Evidence for a second class of membrane glycoprotein involved in cell adhesion

1989 ◽  
Vol 93 (4) ◽  
pp. 631-640
Author(s):  
W.E. Norris
Keyword(s):  
Extracellular Matrix ◽  
Biological Activity ◽  
Cell Adhesion ◽  
Membrane Proteins ◽  
Soluble Fraction ◽  
Biological Activities ◽  
Integral Membrane Proteins ◽  
Membrane Glycoprotein ◽  
Transmembrane Receptors ◽  
Triton X

It is believed that transmembrane relationships exist between the cytoskeleton and the extracellular matrix through integral membrane proteins, almost certainly glycoproteins, which would act as transmembrane receptors. Such receptors would include those involved in cell adhesion. I have been able to isolate a detergent-soluble fraction from chick embryo fibroblasts that is enriched in these integral membrane proteins by making use of their amphipathic character to phase-separate them in the detergent Triton X-114. Antisera raised to this fraction had biological activities interfering with cell adhesion and motility. A 45 X 10(3) Mr glycoprotein unique to this fraction appears to be responsible for this biological activity and is a candidate for a transmembrane receptor involved in cell adhesion.

scholarly journals Fractionation of Tetrahymena ciliary membranes with triton X-114 and the identification of a ciliary membrane ATPase.

1988 ◽  
Vol 107 (6) ◽  
pp. 2679-2688 ◽  
Author(s):  
W L Dentler
Keyword(s):  
Membrane Proteins ◽  
Atpase Activity ◽  
Tetrahymena Thermophila ◽  
High Molecular Mass ◽  
Integral Membrane Proteins ◽  
Matrix Proteins ◽  
Membrane Atpase ◽  
The Matrix ◽  
Triton X

Cilia were isolated from Tetrahymena thermophila, extracted with Triton X-114, and the detergent-soluble membrane + matrix proteins separated into Triton X-114 aqueous and detergent phases. The aqueous phase polypeptides include a high molecular mass polypeptide previously identified as a membrane dynein, detergent-soluble alpha and beta tubulins, and numerous polypeptides distinct from those found in axonemes. Integral membrane proteins partition into the detergent phase and include two major polypeptides of 58 and 50 kD, a 49-kD polypeptide, and 5 polypeptides in relatively minor amounts. The major detergent phase polypeptides are PAS-positive and are phosphorylated in vivo. A membrane-associated ATPase, distinct from the dynein-like protein, partitions into the Triton X-114 detergent phase and contains nearly 20% of the total ciliary ATPase activity. The ATPase requires Mg++ or Ca++ and is not inhibited by ouabain or vanadate. This procedure provides a gentle and rapid technique to separate integral membrane proteins from those that may be peripherally associated with the matrix or membrane.

scholarly journals Biosynthesis of the neural cell adhesion molecule: characterization of polypeptide C.

1985 ◽  
Vol 101 (6) ◽  
pp. 2310-2315 ◽  
Author(s):  
O Nybroe ◽  
M Albrechtsen ◽  
J Dahlin ◽  
D Linnemann ◽  
J M Lyles ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cell Adhesion ◽  
Membrane Proteins ◽  
Glial Cells ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Cell Types ◽  
Integral Membrane Proteins ◽  
Neural Cell Adhesion

The biosynthesis of the neural cell adhesion molecule (N-CAM) was studied in primary cultures of rat cerebral glial cells, cerebellar granule neurons, and skeletal muscle cells. The three cell types produced different N-CAM polypeptide patterns. Glial cells synthesized a 135,000 Mr polypeptide B and a 115,000 Mr polypeptide C, whereas neurons expressed a 200,000 Mr polypeptide A as well as polypeptide B. Skeletal muscle cells produced polypeptide B. The polypeptides synthesized by the three cell types were immunochemically identical. The membrane association of polypeptide C was investigated with methods that distinguish peripheral and integral membrane proteins. Polypeptide C was found to be a peripheral membrane protein, whereas polypeptides A and B were integral membrane proteins with cytoplasmic domains of approximately 50,000 and approximately 25,000 Mr, respectively. The affinity of the membrane binding of polypeptide C increased during postnatal development. The posttranslational modifications of polypeptide C were investigated in glial cell cultures, and it was found to be N-linked glycosylated and sulfated.

Extraction and identification of human platelet integral membrane proteins using triton X-114

1982 ◽  
Vol 27 (2) ◽  
pp. 221-224 ◽  
Author(s):  
Peter J. Newman ◽  
Michael A. Knipp ◽  
Richard A. Kahn
Keyword(s):  
Membrane Proteins ◽  
Human Platelet ◽  
Integral Membrane Proteins ◽  
Triton X

Spatial and temporal expression of fibronecttns and integrins during Xenopus development

1992 ◽  
Vol 50 (1) ◽  
pp. 598-599
Author(s):  
Douglas W. DeSimone ◽  
M. Susan Dalton ◽  
Mark D. Hens ◽  
Bethanne Hill ◽  
Joe W. Ramos ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Structure Function ◽  
Temporal Expression ◽  
Transmembrane Receptors ◽  
Cellular Processes ◽  
Basic Body ◽  
Cell Adhesion And Migration ◽  
Adhesive Interactions ◽  
And Migration

A central challenge in biology is to understand the cellular processes that direct morphogenesis and the formation of the basic body plan during development. These events are controlled to large extent, by adhesive interactions of cells with one another and with their extracellular environments. Specifically, we are investigating the structure, function and expression of two groups of molecules thought to play important roles in promoting cell adhesion and migration in the embryo: fibronectins (FNs), which are large extracellular matrix (ECM) glycoproteins with many adhesion related functions; and integrins, which are the cellular transmembrane-receptors for FNs and several other components of the ECM.

scholarly journals Ca2+-independent cell-adhesion activity of claudins, a family of integral membrane proteins localized at tight junctions

1999 ◽  
Vol 9 (18) ◽  
pp. 1035-S1 ◽  
Author(s):  
Koji Kubota ◽  
Mikio Furuse ◽  
Hiroyuki Sasaki ◽  
Noriyuki Sonoda ◽  
Kohji Fujita ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Membrane Proteins ◽  
Tight Junctions ◽  
Integral Membrane Proteins ◽  
Adhesion Activity
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