell types. The results demonstrate that two antigenically distinct populations of HSPG--an extracellular matrix and a membrane-intercalated population--are found at the surface of several different cultured cells lines; these populations can be distinguished from one another by differences in their distribution in the monolayers by immunocytochemistry and can be separated by hydrophobic chromatography; and basement membrane-type HSPGs are secreted and deposited in the extracellular matrix by cultured cells even though they do not produce a bona fide basement membrane-like layer.

scholarly journals Extracellular Matrix Components Regulate Bone Sialoprotein Expression in MDA-MB-231 Breast Cancer Cells

Cells ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1304
Author(s):  
Florian Keller ◽  
Roman Bruch ◽  
Franziska Clauder ◽  
Mathias Hafner ◽  
Rüdiger Rudolf
Keyword(s):  
Breast Cancer ◽  
Extracellular Matrix ◽  
Basement Membrane ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Bone Sialoprotein ◽  
Extracellular Matrix Components ◽  
Basement Membrane Extract ◽  
Membrane Extract ◽  
Matrix Components

Bone sialoprotein (BSP) has become a target in breast cancer research as it is associated with tumor progression and metastasis. The mechanisms underlying the regulation of BSP expression have been largely elusive. Given that BSP is involved in the homing of cancer cells in bone metastatic niches, we addressed regulatory effects of proteolytic cleavage and extracellular matrix components on BSP expression and distribution in cell culture models. Therefore, MDA-MB-231 human breast cancer cells were kept in 2D and 3D spheroid cultures and exposed to basement membrane extract in the presence or absence of matrix metalloproteinase 9 or the non-polar protease, dispase. Confocal imaging of immunofluorescence samples stained with different antibodies against human BSP demonstrated a strong inducing effect of basement membrane extract on anti-BSP immunofluorescence. Similarly, protease incubation led to acute upregulation of anti-BSP immunofluorescence signals, which was blocked by cycloheximide, suggesting de novo formation of BSP. In summary, our data show that extracellular matrix components play an important function in regulating BSP expression and hint at mechanisms for the formation of bone-associated metastasis in breast cancer that might involve local control of BSP levels by extracellular matrix degradation and release of growth factors.

Epithelial morphogenesis in hydra requires de novo expression of extracellular matrix components and matrix metalloproteinases

Development ◽  
2002 ◽  
Vol 129 (6) ◽  
pp. 1521-1532 ◽  
Author(s):  
Hiroshi Shimizu ◽  
Xiaoming Zhang ◽  
Jinsong Zhang ◽  
Alexey Leontovich ◽  
Kaiyin Fei ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Basement Membrane ◽  
De Novo ◽  
The Body ◽  
Developmental Model ◽  
Epithelial Morphogenesis ◽  
Fibrillar Collagen ◽  
Matrix Components ◽  
Body Column ◽  
Head Regeneration

As a member of the phylum Cnidaria, the body wall of hydra is organized as an epithelium bilayer (ectoderm and endoderm) with an intervening extracellular matrix (ECM). Previous studies have established the general molecular structure of hydra ECM and indicate that it is organized as two subepithelial zones that contain basement membrane components such as laminin and a central fibrous zone that contains interstitial matrix components such as a unique type I fibrillar collagen. Because of its simple structure and high regenerative capacity, hydra has been used as a developmental model to study cell-ECM interaction during epithelial morphogenesis. The current study extends previous studies by focusing on the relationship of ECM biogenesis to epithelial morphogenesis in hydra, as monitored during head regeneration or after simple incision of the epithelium. Histological studies indicated that decapitation or incision of the body column resulted in an immediate retraction of the ECM at the wound site followed by a re-fusion of the bilayer within 1 hour. After changes in the morphology of epithelial cells at the regenerating pole, initiation of de novo biogenesis of an ECM began within hours while full reformation of the mature matrix required approximately 2 days. These processes were monitored using probes to three matrix or matrix-associated components: basement membrane-associated hydra laminin β1 chain (HLM-β1), interstitial matrix-associated hydra fibrillar collagen (Hcol-I) and hydra matrix metalloproteinase (HMMP). While upregulation of mRNA for both HLM-β1 and Hcol-I occurred by 3 hours, expression of the former was restricted to the endoderm and expression of the latter was restricted to the ectoderm. Upregulation of HMMP mRNA was also associated with the endoderm and its expression paralleled that for HLM-β1. As monitored by immunofluorescence, HLM-β1 protein first appeared in each of the two subepithelial zones (basal lamina) at about 7 hours, while Hcol-I protein was first observed in the central fibrous zone (interstitial matrix) between 15 and 24 hours. The same temporal and spatial expression pattern for these matrix and matrix-associated components was observed during incision of the body column, thus indicating that these processes are a common feature of the epithelium in hydra. The correlation of loss of the ECM, cell shape changes and subsequent de novo biogenesis of matrix and matrix-associated components were all functionally coupled by antisense experiments in which translation of HLM-β1 and HMMP was blocked and head regeneration was reversibly inhibited. In addition, inhibition of translation of HLM-β1 caused an inhibition in the appearance of Hcol-I into the ECM, thus suggesting that binding of HLM-β1 to the basal plasma membrane of ectodermal cells signaled the subsequent discharge of Hcol-I from this cell layer into the newly forming matrix. Given the early divergence of hydra, these studies point to the fundamental importance of cell-ECM interactions during epithelial morphogenesis.

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