G-CSF induces the release of the soluble form of LR11, a regulator of myeloid cell mobilization in bone marrow.

Granulocyte colony-stimulating factor (G-CSF) induces the mobilization of leukocytes from the bone marrow (BM) to the circulation by a yet incompletely understood mechanism. Here, we describe that the membrane-bound receptor LR11 is highly expressed in human myeloid cells and that the shed soluble form of LR11 (sLR11) is a modifier of myeloid cell migration. In the process of leukocyte mobilization by G-CSF treatment, circulating sLR11 levels are transiently elevated in humans and mice.

Circulating soluble LR11/SorLA levels are highly increased and ameliorated by chemotherapy in acute leukemias.

Background: LR11/SorLA, a receptor interacting with CD87 on monocytes and macrophages, is highly expressed on human immature hematopoietic stem cells. However, it is unknown whether LR11 is expressed on premature leukemic cells, and whether the levels of circulating soluble LR11 (sLR11) shed from leukemic cells correlate with disease state.

Methods: The expression of LR11 on leucocytes and leukemic cells was examined by flow cytometry.

LDL receptor family: isolation, production, and ligand binding analysis.

Members of the low density lipoprotein receptor gene family have recently received particular attention because of their involvement not only in lipoprotein transport, but also in signal transduction pathways. The main characteristic feature of this protein group is their cysteine-rich ligand binding domain, which is able to bind many unrelated proteins, such as apolipoproteins, proteases, and protease/inhibitor complexes, signaling molecules such as reelin, and several other groups of proteins. The main challenges of studying these proteins in vitro are their extremely high content of disulfide bridges and the detergent-sensibility of their classical ligands, i.

Receptor-mediated chicken oocyte growth: differential expression of endophilin isoforms in developing follicles.

Receptor-mediated endocytosis of yolk precursors via clathrin-coated structures is the key mechanism underlying rapid chicken oocyte growth. In defining oocyte-specific components of clathrin-mediated events, we have to date identified oocyte-specific yolk transport receptors, but little is known about the oocytes' supporting endocytic machinery. Important proteins implicated in clathrin-mediated endocytosis and recycling are the endophilins, which thus far have been studied primarily in synaptic vesicle formation; in the present study, as a different highly active endocytic system, we exploit rapidly growing chicken oocytes.