scholarly journals Layilin, a Novel Integral Membrane Protein, Is a Hyaluronan Receptor

2001 ◽  
Vol 12 (4) ◽  
pp. 891-900 ◽  
Author(s):  
Petri Bono ◽  
Kristofer Rubin ◽  
Jonathan M. G. Higgins ◽  
Richard O. Hynes
Keyword(s):  
Cell Adhesion ◽  
Fusion Protein ◽  
Cell Shape ◽  
Transmembrane Protein ◽  
Adaptor Proteins ◽  
Integral Membrane Protein ◽  
Microtiter Plate ◽  
Binding Assays ◽  
Cellular Processes ◽  
Fc Fusion Protein

The actin cytoskeleton plays a significant role in changes of cell shape and motility, and interactions between the actin filaments and the cell membrane are crucial for a variety of cellular processes. Several adaptor proteins, including talin, maintain the cytoskeleton-membrane linkage by binding to integral membrane proteins and to the cytoskeleton. Layilin, a recently characterized transmembrane protein with homology to C-type lectins, is a membrane-binding site for talin in peripheral ruffles of spreading cells. To facilitate studies of layilin's function, we have generated a layilin-Fc fusion protein comprising the extracellular part of layilin joined to human immunoglobulin G heavy chain and used this chimera to identify layilin ligands. Here, we demonstrate that layilin-Fc fusion protein binds to hyaluronan immobilized to Sepharose. Microtiter plate-binding assays, coprecipitation experiments, and staining of sections predigested with different glycosaminoglycan-degrading enzymes and cell adhesion assays all revealed that layilin binds specifically to hyaluronan but not to other tested glycosaminoglycans. Layilin's ability to bind hyaluronan, a ubiquitous extracellular matrix component, reveals an interesting parallel between layilin and CD44, because both can bind to cytoskeleton-membrane linker proteins through their cytoplasmic domains and to hyaluronan through their extracellular domains. This parallelism suggests a role for layilin in cell adhesion and motility.

scholarly journals Ankyrin-binding domain of CD44(GP85) is required for the expression of hyaluronic acid-mediated adhesion function.

1994 ◽  
Vol 126 (4) ◽  
pp. 1099-1109 ◽  
Author(s):  
V B Lokeshwar ◽  
N Fregien ◽  
L Y Bourguignon
Keyword(s):  
Hyaluronic Acid ◽  
Cell Adhesion ◽  
Fusion Protein ◽  
Transmembrane Protein ◽  
Cytoplasmic Domain ◽  
Binding Domain ◽  
Binding Assays ◽  
Competition Binding ◽  
Biochemical Analyses ◽  
Extracellular Matrix Interactions

GP85 is one of the most common hemopoietic isoforms of the cell adhesion molecule, CD44. CD44(GP85) is known to contain at least one ankyrin-binding site within its 70 aa cytoplasmic domain and to bind hyaluronic acid (HA) with its extracellular domain. In this study we have mapped the ankyrin-binding domain of CD44(GP85) by deleting various portions of the cytoplasmic region followed by expression of these truncated cDNAs in COS cells. The results of these experiments indicate that the ankyrin-binding domain resides between amino acids 305 and 355. Biochemical analyses, using competition binding assays and a synthetic peptide (NGGNGT-VEDRKPSEL) containing 15 aa between aa 305 and aa 320, support the conclusion that this region is required for ankryin binding. Furthermore, we have constructed a fusion protein in which this 15 aa sequence of CD44(GP85) is transplanted onto another transmembrane protein which does not bind ankyrin. Our results show that this fusion protein acquires the ability to bind ankyrin confirming that the sequence (306NGGNGTVEDRKPSE320L) is a critical part of the ankryin-binding domain of CD44(GP85). In addition, we have demonstrated that deletion of this 15 aa ankyrin-binding sequence from CD44(GP85) results in a drastic reduction (> or = 90%) of HA-binding and HA-mediated cell adhesion. These findings strongly suggest that ankyrin binding to the cytoplasmic domain of CD44(GP85) plays a pivotal role in regulating hyaluronic acid-mediated cell-cell and cell-extracellular matrix interactions.

scholarly journals Anti-Tumor Activity and Pharmacokinetics of AP25-Fc Fusion Protein

2019 ◽  
Vol 16 (7) ◽  
pp. 1032-1041
Author(s):  
Dening Pei ◽  
Jialiang Hu ◽  
Chunming Rao ◽  
Pengcheng Yu ◽  
Hanmei Xu ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Fc Fusion Protein ◽  
Anti Tumor Activity

scholarly journals Predicting the Structure and Dynamics of Membrane Protein GerAB from Bacillus subtilis

2021 ◽  
Vol 22 (7) ◽  
pp. 3793
Author(s):  
Sophie Blinker ◽  
Jocelyne Vreede ◽  
Peter Setlow ◽  
Stanley Brul
Keyword(s):  
Bacillus Subtilis ◽  
Membrane Protein ◽  
Spore Germination ◽  
Structural Information ◽  
Transmembrane Protein ◽  
Homology Modelling ◽  
Water Channel ◽  
Md Simulations ◽  
Integral Membrane Protein ◽  
Starting Point

Bacillus subtilis forms dormant spores upon nutrient depletion. Germinant receptors (GRs) in spore’s inner membrane respond to ligands such as L-alanine, and trigger spore germination. In B. subtilis spores, GerA is the major GR, and has three subunits, GerAA, GerAB, and GerAC. L-Alanine activation of GerA requires all three subunits, but which binds L-alanine is unknown. To date, how GRs trigger germination is unknown, in particular due to lack of detailed structural information about B subunits. Using homology modelling with molecular dynamics (MD) simulations, we present structural predictions for the integral membrane protein GerAB. These predictions indicate that GerAB is an α-helical transmembrane protein containing a water channel. The MD simulations with free L-alanine show that alanine binds transiently to specific sites on GerAB. These results provide a starting point for unraveling the mechanism of L-alanine mediated signaling by GerAB, which may facilitate early events in spore germination.

scholarly journals Systemic administration of monovalent follistatin-like 3-Fc-fusion protein increases muscle mass in mice

iScience ◽  
2021 ◽  
pp. 102488
Author(s):  
Takayuki Ozawa ◽  
Masato Morikawa ◽  
Yasuyuki Morishita ◽  
Kazuki Ogikubo ◽  
Fumiko Itoh ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Muscle Mass ◽  
Systemic Administration ◽  
Fc Fusion Protein

scholarly journals Stick around: Cell–Cell Adhesion Molecules during Neocortical Development

Cells ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 118
Author(s):  
David de Agustín-Durán ◽  
Isabel Mateos-White ◽  
Jaime Fabra-Beser ◽  
Cristina Gil-Sanz
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Neural Cells ◽  
Surface Receptors ◽  
Cellular Processes ◽  
Neocortical Development ◽  
Classical Cadherins ◽  
Adhesive Interactions ◽  
Cell Cell

The neocortex is an exquisitely organized structure achieved through complex cellular processes from the generation of neural cells to their integration into cortical circuits after complex migration processes. During this long journey, neural cells need to establish and release adhesive interactions through cell surface receptors known as cell adhesion molecules (CAMs). Several types of CAMs have been described regulating different aspects of neurodevelopment. Whereas some of them mediate interactions with the extracellular matrix, others allow contact with additional cells. In this review, we will focus on the role of two important families of cell–cell adhesion molecules (C-CAMs), classical cadherins and nectins, as well as in their effectors, in the control of fundamental processes related with corticogenesis, with special attention in the cooperative actions among the two families of C-CAMs.

scholarly journals Long‐term safety and efficacy of recombinant factor VIII Fc fusion protein (rFVIIIFc) in subjects with haemophilia A

Haemophilia ◽  
2015 ◽  
Vol 22 (1) ◽  
pp. 72-80 ◽  
Author(s):  
B. Nolan ◽  
J. Mahlangu ◽  
D. Perry ◽  
G. Young ◽  
R. Liesner ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Factor Viii ◽  
Recombinant Factor Viii ◽  
Haemophilia A ◽  
Safety And Efficacy ◽  
Fc Fusion Protein

scholarly journals Characterization and comparison of commercially available TNF receptor 2-Fc fusion protein products

mAbs ◽  
2012 ◽  
Vol 4 (6) ◽  
pp. 761-774 ◽  
Author(s):  
Qingqiao Tan ◽  
Qingcheng Guo ◽  
Chen Fang ◽  
Chong Wang ◽  
Bohua Li ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Tnf Receptor ◽  
Fc Fusion Protein
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