pubmed-article:9195213 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9195213 | lifeskim:mentions | umls-concept:C0017296 | lld:lifeskim |
pubmed-article:9195213 | lifeskim:mentions | umls-concept:C0025517 | lld:lifeskim |
pubmed-article:9195213 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
pubmed-article:9195213 | lifeskim:mentions | umls-concept:C0439660 | lld:lifeskim |
pubmed-article:9195213 | lifeskim:mentions | umls-concept:C0022567 | lld:lifeskim |
pubmed-article:9195213 | lifeskim:mentions | umls-concept:C0268124 | lld:lifeskim |
pubmed-article:9195213 | lifeskim:mentions | umls-concept:C0449445 | lld:lifeskim |
pubmed-article:9195213 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:9195213 | pubmed:dateCreated | 1997-8-6 | lld:pubmed |
pubmed-article:9195213 | pubmed:abstractText | Disorders in which there is toxic buildup of circulating substrate may be treated by furnishing an enzyme reservoir capable of metabolically processing the excess substrate. The epidermal keratinocyte is a potential site for such a reservoir. In this study, we explore the capacity of genetically modified keratinocytes to metabolize extracellular substrate in a culture model that resembles in vivo epidermal architecture. Keratinocytes from adenosine deaminase (ADA)-deficient patients were transduced with a retroviral vector encoding the human ADA gene and the capacity of this tissue to deaminate deoxyadenosine (dAdo) in vitro was measured. The results show that at a substrate concentration of 10 microM, ADA-corrected keratinocytes deaminate dAdo at a rate of 0.38 nmol/min.10(6) cells. These results indicate that keratinocytes process extracellular substrate at rates that suggest complete substrate conversion in a single pass. This study provides a strong indication that the epidermis, the largest and most accessible tissue of the body, is a valuable site for designing clinically relevant gene therapies. | lld:pubmed |
pubmed-article:9195213 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9195213 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9195213 | pubmed:language | eng | lld:pubmed |
pubmed-article:9195213 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9195213 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9195213 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9195213 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9195213 | pubmed:month | May | lld:pubmed |
pubmed-article:9195213 | pubmed:issn | 1043-0342 | lld:pubmed |
pubmed-article:9195213 | pubmed:author | pubmed-author:BlaeseR MRM | lld:pubmed |
pubmed-article:9195213 | pubmed:author | pubmed-author:SchwartzP MPM | lld:pubmed |
pubmed-article:9195213 | pubmed:author | pubmed-author:TaichmanL BLB | lld:pubmed |
pubmed-article:9195213 | pubmed:author | pubmed-author:FenjvesE SES | lld:pubmed |
pubmed-article:9195213 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9195213 | pubmed:day | 20 | lld:pubmed |
pubmed-article:9195213 | pubmed:volume | 8 | lld:pubmed |
pubmed-article:9195213 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9195213 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9195213 | pubmed:pagination | 911-7 | lld:pubmed |
pubmed-article:9195213 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:9195213 | pubmed:meshHeading | pubmed-meshheading:9195213-... | lld:pubmed |
pubmed-article:9195213 | pubmed:meshHeading | pubmed-meshheading:9195213-... | lld:pubmed |
pubmed-article:9195213 | pubmed:meshHeading | pubmed-meshheading:9195213-... | lld:pubmed |
pubmed-article:9195213 | pubmed:meshHeading | pubmed-meshheading:9195213-... | lld:pubmed |
pubmed-article:9195213 | pubmed:meshHeading | pubmed-meshheading:9195213-... | lld:pubmed |
pubmed-article:9195213 | pubmed:meshHeading | pubmed-meshheading:9195213-... | lld:pubmed |
pubmed-article:9195213 | pubmed:meshHeading | pubmed-meshheading:9195213-... | lld:pubmed |
pubmed-article:9195213 | pubmed:meshHeading | pubmed-meshheading:9195213-... | lld:pubmed |
pubmed-article:9195213 | pubmed:meshHeading | pubmed-meshheading:9195213-... | lld:pubmed |
pubmed-article:9195213 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9195213 | pubmed:articleTitle | Keratinocyte gene therapy for adenosine deaminase deficiency: a model approach for inherited metabolic disorders. | lld:pubmed |
pubmed-article:9195213 | pubmed:affiliation | Department of Oral Biology and Pathology, State University of New York at Stony Brook 11794, USA. | lld:pubmed |
pubmed-article:9195213 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9195213 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9195213 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9195213 | lld:pubmed |