| pubmed-article:8902191 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8902191 | lifeskim:mentions | umls-concept:C1123023 | lld:lifeskim |
| pubmed-article:8902191 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
| pubmed-article:8902191 | lifeskim:mentions | umls-concept:C0031603 | lld:lifeskim |
| pubmed-article:8902191 | lifeskim:mentions | umls-concept:C0026697 | lld:lifeskim |
| pubmed-article:8902191 | lifeskim:mentions | umls-concept:C1155437 | lld:lifeskim |
| pubmed-article:8902191 | lifeskim:mentions | umls-concept:C0243144 | lld:lifeskim |
| pubmed-article:8902191 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
| pubmed-article:8902191 | lifeskim:mentions | umls-concept:C0205266 | lld:lifeskim |
| pubmed-article:8902191 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8902191 | pubmed:dateCreated | 1997-2-28 | lld:pubmed |
| pubmed-article:8902191 | pubmed:abstractText | Mucolipidosis type 4 (ML-4) is an autosomal recessive inborn error of metabolism, the pathogenesis of which is not known. We characterized protein kinase C (PKC) activation and cellular phosphate uptake in intact quiescent ML-4 skin fibroblasts and after stimulation with phorbol myristate acetate (PMA). [3H]Phorbol dibutyrate uptake was not altered in ML-4 compared to control cells. Translocation of PKC from the cytosolic to the membranous compartment upon stimulation with PMA was perturbed in ML-4 cells. Phosphate uptake was reduced in both cytosolic and membranous fractions of quiescent ML-4 cells. Stimulation with PMA did not elicit an increase in phosphate uptake in the cytosolic fraction of ML-4 cells compared with control cells, but led to comparable phosphate uptake in the membranous fraction of both cell types. The data indicate that PKC-mediated signal transduction may be perturbed in ML-4. Other kinases and phosphatases may be involved. These alterations may play an important role in the pathogenesis of this disorder. | lld:pubmed |
| pubmed-article:8902191 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8902191 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8902191 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8902191 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8902191 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8902191 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8902191 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8902191 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8902191 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:8902191 | pubmed:issn | 1077-3150 | lld:pubmed |
| pubmed-article:8902191 | pubmed:author | pubmed-author:BonehAA | lld:pubmed |
| pubmed-article:8902191 | pubmed:author | pubmed-author:TurgemanDD | lld:pubmed |
| pubmed-article:8902191 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8902191 | pubmed:volume | 59 | lld:pubmed |
| pubmed-article:8902191 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8902191 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8902191 | pubmed:pagination | 33-7 | lld:pubmed |
| pubmed-article:8902191 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:8902191 | pubmed:meshHeading | pubmed-meshheading:8902191-... | lld:pubmed |
| pubmed-article:8902191 | pubmed:meshHeading | pubmed-meshheading:8902191-... | lld:pubmed |
| pubmed-article:8902191 | pubmed:meshHeading | pubmed-meshheading:8902191-... | lld:pubmed |
| pubmed-article:8902191 | pubmed:meshHeading | pubmed-meshheading:8902191-... | lld:pubmed |
| pubmed-article:8902191 | pubmed:meshHeading | pubmed-meshheading:8902191-... | lld:pubmed |
| pubmed-article:8902191 | pubmed:meshHeading | pubmed-meshheading:8902191-... | lld:pubmed |
| pubmed-article:8902191 | pubmed:meshHeading | pubmed-meshheading:8902191-... | lld:pubmed |
| pubmed-article:8902191 | pubmed:meshHeading | pubmed-meshheading:8902191-... | lld:pubmed |
| pubmed-article:8902191 | pubmed:meshHeading | pubmed-meshheading:8902191-... | lld:pubmed |
| pubmed-article:8902191 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8902191 | pubmed:articleTitle | Protein kinase C activation and phosphate uptake are altered in intact mucolipidosis type-4 skin fibroblasts. | lld:pubmed |
| pubmed-article:8902191 | pubmed:affiliation | Department of Paediatrics, Hadassah University Hospital, Mt. Scopus, Jerusalem, Israel. | lld:pubmed |
| pubmed-article:8902191 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8902191 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8902191 | lld:pubmed |
