Steven C. Hauser

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We have studied in rat liver the subcellular sites and topography of xylosylation and galactosylation reactions occurring in the biosynthesis of the D-glucuronic acid-galactose-galactose-D-xylose linkage region of proteoglycans and of glucuronosylation reactions involved in both glycosaminoglycan biosynthesis and bile acid and bilirubin conjugation. The(More)
We have investigated the subcellular location and regulation of hepatic bilirubin UDP-glucuronyltransferase, which has been presumed to be located largely in the smooth endoplasmic reticulum. Purity of subcellular membrane fractions isolated from rat liver was assessed by electron microscopy and marker enzymes. Bilirubin UDP-glucuronyltransferase activity(More)
Hepatic glucuronidation of a wide variety of substrates is catalyzed by the membrane-bound UDP-glucuronosyltransferases. Uridine 5'-diphosphoglucuronic acid (UDP-GlcUA) is the essential cosubstrate for all UDP-glucuronosyltransferase-mediated reactions. The mechanism by which this bulky, hydrophilic nucleotide-sugar is transported from the cytosol (where it(More)
Distinguishing an object's compliance, into percepts of "softness" and "hardness," is crucial to our ability to grasp and manipulate it. Biomechanical cues at the skin's surface such as contact area and force rate have been thought to help encode compliance. However, no one has directly measured contact area with compliant materials, and few studies have(More)
To determine whether liver alkaline phosphatase (AP) reaches the circulation by crossing the space of Dissé and traversing lymphatic channels to the thoracic duct, AP was measured in lymph and serum hourly for 12 h after bile duct ligation in thoracic duct cannulated rats. AP did not rise at any time point in lymph, was markedly increased in serum by 7 h(More)
Cytosolic uridine 5'-diphosphoglucuronic acid is the essential cosubstrate for all hepatic microsomal UDP-glucuronosyltransferase-mediated reactions. Uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc) has been implicated as an activator of UDP-glucuronosyltransferases in vivo, acting either as an allosteric effector or by enhancing access of uridine(More)