SLAC2B‐dependent microtubule acetylation regulates extracellular matrix‐mediated intracellular TM4SF5 traffic to the plasma membranes

2021 ◽  
Vol 35 (3) ◽  
Author(s):  
Hye‐Jin Kim ◽  
Eunmi Kim ◽  
Haesong Lee ◽  
Jae Woo Jung ◽  
Ji Eon Kim ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Plasma Membranes

Immunolocalization of fimbrial epitopes in thin sections of Microbotryum violaceum

1997 ◽  
Vol 43 (2) ◽  
pp. 136-142 ◽  
Author(s):  
Martina Celerin ◽  
Alan W. Day ◽  
Ronald J. Smith ◽  
David E. Laudenbach
Keyword(s):  
Extracellular Matrix ◽  
Cell Wall ◽  
Plasma Membranes ◽  
Microbotryum Violaceum ◽  
Thin Sections ◽  
Present Evidence ◽  
Biochemical Analyses ◽  
Protein Moiety ◽  
Peripheral Cytoplasm

Fungal fimbriae are long (0.5–20 μm), narrow (7 nm) surface appendages that have been observed on most members of the Mycota. Biochemical analyses have determined that fimbriae from Microbotryum violaceum are composed of 74-kDa glycoproteinaceous subunits in which the protein moiety is fungal collagen. We present evidence for the localization of fimbrial subunits prior to their exportation from the cell. We term these internal, likely nonpolymerized fimbriae "pro-fimbriae" and demonstrate the location of the reserves within the peripheral cytoplasm. Also, we show that fimbriae may not traverse the cell wall as previously believed, but may instead originate from within the outer lamella of the cell wall, possibly being anchored to the cell wall via other molecules. This model is analogous to the animal extracellular matrix arrangement in which collagens are anchored to plasma membranes via other proteins such as fibronectin.Key words: fungus, immunolocalization, fimbriae, Microbotryum, Ustilago.

scholarly journals Modulation of 5′-nucleotidase activity in plasma membranes and intact cells by the extracellular matrix proteins laminin and fibronectin

1992 ◽  
Vol 282 (1) ◽  
pp. 181-188 ◽  
Author(s):  
N Olmo ◽  
J Turnay ◽  
G Risse ◽  
R Deutzmann ◽  
K von der Mark ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Plasma Membrane ◽  
Inhibitory Activity ◽  
Plasma Membranes ◽  
Extracellular Matrix Proteins ◽  
Cell Receptor ◽  
Inhibitory Effect ◽  
Matrix Proteins ◽  
Nucleotidase Activity ◽  
Intact Cells

Modulation of 5′-nucleotidase activity by the extracellular matrix proteins fibronectin, laminin and their fragments has been studied in plasma membrane preparations as well as in intact BCS-TC2 and Rugli cells. The ectoenzyme on plasma membranes is activated by laminin; fibronectin inhibits the AMPase activity on BCS-TC2 plasma membranes but no inhibitory effect is found in plasma membrane preparations from Rugli cells. These effects are dependent on the preincubation time and protein concentration. When the effect of the extracellular matrix proteins is studied on intact cells, both BCS-TC2 and Rugli cells show similar behaviour. A decrease in the enzyme activity is observed in the presence of fibronectin. The AMPase inhibitory activity is located on its 40 kDa fragment. No inhibitory activity is found in other fibronectin fragments, including the 140 kDa fragment which contains the RGDS cell-adhesion sequence. Laminin and its E1-4 and E8 fragments are able to activate the ecto-5′-nucleotidase activity of both BCS-TC2 and Rugli cells. The effect of the E1-4 fragment on intact cells is greater than that observed for the E8 fragment and uncleaved laminin. Our results suggest a bifunctional role for 5′-nucleotidase as ectoenzyme and cell receptor for extracellular matrix proteins.

scholarly journals A plasma membrane protein is involved in cell contact-mediated regulation of tissue-specific genes in adult hepatocytes.

1991 ◽  
Vol 115 (2) ◽  
pp. 505-515 ◽  
Author(s):  
A Corlu ◽  
B Kneip ◽  
C Lhadi ◽  
G Leray ◽  
D Glaise ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Plasma Membrane ◽  
Membrane Protein ◽  
Plasma Membranes ◽  
Surface Protein ◽  
Cell Aggregation ◽  
Cell Interaction ◽  
Cell Contact ◽  
Plasma Membrane Protein ◽  
Extracellular Matrix Components

We have identified the liver-regulating protein (LRP), a cell surface protein involved in the maintenance of hepatocyte differentiation when cocultured with rat liver epithelial cells (RLEC). LRP was defined by immunoreactivity to a monoclonal antibody (mAb L8) prepared from RLEC. mAb L8 specifically detected two polypeptides of 85 and 73 kD in immunoprecipitation of both hepatocyte- and RLEC-iodinated plasma membranes. The involvement of these polypeptides, which are integral membrane proteins, in cell interaction-mediated regulation of hepatocytes was assessed by evaluating the perturbing effects of the antibody on cocultures with RLEC. Several parameters characteristic of differentiated hepatocytes were studied, such as liver-specific and house-keeping gene expression, cytoskeletal organization and deposition of extracellular matrix (ECM). An early cytoskeletal disturbance was evidenced and a marked alteration of hepatocyte functional capacity was observed in the presence of the antibody, together with a loss of ECM deposition. By contrast, cell-cell aggregation or cell adhesion to various extracellular matrix components were not affected. These findings suggest that LRP is distinct from an extracellular matrix receptor. The fact that early addition of mAb L8 during cell contact establishment was necessary to be effective may indicate that LRP is a novel plasma membrane protein that plays an early pivotal role in the coordinated metabolic changes which lead to the differentiated phenotype of mature hepatocytes.

scholarly journals Crosstalk between basal extracellular matrix adhesion and building of apical architecture during morphogenesis

Biology Open ◽  
2021 ◽  
Vol 10 (11) ◽  
Author(s):  
Mariana Barrera-Velázquez ◽  
Luis Daniel Ríos-Barrera
Keyword(s):  
Extracellular Matrix ◽  
Plasma Membrane ◽  
Cell Shape ◽  
Plasma Membranes ◽  
Tube Formation ◽  
Apical Plasma Membrane ◽  
Complex Structures ◽  
Apicobasal Polarity ◽  
Basal Plasma ◽  
Shape Changes

ABSTRACT Tissues build complex structures like lumens and microvilli to carry out their functions. Most of the mechanisms used to build these structures rely on cells remodelling their apical plasma membranes, which ultimately constitute the specialised compartments. In addition to apical remodelling, these shape changes also depend on the proper attachment of the basal plasma membrane to the extracellular matrix (ECM). The ECM provides cues to establish apicobasal polarity, and it also transduces forces that allow apical remodelling. However, physical crosstalk mechanisms between basal ECM attachment and the apical plasma membrane remain understudied, and the ones described so far are very diverse, which highlights the importance of identifying the general principles. Here, we review apicobasal crosstalk of two well-established models of membrane remodelling taking place during Drosophila melanogaster embryogenesis: amnioserosa cell shape oscillations during dorsal closure and subcellular tube formation in tracheal cells. We discuss how anchoring to the basal ECM affects apical architecture and the mechanisms that mediate these interactions. We analyse this knowledge under the scope of other morphogenetic processes and discuss what aspects of apicobasal crosstalk may represent widespread phenomena and which ones are used to build subsets of specialised compartments.

scholarly journals Properties of Plasma Membranes from Granulation Tissue with Reference to Extracellular Matrix.

1975 ◽  
Vol 29b ◽  
pp. 963-968 ◽  
Author(s):  
Pirjo Lehtinen ◽  
Liisa Känkänen ◽  
E. Kulonen ◽  
J. Jänne ◽  
Synnøve Liaaen-Jensen
Keyword(s):  
Extracellular Matrix ◽  
Granulation Tissue ◽  
Plasma Membranes

scholarly journals Regulation of Oligodendrocyte Functions: Targeting Lipid Metabolism and Extracellular Matrix for Myelin Repair

2020 ◽  
Vol 9 (2) ◽  
pp. 470 ◽  
Author(s):  
Davide Marangon ◽  
Marta Boccazzi ◽  
Davide Lecca ◽  
Marta Fumagalli
Keyword(s):  
Extracellular Matrix ◽  
Lipid Metabolism ◽  
Plasma Membranes ◽  
Neurological Diseases ◽  
Membrane Composition ◽  
Myelin Repair ◽  
Approved Drugs ◽  
Fda Approved Drugs ◽  
Extracellular Environment

Myelin is an essential structure that protects axons, provides metabolic support to neurons and allows fast nerve transmission. Several neurological diseases, such as multiple sclerosis, are characterized by myelin damage, which is responsible of severe functional impairment. Myelin repair requires the timely recruitment of adult oligodendrocyte precursor cells (OPCs) at the lesion sites, their differentiation and maturation into myelinating oligodendrocytes. As a consequence, OPCs undergo profound changes in their morphology, functions, and interactions with other cells and extracellular environment, thus requiring the reorganization of both their lipid metabolism and their membrane composition, which is substantially different compared to other plasma membranes. Despite the growing knowledge in oligodendroglia biology and in the mechanisms involved in OPC-mediated regeneration, the identification of strategies to promote remyelination still remains a challenge. Here, we describe how altered lipid metabolism in oligodendrocytes influences the pathogenesis of demyelination, and we show that several FDA-approved drugs with a previously unknown remyelination potential do act on cholesterol and lipid biosynthetic pathways. Since the interplay between myelin lipids and axons is strictly coordinated by the extracellular matrix (ECM), we also discuss the role of different ECM components, and report the last findings on new ECM-modifiers able to foster endogenous remyelination.

scholarly journals Nerve terminal anchorage protein 1 (TAP-1) is a chondroitin sulfate proteoglycan: biochemical and electron microscopic characterization.

1987 ◽  
Vol 105 (6) ◽  
pp. 3075-3086 ◽  
Author(s):  
S S Carlson ◽  
T N Wight
Keyword(s):  
Molecular Weight ◽  
Extracellular Matrix ◽  
Electron Microscope ◽  
Chondroitin Sulfate ◽  
Basal Lamina ◽  
Nerve Terminal ◽  
Plasma Membranes ◽  
Average Molecular Weight ◽  
Electric Organ ◽  
Side Chains

The plasma membranes of the nerve terminal and the postsynaptic cell of electric organ are separated by a basal lamina. We have purified, biochemically characterized, and visualized in the electron microscope a macromolecule which appears to anchor the nerve terminal to this basal lamina. This molecule, terminal anchorage protein 1 (TAP-1) is associated with the nerve terminal membrane of electric organ, has the properties of an integral membrane protein, and is tightly bound to the extracellular matrix (Carlson, S.S., P. Caroni, and R.B. Kelly. 1986. J. Cell Biol. 103:509-520). TAP-1 can be solubilized from an electric organ extracellular matrix preparation with guanidine-HCl/3-[(3-cholamidopropyl)-dimethylammnio]-1-propane sulfonate and purified by a combination of permeation chromatography on Sephacryl S-1000, sedimentation velocity, and ion exchange chromatography on DEAE Sephacel. The total purification from electric organ is 91-fold and results in at least 86% purity. Digestion of the molecule with chondroitin ABC or AC lyase produces a large but similar shift in the molecular weight of the molecule on SDS-PAGE. The presence of chondroitin-4- or 6-sulfate is confirmed by identification of the isolated glycosaminoglycans with cellulose acetate electrophoresis. Gel filtration of the isolated chains indicates an average molecular weight of 42,000. Digestion of TAP-1 with other glycosaminoglycan lyases such as heparitinase indicates that only chondroitin sulfate is present. These results demonstrate that TAP-1 is a proteoglycan. Visualization of TAP-1 in the electron microscope reveals a "bottlebrush" structure expected for a proteoglycan. The molecule has an average total length of 345 +/- 17 nm with 20 +/- 2 side projections of 113 +/- 5 nm in length. These side projections are presumably the glycosaminoglycan side chains. From this structure, we predict that the TAP-1 glycosaminoglycan side chains should have a molecular weight of approximately 50,000, which is in close agreement with the biochemical studies. Both biochemical and morphologic data indicate that TAP-1 has a relative molecular weight of approximately 1.2 X 10(6). The large size of TAP-1 suggests that this molecule could span the synaptic cleft and make a significant contribution to the structure of the nerve terminal basal lamina of electric organ.

Changes in cell surface expression of fibronectin and fibronectin receptor during liver regeneration

1992 ◽  
Vol 102 (4) ◽  
pp. 815-820
Author(s):  
C. Pujades ◽  
E. Forsberg ◽  
C. Enrich ◽  
S. Johansson
Keyword(s):  
Extracellular Matrix ◽  
Liver Regeneration ◽  
Immunohistochemical Staining ◽  
Plasma Membranes ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Pericellular Matrix ◽  
Plasma Fibronectin ◽  
Integrin Receptor ◽  
Fibronectin Receptor

The surface expression of fibronectin and its major integrin receptor in liver, integrin alpha 5 beta 1, was studied during liver regeneration after partial hepatectomy. Using immunoblotting, plasma membranes isolated from livers at different regeneration stages were found to contain 6- to 8-fold elevated levels of fibronectin, alpha 5 and beta 1 at 12–24 h after the operation. Normal levels were gradually restored during the following 8–9 days. The membrane-associated fibronectin lacked the ED-A domain, suggesting that it consisted of plasma fibronectin. A prominent fibronectin fragment (180 kDa) was present at 12–24 h after surgery, possibly reflecting turnover of the pericellular matrix during cell division. Indirect immunohistochemical staining of liver sections revealed beta 1 and fibronectin mainly in the sinusoidal region of the hepatocyte plasma membrane. The distribution was not markedly altered during liver regeneration. The results suggest that the fibronectin-mediated contacts between the cells and the extracellular matrix increase during the pre-replicative and proliferative phases of liver regeneration. The significance of these results for the growth and for the structure of the liver during regeneration and development is discussed.

scholarly journals Effects of cell density and extracellular matrix on the lateral diffusion of major histocompatibility antigens in cultured fibroblasts.

1986 ◽  
Vol 103 (1) ◽  
pp. 215-222 ◽  
Author(s):  
M L Wier ◽  
M Edidin
Keyword(s):  
Extracellular Matrix ◽  
Cell Density ◽  
Plasma Membranes ◽  
Proteolytic Enzymes ◽  
Lateral Diffusion ◽  
Human Skin Fibroblast ◽  
Major Histocompatibility ◽  
Cultured Fibroblasts ◽  
Mhc Antigens ◽  
Cell Cell

We have studied the effect of cell density on the lateral diffusion of major histocompatibility (MHC) antigens in the plasma membranes of fibroblasts using fluorescence recovery after photobleaching. The percent recovery of fluorescence was decreased in fibroblasts grown in confluent cultures. While recovery of fluorescence was measurable in greater than 90% of the cells from sparse cultures, measurable recovery was detected in only 60-80% of the cells from dense cultures; no mobile antigens were detectable in 20-40% of cells examined. The diffusion coefficient on human skin fibroblast cells that did show recovery was the same for cells grown in sparse or dense conditions. In WI-38, VA-2, and c1 1d cultures the diffusion coefficients of mobile antigens were smaller in cells from dense cultures. Changes in lateral diffusion occurred with increased cell-cell contact and with age of cell culture but were not observed in growth-arrested cells or in sparse cells cultured in medium conditioned by confluent cells. Decreased mobile fractions of MHC antigens were observed when cells were plated on extracellular matrix materials derived from confluent cultures. Treatment of the extracellular matrix materials with a combination of proteolytic enzymes or by enzymes that degrade proteoglycans abolished this effect. Matrices produced by cells from other cell lines were less effective in inducing changes in mobile fractions and purified matrix components alone did not induce changes in lateral diffusion. Finally, there were no differences in the proportion of MHC antigens that were resistant to Triton X-100 extraction in sparse and dense cells. These results suggest that cell-cell interactions mediated through extracellular matrix materials can influence the lateral diffusion of at least part of the population of MHC antigens.

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