Inhibition of P-selectin specific cell adhesion by a low molecular weight, non-carbohydrate compound, KF38789

2001 ◽  
Vol 50 (11) ◽  
pp. 544-551 ◽  
Author(s):  
S. Ohta ◽  
Y. Inujima ◽  
M. Abe ◽  
Y. Uosaki ◽  
S. Sato ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cell Adhesion ◽  
Low Molecular Weight ◽  
Specific Cell

Low-Molecular-Weight Heparins Inhibit CCL21-Induced T Cell Adhesion and Migration

2002 ◽  
Vol 302 (1) ◽  
pp. 290-295 ◽  
Author(s):  
Kent W. Christopherson ◽  
James J. Campbell ◽  
Jeffrey B. Travers ◽  
Robert A. Hromas
Keyword(s):  
Molecular Weight ◽  
Cell Adhesion ◽  
T Cell ◽  
Low Molecular Weight ◽  
Low Molecular Weight Heparins ◽  
Cell Adhesion And Migration ◽  
And Migration ◽  
T Cell Adhesion

Low molecular weight heparin inhibits melanoma cell adhesion and migration through a PKCa/JNK signaling pathway inducing actin cytoskeleton changes

2011 ◽  
Vol 312 (2) ◽  
pp. 235-244 ◽  
Author(s):  
Georgia Chalkiadaki ◽  
Dragana Nikitovic ◽  
Pavlos Katonis ◽  
Aikaterini Berdiaki ◽  
Aristidis Tsatsakis ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Signaling Pathway ◽  
Low Molecular Weight Heparin ◽  
Low Molecular Weight ◽  
Jnk Signaling ◽  
Cell Adhesion And Migration ◽  
Jnk Signaling Pathway ◽  
And Migration

scholarly journals Lymphocyte Function-associated Antigen-1-mediated T Cell Adhesion Is Impaired by Low Molecular Weight Phosphotyrosine Phosphatase-dependent Inhibition of FAK Activity

2003 ◽  
Vol 278 (38) ◽  
pp. 36763-36776 ◽  
Author(s):  
Elisa Giannoni ◽  
Paola Chiarugi ◽  
Giacomo Cozzi ◽  
Lucia Magnelli ◽  
Maria Letizia Taddei ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cell Adhesion ◽  
T Cell ◽  
Low Molecular Weight ◽  
Lymphocyte Function ◽  
Phosphotyrosine Phosphatase ◽  
Dependent Inhibition ◽  
T Cell Adhesion

Promotion of cell adhesion by low-molecular-weight hydrogel by Lys based amphiphile

2015 ◽  
Vol 47 ◽  
pp. 345-350 ◽  
Author(s):  
Torao Suga ◽  
Satoshi Osada ◽  
Takayuki Narita ◽  
Yushi Oishi ◽  
Hiroaki Kodama
Keyword(s):  
Molecular Weight ◽  
Cell Adhesion ◽  
Low Molecular Weight

scholarly journals Role of Receptor for Hyaluronic Acid-mediated Motility (RHAMM) in Low Molecular Weight Hyaluronan (LMWHA)-mediated Fibrosarcoma Cell Adhesion

2011 ◽  
Vol 286 (44) ◽  
pp. 38509-38520 ◽  
Author(s):  
Katerina Kouvidi ◽  
Aikaterini Berdiaki ◽  
Dragana Nikitovic ◽  
Pavlos Katonis ◽  
Nikos Afratis ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Hyaluronic Acid ◽  
Cell Adhesion ◽  
Low Molecular Weight ◽  
Fibrosarcoma Cell

scholarly journals Reversible Masking Using Low-Molecular-Weight Neutral Lipids to Achieve Optimal-Targeted Delivery

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Nancy Smyth Templeton ◽  
Neil Senzer
Keyword(s):  
Molecular Weight ◽  
Targeted Delivery ◽  
Neutral Lipids ◽  
Metastatic Cancer ◽  
Target Cells ◽  
Low Molecular Weight ◽  
Specific Cell ◽  
Surface Receptors ◽  
Normal Tissues ◽  
Delivery Vehicles

Intravenous injection of therapeutics is required to effectively treat or cure metastatic cancer, certain cardiovascular diseases, and other acquired or inherited diseases. Using this route of delivery allows potential uptake in all disease targets that are accessed by the bloodstream. However, normal tissues and organs also have the potential for uptake of therapeutic agents. Therefore, investigators have used targeted delivery to attempt delivery solely to the target cells; however, use of ligands on the surface of delivery vehicles to target specific cell surface receptors is not sufficient to avoid nonspecific uptake. PEGylation has been used for decades to try to avoid nonspecific uptake but suffers from many problems known as “The PEGylation Dilemma.” We have solved this dilemma by replacing PEGylation with reversible masking using low-molecular-weight neutral lipids in order to achieve optimal-targeted delivery solely to target cells. Our paper will focus on this topic.

Review: Inhibitory potential of low molecular weight Heparin in cell adhesion; emphasis on tumor metastasis

2021 ◽  
Vol 892 ◽  
pp. 173778
Author(s):  
Umer Ejaz ◽  
Fahad Akhtar ◽  
Jinbing Xue ◽  
Xinyu Wan ◽  
Tong Zhang ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cell Adhesion ◽  
Low Molecular Weight Heparin ◽  
Tumor Metastasis ◽  
Low Molecular Weight ◽  
Inhibitory Potential

scholarly journals Reversible conformational changes induced in glycoprotein IIb-IIIa by a potent and selective peptidomimetic inhibitor

Blood ◽  
1992 ◽  
Vol 80 (10) ◽  
pp. 2539-2547 ◽  
Author(s):  
WC Kouns ◽  
D Kirchhofer ◽  
P Hadvary ◽  
A Edenhofer ◽  
T Weller ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibody ◽  
Cell Adhesion ◽  
Platelet Aggregation ◽  
Conformational Changes ◽  
Platelet Membrane ◽  
Platelet Glycoprotein ◽  
Low Molecular Weight ◽  
Antithrombotic Agents ◽  
Fibrinogen Binding

Abstract Platelet glycoprotein (GP) IIb-IIIa inhibitors may become useful antithrombotic agents. Ro 4–5054 is a low molecular weight, noncyclic, peptidomimetic inhibitor that is three orders of magnitude more potent than RGDS in inhibiting fibrinogen binding to purified GPIIb-IIIa and in preventing platelet aggregation. Comparisons of RGDS and Ro 4–5054 in cell adhesion assays showed that, in contrast to RGDS, Ro 4–5054 was highly selective GPIIb-IIIa inhibitor. Effects of RGDV and Ro 4– 5054 on the conformation and activation state of GPIIb-IIIa were also examined. RGDV and Ro 4–5054 induced conformational changes in purified inactive GPIIb-IIIa as determined by binding of the monoclonal antibody D3GP3 (D3). These conformational alterations were not reversed after inhibitor removal, as indicated by the continued exposure of the D3 epitope and a newly acquired ability to bind fibrinogen. Similarly, RGDV and Ro 4–5054 induced conformational changes in GPIIb-IIIa on the intact platelet. However, after removal of the inhibitors, exposure of the D3 epitope was fully reversed and the platelets did not aggregate in the absence of agonist. Thus, while RGD(X) peptides and Ro 4–5054 transformed purified inactive GPIIb-IIIa into an irreversibly activated conformer, the effects of these inhibitors were reversible on the intact platelet. This suggests that factors present in the platelet membrane or cytoplasm may regulate in part the ability of the complex to shift between active and inactive conformers.

Sign in / Sign up

Export Citation Format

Share Document