Importance of the membrane-proximal extracellular domains for activation of the signal transducer glycoprotein 130.

Signal Transducer Glycoprotein 130 Extracellular Domains for Activation of the Importance of the Membrane - Proximal

Signal transducer gp130: biochemical characterization of the three membrane-proximal extracellular domains and evaluation of their oligomerization potential.

Glycoprotein 130 (gp130) is a type I transmembrane protein and serves as the common signal-transducing receptor subunit of the interleukin-6-type cytokines. Whereas the membrane-distal half of the gp130 extracellular part confers ligand binding and has been subject to intense investigation, the structural and functional features of its membrane-proximal half are poorly understood. On the basis ...

Research Paper: GONAL-F Induced Endometrial Thickness Changes in Ovariectomized Rats With and Without HCG

Introduction: To attach the fetus to the endometrial epithelium, the endometrium should be affected and allowed by the steroid hormones secreted from the ovary. Thus, the endometrium is then subject to several structural and biochemical changes. Implantation involves the embedment, adhesion and invasion steps that specific receptors are engaged in that. The role of membrane receptors in uterine...

Changing Roles of Matrix Metalloproteases and Their Inhibitors, TIMPs, During Tumor Progression and Angiogenesis

Inhibition of matrix-metalloproteinases (MMPs) by tissue inhibitors of metalloproteinases (TIMPs) has been shown in vivo to decrease metastasis and tumor-associated angiogenesis. Our laboratory is interested in understanding the role of these proteins at the pericellular microenvironment of tumor and endothelial cells. Secretion of MMPs by tumor cells enables the migration, invasion and metasta...

Association of the membrane proximal regions of the alpha and beta subunit cytoplasmic domains constrains an integrin in the inactive state.

The adhesiveness of integrins is regulated through a process termed "inside-out" signaling. To understand the molecular mechanism of integrin inside-out signaling, we generated K562 stable cell lines that expressed LFA-1 (alpha(L)beta(2)) or Mac-1 (alpha(M)beta(2)) with mutations in the cytoplasmic domain. Complete truncation of the beta(2) cytoplasmic domain, but not a truncation that retained...