scholarly journals Hexabrachion proteins in embryonic chicken tissues and human tumors.

1987 ◽  
Vol 105 (3) ◽  
pp. 1387-1394 ◽  
Author(s):  
H P Erickson ◽  
H C Taylor
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Cell Attachment ◽  
Human Fibroblasts ◽  
Human Tumors ◽  
Extracellular Matrix Protein ◽  
Functional Roles ◽  
Chicken Tissues ◽  
Extracellular Matrix Molecule ◽  
Separate Factor

Cell cultures of chicken embryo and human fibroblasts produce a large extracellular matrix molecule with a six-armed structure that we called a hexabrachion (Erickson, H. P., and J. L. Iglesias, 1984, Nature (Lond.), 311:267-269. In the present work we have determined that the myotendinous (M1) antigen described by M. Chiquet and D. M. Fambrough in chicken tissues (1984, J. Cell Biol., 98:1926-1936), and the glioma mesenchymal extracellular matrix protein described by Bourdon et al. in human tumors (Bourdon, M. A., C. J. Wikstrand, H. Furthmayr, T. J. Matthews, and D. D. Bigner, 1983, Cancer Res. 43:2796-2805) have the structure of hexabrachions. We also demonstrate that the M1 antigen is present in embryonic brain, where it was previously reported absent, and have purified hexabrachions from brain homogenates. The recently described cytotactin (Grumet, M., S. Hoffman, K. L. Crossin, and G. M. Edelman, 1985, Proc. Natl. Acad. Sci. USA, 82:8075-8079) now appears to be identical to the chicken hexabrachion protein. In a search for functional roles, we looked for a possible cell attachment activity. A strong, fibronectin-like attachment activity was present in (NH4)2SO4 precipitates of cell supernatant and sedimented with hexabrachions in glycerol gradients. Hexabrachions purified by antibody adsorption, however, had lost this activity, suggesting that it was due to a separate factor associated with hexabrachions in the gradient fractions. The combined information in the several, previously unrelated studies suggests that hexabrachions may play a role in organizing localized regions of extracellular matrix. The protein is prominently expressed at specific times and locations during embryonic development, is retained in certain adult tissues, and is reexpressed in a variety of tumors.

Restrictin: a chick neural extracellular matrix protein involved in cell attachment co-purifies with the cell recognition molecule F11

Development ◽  
1991 ◽  
Vol 113 (1) ◽  
pp. 151-164 ◽  
Author(s):  
F.G. Rathjen ◽  
J.M. Wolff ◽  
R. Chiquet-Ehrismann
Keyword(s):  
Extracellular Matrix ◽  
Nervous System ◽  
Matrix Protein ◽  
Cell Attachment ◽  
Extracellular Matrix Protein ◽  
Relative Molecular Mass ◽  
Adhesion Assay ◽  
Cell Recognition ◽  
Neural Extracellular Matrix ◽  
Recognition Molecule

We report here the characterization of restrictin, a novel chick neural extracellular matrix glycoprotein associated with the cell recognition molecule F11. Immunoaffinity chromatography using monoclonal antibody 23–13 directed to restrictin yield a major relative molecular mass band at 170 × 10(3) and minor bands at 160, 180, 250 and 320 × 10(3) which are immunologically related to each other. Neural cells attach on immobilized restrictin in a short-term adhesion assay. This adhesion can be blocked specifically by monoclonal or polyclonal antibodies to restrictin but not by antibodies to F11 or by the peptide GRGDSP. Antibodies to restrictin do not interfere with the fasciculation of retinal axons and the isolated restrictin does not stimulate the outgrowth of axons. In the developing nervous system, restrictin is localized in very restricted regions and is found within areas of F11 expression. The timing and pattern of expression of restrictin and its cell attachment activity suggest that it participates in developmental events of the nervous system.

scholarly journals The c-Jun-induced transformation process involves complex regulation of tenascin-C expression.

1997 ◽  
Vol 17 (6) ◽  
pp. 3202-3209 ◽  
Author(s):  
A Mettouchi ◽  
F Cabon ◽  
N Montreau ◽  
V Dejong ◽  
P Vernier ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Cell Attachment ◽  
Matrix Composition ◽  
Expression Vectors ◽  
Extracellular Matrix Protein ◽  
Cdna Clones ◽  
Tenascin C ◽  
Nf Kappab ◽  
Factor C

In cooperation with an activated ras oncogene, the site-dependent AP-1 transcription factor c-Jun transforms primary rat embryo fibroblasts (REF). Although signal transduction pathways leading to activation of c-Jun proteins have been extensively studied, little is known about c-Jun cellular targets. We identified c-Jun-upregulated cDNA clones homologous to the tenascin-C gene by differential screening of a cDNA library from REF. This tightly regulated gene encodes a rare extracellular matrix protein involved in cell attachment and migration and in the control of cell growth. Transient overexpression of c-Jun induced tenascin-C expression in primary REF and in FR3T3, an established fibroblast cell line. Surprisingly, tenascin-C synthesis was repressed after stable transformation by c-Jun compared to that in the nontransformed parental cells. As assessed by using the tenascin-C (-220 to +79) promoter fragment cloned in a reporter construct, the c-Jun-induced transient activation is mediated by two binding sites: one GCN4/AP-1-like site, at position -146, and one NF-kappaB site, at position -210. Furthermore, as demonstrated by gel shift experiments and cotransfections of the reporter plasmid and expression vectors encoding the p65 subunit of NF-kappaB and c-Jun, the two transcription factors bind and synergistically transactivate the tenascin-C promoter. We previously described two other extracellular matrix proteins, SPARC and thrombospondin-1, as c-Jun targets. Thus, our results strongly suggest that the regulation of the extracellular matrix composition plays a central role in c-Jun-induced transformation.

scholarly journals Fibrilar Polymorphism of the Bacterial Extracellular Matrix Protein TasA

2021 ◽  
Vol 9 (3) ◽  
pp. 529
Author(s):  
Mnar Ghrayeb ◽  
Shahar Hayet ◽  
Neta Lester-Zer ◽  
Yael Levi-Kalisman ◽  
Liraz Chai
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Mechanical Stability ◽  
Extracellular Matrix Protein ◽  
Fiber Axis ◽  
Amyloid Proteins ◽  
Functional Amyloid ◽  
Amyloid Fibers ◽  
Functional Roles ◽  
Biofilm Development

Functional amyloid proteins often appear as fibers in extracellular matrices of microbial soft colonies. In contrast to disease-related amyloid structures, they serve a functional goal that benefits the organism that secretes them, which is the reason for the title “functional”. Biofilms are a specific example of a microbial community in which functional amyloid fibers play a role. Functional amyloid proteins contribute to the mechanical stability of biofilms and mediate the adhesion of the cells to themselves as well as to surfaces. Recently, it has been shown that functional amyloid proteins also play a regulatory role in biofilm development. TasA is the major proteinaceous fibrilar component of the extracellular matrix of biofilms made of the soil bacterium and Gram-positive Bacillus subtilis. We have previously shown, as later corroborated by others, that in acidic solutions, TasA forms compact aggregates that are composed of tangled fibers. Here, we show that in a neutral pH and above a certain TasA concentration, the fibers of TasA are elongated and straight and that they bundle up in highly concentrated salt solutions. TasA fibers resemble the canonic amyloid morphology; however, these fibers also bear an interesting nm-scale periodicity along the fiber axis. At the molecular level, TasA fibers contain a twisted β-sheet structure, as indicated by circular dichroism measurements. Our study shows that the morphology of TasA fibers depends on the environmental conditions. Different fibrilar morphologies may be related with different functional roles in biofilms, ranging from granting biofilms with a mechanical support to acting as antibiotic agents.

scholarly journals A nerve terminal anchorage protein from electric organ.

1986 ◽  
Vol 103 (2) ◽  
pp. 509-520 ◽  
Author(s):  
S S Carlson ◽  
P Caroni ◽  
R B Kelly
Keyword(s):  
Extracellular Matrix ◽  
Basal Lamina ◽  
Nerve Terminal ◽  
Synaptic Vesicles ◽  
Matrix Protein ◽  
Electric Organ ◽  
Extracellular Matrix Protein ◽  
Affinity Column ◽  
Extracellular Matrix Molecule ◽  
Hydrophobic Tail

The nerve terminal and the postsynaptic receptor-containing membranes of the electric organ are both linked to the basal lamina that runs between them. We have identified an extracellular matrix protein whose physical properties suggest it anchors the nerve terminal to the basal lamina. The protein was identified because it shares an epitope with a proteoglycan component of electric organ synaptic vesicles. It too behaves like a proteoglycan. It is solubilized with difficulty from extracellular matrix fractions, elutes from DEAE Sephacel at pH 4.9 only at high ionic strength, and binds to a laminin affinity column from which it can be eluted with heparin. Under denaturing conditions it sediments rapidly and has a large excluded volume although it can be included in Sephacryl S-1000 columns. This large, highly charged extracellular matrix molecule can be readily reconstituted into liposomes consistent with the presence of a hydrophobic tail. By immunoelectron microscopy the antigen is found both in synaptic vesicles and on the plasma membrane of the nerve terminal. Since this is the first protein described that links the nerve terminal membrane to the extracellular matrix, we propose calling it terminal anchorage protein one (TAP-1).

Cell attachment effects of collagen nanoparticles on crosslinked electrospun nanofibers

2020 ◽  
pp. 039139882094773
Author(s):  
Fereshteh Ziaei Amiri ◽  
Zaiddodine Pashandi ◽  
Nasrin Lotfibakhshaiesh ◽  
Mohammad Javad Mirzaie Parsa ◽  
Hossein Ghanbari ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Extracellular Matrix ◽  
Cell Viability ◽  
Matrix Protein ◽  
Cellular Proliferation ◽  
Cell Attachment ◽  
Extracellular Matrix Protein ◽  
Cross Linking ◽  
Scanning Electron

Since collagen is naturally a main extracellular matrix protein, it has been applied widely in skin’s tissue engineering scaffolds to mimics the characteristics of extracellular matrix for proper transplantation of living cells. However, there are challenges that come with application of this natural polymer such as high solubility in aqueous environments which requires further consideration such as chemically cross-linking in order to stabilization. But these treatments also affect its functionality and finally cellular behaviors on scaffold. In this research we evaluated the suitability of collagen nanofibers versus collagen nanoparticles for cell adhesion and viability on glutaraldehyde cross-linked scaffolds. Appling a dual-pump electrospining machine a blend PCL-Gelatin from one side and collagen nanofibers or collagen nanoparticles from the other side were collected on the collector. The fabricated scaffolds were characterized by scanning electron microscopy, contact angle, and mechanical analysis. The cell viability, adhesion and morphology were studied respectively using MTT assay, hoechst staining and scanning electron microscopy. The results indicated significantly improvement of cell viability, adhesion and better spreading on scaffolds with collagen nanoparticles than collagen nanofibers. It seems changes in surface morphology, viscoelastic moduli and swelling ability following cross-linking with glutaraldehyde in scaffold with collagen nanoparticles are still favorable for cellular proliferation. Based on these results, in the case of glutaraldehyde cross-linking, application of collagen nanoparticles rather than collagen nanofibers in tissue regeneration scaffolds will better mimic the extracellular matrix characteristics; and preserve the viability and adhesion of seeded cells.

The extracellular matrix protein TasA is a developmental cue that maintains a motile subpopulation within Bacillus subtilis biofilms

2020 ◽  
Vol 13 (632) ◽  
pp. eaaw8905 ◽  
Author(s):  
Nitai Steinberg ◽  
Alona Keren-Paz ◽  
Qihui Hou ◽  
Shany Doron ◽  
Keren Yanuka-Golub ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Bacillus Subtilis ◽  
Matrix Protein ◽  
Cell Attachment ◽  
Extracellular Matrix Protein ◽  
Two Component System ◽  
Suppressor Mutations ◽  
Specific Subset ◽  
Two Component ◽  
Friction Surfaces

In nature, bacteria form biofilms—differentiated multicellular communities attached to surfaces. Within these generally sessile biofilms, a subset of cells continues to express motility genes. We found that this subpopulation enabled Bacillus subtilis biofilms to expand on high-friction surfaces. The extracellular matrix (ECM) protein TasA was required for the expression of flagellar genes. In addition to its structural role as an adhesive fiber for cell attachment, TasA acted as a developmental signal stimulating a subset of biofilm cells to revert to a motile phenotype. Transcriptomic analysis revealed that TasA stimulated the expression of a specific subset of genes whose products promote motility and repress ECM production. Spontaneous suppressor mutations that restored motility in the absence of TasA revealed that activation of the biofilm-motility switch by the two-component system CssR/CssS antagonized the TasA-mediated reversion to motility in biofilm cells. Our results suggest that although mostly sessile, biofilms retain a degree of motility by actively maintaining a motile subpopulation.

1280: Increased Susceptibility to Genitovaginal Prolapse Associated with a Polymorphism in the Promoter of the Extracellular Matrix Protein LAMC1

2007 ◽  
Vol 177 (4S) ◽  
pp. 421-422
Author(s):  
Ganka Nikolova ◽  
Christian O. Twiss ◽  
Hane Lee ◽  
Nelson Stanley ◽  
Janet Sinsheimer ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Extracellular Matrix Protein ◽  
Increased Susceptibility

scholarly journals Homogenous overexpression of the extracellular matrix protein Netrin-1 in a hollow fiber bioreactor

2021 ◽  
Author(s):  
Aniel Moya-Torres ◽  
Monika Gupta ◽  
Fabian Heide ◽  
Natalie Krahn ◽  
Scott Legare ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Hollow Fiber ◽  
Mammalian Cells ◽  
Matrix Protein ◽  
Continuous Production ◽  
Extracellular Matrix Protein ◽  
Close Monitoring ◽  
High Quality ◽  
Biolayer Interferometry ◽  
Hollow Fiber Bioreactor

Abstract The production of recombinant proteins for functional and biophysical studies, especially in the field of structural determination, still represents a challenge as high quality and quantities are needed to adequately perform experiments. This is in part solved by optimizing protein constructs and expression conditions to maximize the yields in regular flask expression systems. Still, work flow and effort can be substantial with no guarantee to obtain improvements. This study presents a combination of workflows that can be used to dramatically increase protein production and improve processing results, specifically for the extracellular matrix protein Netrin-1. This proteoglycan is an axon guidance cue which interacts with various receptors to initiate downstream signaling cascades affecting cell differentiation, proliferation, metabolism, and survival. We were able to produce large glycoprotein quantities in mammalian cells, which were engineered for protein overexpression and secretion into the media using the controlled environment provided by a hollow fiber bioreactor. Close monitoring of the internal bioreactor conditions allowed for stable production over an extended period of time. In addition to this, Netrin-1 concentrations were monitored in expression media through biolayer interferometry which allowed us to increase Netrin-1 media concentrations tenfold over our current flask systems while preserving excellent protein quality and in solution behavior. Our particular combination of genetic engineering, cell culture system, protein purification, and biophysical characterization permitted us to establish an efficient and continuous production of high-quality protein suitable for structural biology studies that can be translated to various biological systems. Key points • Hollow fiber bioreactor produces substantial yields of homogenous Netrin-1 • Biolayer interferometry allows target protein quantitation in expression media • High production yields in the bioreactor do not impair Netrin-1 proteoglycan quality Graphical abstract

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