Locomotory competence and laminin-specific cell surface binding sites are lost during myoblast differentiation

Development ◽  
1989 ◽  
Vol 105 (4) ◽  
pp. 795-802
Author(s):  
S.L. Goodman ◽  
R. Deutzmann ◽  
V. Nurcombe
Keyword(s):  
Cell Surface ◽  
Binding Sites ◽  
Radioligand Binding ◽  
Specific Interaction ◽  
Myoblast Differentiation ◽  
Specific Cell ◽  
Surface Binding ◽  
Cell Surface Binding ◽  
Locomotory Response ◽  
Specific Cell Surface

The specific interaction of embryonal cells with the extracellular matrix (ECM) is one of the principal forces influencing embryonal development (Hay, 1984; Trinkaus, 1984). We used a muscle satellite cell line (MM14dy) to determine the relationship between locomotory response to laminin and the expression of specific cell surface binding sites for it. Time lapse videomicroscopic analysis was used to study the locomotory response and radioligand binding assays and cell attachment assays were used to follow the expression levels of binding sites for laminin and its subfragments E8 and E1–4. We report here the novel finding that the ability of MM14dy to locomote over laminin diminishes and finally vanishes as the cells differentiate. The simultaneous drop in expression of binding sites for laminin is interpreted as being of potential significance during development and repair.

scholarly journals Cell surface-binding sites for progesterone mediate calcium uptake in human sperm.

1991 ◽  
Vol 266 (28) ◽  
pp. 18655-18659 ◽  
Author(s):  
P.F. Blackmore ◽  
J. Neulen ◽  
F. Lattanzio ◽  
S.J. Beebe
Keyword(s):  
Cell Surface ◽  
Binding Sites ◽  
Calcium Uptake ◽  
Human Sperm ◽  
Surface Binding ◽  
Cell Surface Binding

scholarly journals Structure and Analysis of R1 and R2 Pyocin Receptor-Binding Fibers

Viruses ◽  
2018 ◽  
Vol 10 (8) ◽  
pp. 427 ◽  
Author(s):  
Sergey Buth ◽  
Mikhail Shneider ◽  
Dean Scholl ◽  
Petr Leiman
Keyword(s):  
Cell Surface ◽  
Host Cell ◽  
Receptor Binding ◽  
Binding Sites ◽  
Cell Envelope ◽  
Surface Binding ◽  
Cell Surface Binding ◽  
C Terminus ◽  
Host Cell Surface ◽  
Substrate Binding Sites

The R-type pyocins are high-molecular weight bacteriocins produced by some strains of Pseudomonas aeruginosa to specifically kill other strains of the same species. Structurally, the R-type pyocins are similar to “simple” contractile tails, such as those of phage P2 and Mu. The pyocin recognizes and binds to its target with the help of fibers that emanate from the baseplate structure at one end of the particle. Subsequently, the pyocin contracts its sheath and drives the rigid tube through the host cell envelope. This causes depolarization of the cytoplasmic membrane and cell death. The host cell surface-binding fiber is ~340 Å-long and is attached to the baseplate with its N-terminal domain. Here, we report the crystal structures of C-terminal fragments of the R1 and R2 pyocin fibers that comprise the distal, receptor-binding part of the protein. Both proteins are ~240 Å-long homotrimers in which slender rod-like domains are interspersed with more globular domains—two tandem knob domains in the N-terminal part of the fragment and a lectin-like domain at its C-terminus. The putative substrate binding sites are separated by about 100 Å, suggesting that binding of the fiber to the cell surface causes the fiber to adopt a certain orientation relative to the baseplate and this then triggers sheath contraction.

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