| pubmed-article:1919574 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1919574 | lifeskim:mentions | umls-concept:C0007427 | lld:lifeskim |
| pubmed-article:1919574 | lifeskim:mentions | umls-concept:C0041348 | lld:lifeskim |
| pubmed-article:1919574 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:1919574 | lifeskim:mentions | umls-concept:C0024773 | lld:lifeskim |
| pubmed-article:1919574 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:1919574 | pubmed:dateCreated | 1991-11-15 | lld:pubmed |
| pubmed-article:1919574 | pubmed:abstractText | The in vitro degradation of microtubule-associated protein 2 (MAP-2) and tubulin by the lysosomal aspartyl endopeptidase cathepsin D was studied. MAP-2 was very sensitive to cathepsin D-induced hydrolysis in a relatively broad, acidic pH range (3.0-5.0). However, at a pH value of 5.5, cathepsin D-mediated hydrolysis of MAP-2 was significantly reduced and at pH 6.0 only a small amount of MAP-2 was degraded at 60 min. Interestingly, the two electrophoretic forms of MAP-2 showed different sensitivities to cathepsin D-induced degradation, with MAP-2b being significantly more resistant to hydrolysis than MAP-2a. To our knowledge, this is the first clear demonstration that MAP-2 is a substrate in vitro for cathepsin D. In contrast to MAP-2, tubulin was relatively resistant to cathepsin D-induced hydrolysis. At pH 3.5 and an enzyme-to-substrate ratio of 1: 20, only 35% of the tubulin was degraded by cathepsin D at 60 min. The cathepsin D-mediated hydrolysis of tubulin was optimal only at pH 4.5. These results demonstrate that MAP-2 and tubulin are unequally susceptible to degradation by cathepsin D. These data also imply a potential for rapid degradation of MAP-2 in vivo by cathepsin D either in lysosomes or perhaps autophagic vacuoles of the neuron. | lld:pubmed |
| pubmed-article:1919574 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1919574 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1919574 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1919574 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1919574 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1919574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1919574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1919574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1919574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1919574 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1919574 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:1919574 | pubmed:issn | 0022-3042 | lld:pubmed |
| pubmed-article:1919574 | pubmed:author | pubmed-author:WhitakerJ NJN | lld:pubmed |
| pubmed-article:1919574 | pubmed:author | pubmed-author:JohnsonG VGV | lld:pubmed |
| pubmed-article:1919574 | pubmed:author | pubmed-author:LiterskyJ MJM | lld:pubmed |
| pubmed-article:1919574 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1919574 | pubmed:volume | 57 | lld:pubmed |
| pubmed-article:1919574 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1919574 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1919574 | pubmed:pagination | 1577-83 | lld:pubmed |
| pubmed-article:1919574 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1919574 | pubmed:meshHeading | pubmed-meshheading:1919574-... | lld:pubmed |
| pubmed-article:1919574 | pubmed:meshHeading | pubmed-meshheading:1919574-... | lld:pubmed |
| pubmed-article:1919574 | pubmed:meshHeading | pubmed-meshheading:1919574-... | lld:pubmed |
| pubmed-article:1919574 | pubmed:meshHeading | pubmed-meshheading:1919574-... | lld:pubmed |
| pubmed-article:1919574 | pubmed:meshHeading | pubmed-meshheading:1919574-... | lld:pubmed |
| pubmed-article:1919574 | pubmed:meshHeading | pubmed-meshheading:1919574-... | lld:pubmed |
| pubmed-article:1919574 | pubmed:meshHeading | pubmed-meshheading:1919574-... | lld:pubmed |
| pubmed-article:1919574 | pubmed:meshHeading | pubmed-meshheading:1919574-... | lld:pubmed |
| pubmed-article:1919574 | pubmed:meshHeading | pubmed-meshheading:1919574-... | lld:pubmed |
| pubmed-article:1919574 | pubmed:meshHeading | pubmed-meshheading:1919574-... | lld:pubmed |
| pubmed-article:1919574 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1919574 | pubmed:articleTitle | Proteolysis of microtubule-associated protein 2 and tubulin by cathepsin D. | lld:pubmed |
| pubmed-article:1919574 | pubmed:affiliation | Department of Neurology, University of Alabama, Birmingham 35294. | lld:pubmed |
| pubmed-article:1919574 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1919574 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1919574 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:1919574 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1919574 | lld:pubmed |
