Functional analysis of chick heparan sulfate 6-O-sulfotransferases in limb bud development.

Heparan sulfate (HS) interacts with numerous growth factors, morphogens, receptors, and extracellular matrix proteins. Disruption of HS synthetic enzymes causes perturbation of growth factor signaling and malformation in vertebrate and invertebrate development. Our previous studies show that the O-sulfation patterns of HS are essential for the specific binding of growth factors to HS chains, and that depletion of O-sulfotransferases results in remarkable developmental defects in Drosophila, zebrafish, chick, and mouse.

Home traction in the treatment schedule of overhead traction for developmental dysplasia of the hip.

Background: Our department introduced an overhead traction method (OHT) into the treatment protocol for developmental dysplasia of the hip (DDH) in 1964. With our method, a minimum of 6 weeks of hospitalization was necessary, and the burden for the patients and their families was significant. Since 1998, we have employed home traction into the OHT protocol to shorten the duration of hospitalization.

Distinctive expression patterns of heparan sulfate O-sulfotransferases and regional differences in heparan sulfate structure in chick limb buds.

The skeletal tissue development and patterning in chick limb buds are known to be under the spacio-temporal control of various heparin-binding cell growth factors such as fibroblast growth factors and bone morphogenetic proteins. Different structural regions on heparan sulfate (HS) chains of proteoglycans could be implicated in regional differences in the binding capacities of these cell growth factors, by which they could selectively interact with targeted cells and regulate their signaling in those processes. In this study we first demonstrated by cDNA cloning that one heparan sulfate 2-O-sulfotransferase (HS2ST) and two isoforms of heparan sulfate 6-O-sulfotransferase (HS6ST-1 and -2) occurred in chick embryos and had different substrate specificities each other.

Biosynthesis of heparan sulphate with diverse structures and functions: two alternatively spliced forms of human heparan sulphate 6-O-sulphotransferase-2 having different expression patterns and properties.

Heparan sulphate 6- O -sulphotransferase (HS6ST) catalyses the transfer of sulphate from adenosine 3'-phosphate, 5'-phosphosulphate to the 6th position of the N -sulphoglucosamine residue in HS. We previously described the occurrence of three isoforms of mouse HS6ST, mHS6ST-1, -2, and -3 [Habuchi, Tanaka, Habuchi, Yoshida, Suzuki, Ban and Kimata (2000) J. Biol.