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.

Initial characterization of anosmin-1, a putative extracellular matrix protein synthesized by definite neuronal cell populations in the central nervous system

1996 ◽  
Vol 109 (7) ◽  
pp. 1749-1757 ◽  
Author(s):  
N. Soussi-Yanicostas ◽  
J.P. Hardelin ◽  
M.M. Arroyo-Jimenez ◽  
O. Ardouin ◽  
R. Legouis ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Extracellular Matrix ◽  
Nervous System ◽  
Cell Membrane ◽  
Heparan Sulfate ◽  
Matrix Protein ◽  
Neuronal Cell ◽  
Extracellular Matrix Protein ◽  
Cell Populations

The KAL gene is responsible for the X-chromosome linked form of Kallmann's syndrome in humans. Upon transfection of CHO cells with a human KAL cDNA, the corresponding encoded protein, KALc, was produced. This protein is N-glycosylated, secreted in the cell culture medium, and is localized at the cell surface. Several lines of evidence indicate that heparan-sulfate chains of proteoglycan(s) are involved in the binding of KALc to the cell membrane. Polyclonal and monoclonal antibodies to the purified KALc were generated. They allowed us to detect and characterize the protein encoded by the KAL gene in the chicken central nervous system at late stages of embryonic development. This protein is synthesized by definite neuronal cell populations including Purkinje cells in the cerebellum, mitral cells in the olfactory bulbs and several subpopulations in the optic tectum and the striatum. The protein, with an approximate molecular mass of 100 kDa, was named anosmin-1 in reference to the deficiency of the sense of smell which characterizes the human disease. Anosmin-1 is likely to be an extracellular matrix component. Since heparin treatment of cell membrane fractions from cerebellum and tectum resulted in the release of the protein, we suggest that one or several heparan-sulfate proteoglycans are involved in the binding of anosmin-1 to the membranes in vivo.

scholarly journals Loss of the Extracellular Matrix Protein DIG-1 Causes Glial Fragmentation, Dendrite Breakage and Dendrite Extension Defects

2021 ◽  
Vol 9 (4) ◽  
pp. 42
Author(s):  
Megan K. Chong ◽  
Elizabeth R. Cebul ◽  
Karolina Mizeracka ◽  
Maxwell G. Heiman
Keyword(s):  
Extracellular Matrix ◽  
Nervous System ◽  
Young Adults ◽  
Glial Cell ◽  
Sensory Neurons ◽  
Matrix Protein ◽  
Extracellular Matrix Protein ◽  
C Elegans ◽  
Cellular Integrity ◽  
Novel Alleles

The extracellular matrix (ECM) guides and constrains the shape of the nervous system. In C. elegans, DIG-1 is a giant ECM component that is required for fasciculation of sensory dendrites during development and for maintenance of axon positions throughout life. We identified four novel alleles of dig-1 in three independent screens for mutants affecting disparate aspects of neuronal and glial morphogenesis. First, we find that disruption of DIG-1 causes fragmentation of the amphid sheath glial cell in larvae and young adults. Second, it causes severing of the BAG sensory dendrite from its terminus at the nose tip, apparently due to breakage of the dendrite as animals reach adulthood. Third, it causes embryonic defects in dendrite fasciculation in inner labial (IL2) sensory neurons, as previously reported, as well as rare defects in IL2 dendrite extension that are enhanced by loss of the apical ECM component DYF-7, suggesting that apical and basolateral ECM contribute separately to dendrite extension. Our results highlight novel roles for DIG-1 in maintaining the cellular integrity of neurons and glia, possibly by creating a barrier between structures in 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 Loss of the extracellular matrix protein DIG-1 causes glial fragmentation, dendrite breakage, and dendrite extension defects

2021 ◽  
Author(s):  
Megan K Chong ◽  
Elizabeth R Cebul ◽  
Karolina Mizeracka ◽  
Maxwell G Heiman
Keyword(s):  
Extracellular Matrix ◽  
Nervous System ◽  
Young Adults ◽  
Glial Cell ◽  
Sensory Neurons ◽  
Matrix Protein ◽  
Extracellular Matrix Protein ◽  
C Elegans ◽  
Cellular Integrity ◽  
Novel Alleles

The extracellular matrix (ECM) guides and constrains the shape of the nervous system. In C. elegans, DIG-1 is a giant ECM component that is required for fasciculation of sensory dendrites during development and for maintenance of axon positions throughout life. We identified four novel alleles of dig-1 in three independent screens for mutants affecting disparate aspects of neuronal and glial morphogenesis. First, we find that disruption of DIG-1 causes fragmentation of the amphid sheath glial cell in larvae and young adults. Second, it causes severing of the BAG sensory dendrite from its terminus at the nose tip, apparently due to breakage of the dendrite as animals reach adulthood. Third, it causes embryonic defects in dendrite fasciculation in inner labial (IL2) sensory neurons, as previously reported, as well as rare defects in IL2 dendrite extension that are enhanced by loss of the apical ECM component DYF-7, suggesting that apical and basolateral ECM contribute separately to dendrite extension. Our results highlight novel roles for DIG-1 in maintaining the cellular integrity of neurons and glia, possibly by creating a barrier between structures in the nervous system.

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.

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.

Sign in / Sign up

Export Citation Format

Share Document