Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.6.1 (sulfatase)
 3,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Steroid sulfatase activity was quantified in liver microsomes from hypophysectomized adult female rats treated with estradiol and continuous or intermittent human growth hormone (hGH). Hypophysectomy clearly enhanced sulfatase activity as compared to intact female rats. Normal female values were completely restored by continuous infusion of hGH (1.4 i.u./kg/day). Neither the same dose of hGH given as two daily injections nor estrogen replacement therapy had any effect. It is concluded that liver microsome sulfatase activity in the non-pregnant rat is regulated by the sexually dimorphic secretory pattern of GH.
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PMID:Secretory pattern of growth hormone regulates steroid sulfatase activity in rat liver. 277 33

It is now well established that the activity of certain liver enzymes displays sex differences and that administration of human growth hormone to male rats alters the liver metabolism in a "female" direction. In this work we studied steroid sulfatase activity and binding of estradiol-17 beta in livers from intact rats and found a sex difference, with considerably higher enzyme activity in male as compared to female liver tissue. Continuous infusion of native and recombinant human growth hormone and estradiol-17 beta to male rats reduced sulfatase activity to "female" levels. A specific binding of estradiol-17 beta with receptor properties was found in the rat livers, but the concentration of binding sites did not change after administration of growth hormone or estradiol in this group of intact animals. Our data confirm previous reports that continuous administration of human growth hormone "feminize" liver metabolism, and since estradiol was found to have an identical effect on sulfatase activity it is suggested that the effect of estradiol-17 beta in this respect may be indirect, mediated via an altered secretory pattern of rat growth hormone.
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PMID:Effects of estrogen and growth hormone on steroid sulfatase activity and estrogen binding in rat liver. 296 75

Non-autologous somatic gene therapy is an alternate approach to delivering recombinant gene products through implantation of a "universal" donor cell line engineered to produce a therapeutic gene product. The cells are immunologically isolated by enclosure in immunoprotective microcapsules fabricated from alginate-poly-L-lysine-alginate. The molecular weight cutoff of these microcapsules was thought to be <100 kd, thus, excluding the immunoglobulins. However, when such microcapsules are fabricated to enclose cells, they show a higher permeability threshold than expected. The secretion rates of recombinant gene products ranging from 21 through 150 to 300 kd (human growth hormone, rat serum albumin, human arylsulfatase A, human immunoglobulin, mouse beta-hexosaminidase, mouse beta-glucuronidase) were similar between the nonencapsulated and encapsulated recombinant cells with the exception of the largest molecular species, the 300-kd beta-glucuronidase. Its secretion was reduced about eightfold after encapsulation. Increasing the thickness of the membrane by prolonging the coating time with poly-L-lysine did not provide a lower molecular weight cutoff. An additional coating with alginate, however, reduced the leakage of the larger molecular species, but the effect was short lived: After 2 weeks in culture, the double- and single-coated microcapsules were equally permeable. Both the increased poly-L-lysine and alginate coating were detrimental to the long-term viability and proliferation of the encapsulated cells. Hence, immunoisolation of encapsulated cells with alginate-poly-L-lysine-alginate microcapsules cannot provide a molecular weight cutoff below 300 kd. (c) 1996 John Wiley & Sons, Inc.
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PMID:Permeability of alginate microcapsules to secretory recombinant gene products. 1862 20