Antibodies that bind complex glycosaminoglycans accumulate in the Golgi.

Light (L) chains that edit anti-DNA heavy (H) chains rescue B-cell development by suppressing DNA binding. However, exceptional editor L chains allow B cells to reach splenic compartments even though their B-cell receptors remain autoreactive. Such incompletely edited B cells express multireactive antibodies that accumulate in the Golgi and are released as insoluble, amyloid-like immune complexes.

Consequences of receptor editing at the lambda locus: multireactivity and light chain secretion.

To investigate the manner in which B cells with lambda light (L) chains undergo receptor editing, we have studied hybridoma panels from 56R/kappa-deleted (kdel) mice. 56R/kdel mice only produce four L chains (lambda1, lambda2, lambda3, and lambdaX). They also have a simplified heavy (H) chain repertoire: All B cells start out with a 56R anti-DNA H chain.

[Relationship between protein tyrosine phosphorylation level and anoikis resistance of breast tumor cell lines].

Background & Objectives: Normal epithelial or endothelial cells can undergo anoikis, a type of apoptosis, when they are detached from their extracellular matrices (ECM), while most tumor cells derived from epithelial or endothelial tissues lose this feature. Most of the studies indicate that anoikis resistance of tumor cells is closely related to abnormal signal transductioin. The aim of this research was to screen out the tumor cell lines that are anoikis resistant, then to investigate the relationship between the protein tyrosine phosphorylation of signaling molecules and anoikis resistance feature of tumor cells.

PH domain of G protein-coupled receptor kinase-2 binds to protein kinase C (PKC) and negatively regulates activity of PKC kinase.

G protein-coupled receptor kinase-2 (GRK),also known as beta1-adrenergic receptor kinase(beta-ARK1), plays an important role in agonist-induced desensitization of the beta-adrenergic receptors. Activation of protein kinase C (PKC) is able to stimulate phosphorylation and activation of GRKs and induce desensitization of G protein-coupled receptor. However, detail mechanism of interaction between PKC and GRK2 and the effect of GRK2 on activity of PKC remain unknown.

Identification of the Peptides that Bind to Tyrosine Kinase Receptor EphB2 by Phage Display.

The gene encoding the Ig-like domain of tyrosine protein kinase receptor EphB2 was cloned into the expressing vector pET28a. Under induction with IPTG, the positive strain expressed the fusion protein with a hexahistidine tail on the N-terminal. The protein was purified under denaturing conditions using metal chelate chromatography.