Connexin 57 is expressed by the axon terminal network of B-type horizontal cells in the rabbit retina.

In the rabbit retina there are two types of horizontal cell (HC). A-type HCs (AHC) are axonless and extensively coupled via connexin (Cx)50 gap junctions. The B-type HC (BHC) is axon-bearing; the somatic dendrites form a second network coupled by gap junctions while the axon terminals (ATs) form a third independent network in the outer plexiform layer (OPL).

Processing and presentation of a mycobacterial antigen 85B epitope by murine macrophages is dependent on the phagosomal acquisition of vacuolar proton ATPase and in situ activation of cathepsin D.

Mycobacterium tuberculosis (strain H37Rv) and bacillus Calmette-Guérin (BCG) vaccine inhibit phagosome maturation in macrophages and their effect on processing, and presentation of a secreted Ag85 complex B protein, Ag85B, by mouse macrophages was analyzed. Macrophages were infected with GFP-expressing mycobacterial strains and analyzed for in situ localization of vacuolar proton ATPase (v-ATPase) and cathepsin D (Cat D) using Western blot analysis and immunofluorescence. H37Rv and BCG phagosomes excluded the v-ATPase and maintained neutral pH while the attenuated H37Ra strain acquired v-ATPase and acidified.

Localization of the transmembrane proteoglycan syndecan-4 and its regulatory kinases in costameres of rat cardiomyocytes: a deconvolution microscopic study.

Syndecan-4 (syn-4), a transmembrane heparan sulfate-containing proteoglycan, is unique among the four members of the syndecan family in its specific cellular localization to complex cytoskeletal adhesion sites, i.e., focal adhesions.

Heparan sulfate abnormalities in exostosis growth plates.

Hereditary multiple exostoses (HME), a condition associated with development and growth of bony exostoses at the ends of the long bones, is caused by germline mutations in the EXT genes. EXT1 and EXT2 function as glycosyltransferases that participate in the biosynthesis of heparan sulfate (HS) to modify proteoglycans. HS proteoglycans, synthesized by chondrocytes and secreted to the extracellular matrix of the growth plate, play critical roles in growth plate signaling and remodeling.

Role of three FKHR phosphorylation sites in insulin inhibition of FKHR action in hepatocytes.

Insulin inhibits insulin-like growth factor binding protein-1 (IGFBP-1) transcription by preventing FKHR protein family members from binding a specific insulin response element in the IGFBP-1 promoter. In most cells, three serine/threonine moieties in FKHR family members are phosphorylated after insulin treatment or protein kinase B/Akt (PKB) transfection, and each of the three phosphorylated PKB sites contributes to insulin- or PKB-mediated inhibition of both the action and the nuclear localization of FKHR family members. In hepatocytes, however, the middle PKB site (PKB2) of FKHR was required for insulin to phosphorylate FKHR and was the only PKB site that participated in insulin inhibition of FKHR action, indicating that insulin utilizes a unique pathway to regulate FKHR action in hepatocytes.