| pubmed-article:3360762 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3360762 | lifeskim:mentions | umls-concept:C0242692 | lld:lifeskim |
| pubmed-article:3360762 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:3360762 | lifeskim:mentions | umls-concept:C1179121 | lld:lifeskim |
| pubmed-article:3360762 | lifeskim:mentions | umls-concept:C1552961 | lld:lifeskim |
| pubmed-article:3360762 | lifeskim:mentions | umls-concept:C0005187 | lld:lifeskim |
| pubmed-article:3360762 | lifeskim:mentions | umls-concept:C0302167 | lld:lifeskim |
| pubmed-article:3360762 | lifeskim:mentions | umls-concept:C0444930 | lld:lifeskim |
| pubmed-article:3360762 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:3360762 | pubmed:dateCreated | 1988-6-9 | lld:pubmed |
| pubmed-article:3360762 | pubmed:abstractText | We examined the function of beta-actinin as a pointed end capping protein of thin filaments in skeletal muscle. An improvement in preparing beta-actinin yielded purified beta-actinin which retained its activity for more than a week. Two-dimensional gel electrophoresis showed that the two subunits, beta I and beta II, of beta-actinin are, respectively, split into two to three components (isoforms) with different isoelectric points. Polyclonal antibody was raised by injecting such purified and undenatured chicken breast muscle beta-actinin composed of several components into a rabbit. Immuno-gold labeling examination with electron microscopy of an F-actin-beta-actinin complex decorated with HMM showed that 85% of bound gold particles was on the pointed end of actin filaments, while the remaining 15% was on the barbed end. This suggests that in beta-actinin preparation pointed end and barbed end capping proteins inevitably coexist. Immunofluorescence and immunoelectron microscopy directly showed that beta-actinin is located at the pointed end of thin filaments in myofibrils; it was also suggested that a capping protein having common antigenic determinants to beta-actinin is located at Z-line. Thus, the physiological function of beta-actinin as a pointed end capping protein was examined as follows: When beta-actinin was dissociated from the pointed end of thin filaments in an I-Z-I brush by using a high salt solution, thin filaments could be disassembled at the pointed ends at concentrations of exogenous actin lower than a critical value. At a physiological ionic strength, these salt-washed thin filaments gradually shortened at a constant rate of about 45 nm/h. Both the association and dissociation of monomeric actin at the pointed end were suppressed by the rebinding of exogenous beta-actinin. The main physiological role of beta-actinin is therefore to stabilize thin filaments in the sarcomere by preventing addition and removal of actin monomers at the pointed filament end. | lld:pubmed |
| pubmed-article:3360762 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3360762 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3360762 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3360762 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3360762 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3360762 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3360762 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3360762 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:3360762 | pubmed:issn | 0021-924X | lld:pubmed |
| pubmed-article:3360762 | pubmed:author | pubmed-author:FunatsuTT | lld:pubmed |
| pubmed-article:3360762 | pubmed:author | pubmed-author:AsamiYY | lld:pubmed |
| pubmed-article:3360762 | pubmed:author | pubmed-author:IshiwataSS | lld:pubmed |
| pubmed-article:3360762 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3360762 | pubmed:volume | 103 | lld:pubmed |
| pubmed-article:3360762 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3360762 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3360762 | pubmed:pagination | 61-71 | lld:pubmed |
| pubmed-article:3360762 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:3360762 | pubmed:meshHeading | pubmed-meshheading:3360762-... | lld:pubmed |
| pubmed-article:3360762 | pubmed:meshHeading | pubmed-meshheading:3360762-... | lld:pubmed |
| pubmed-article:3360762 | pubmed:meshHeading | pubmed-meshheading:3360762-... | lld:pubmed |
| pubmed-article:3360762 | pubmed:meshHeading | pubmed-meshheading:3360762-... | lld:pubmed |
| pubmed-article:3360762 | pubmed:meshHeading | pubmed-meshheading:3360762-... | lld:pubmed |
| pubmed-article:3360762 | pubmed:meshHeading | pubmed-meshheading:3360762-... | lld:pubmed |
| pubmed-article:3360762 | pubmed:meshHeading | pubmed-meshheading:3360762-... | lld:pubmed |
| pubmed-article:3360762 | pubmed:meshHeading | pubmed-meshheading:3360762-... | lld:pubmed |
| pubmed-article:3360762 | pubmed:meshHeading | pubmed-meshheading:3360762-... | lld:pubmed |
| pubmed-article:3360762 | pubmed:meshHeading | pubmed-meshheading:3360762-... | lld:pubmed |
| pubmed-article:3360762 | pubmed:meshHeading | pubmed-meshheading:3360762-... | lld:pubmed |
| pubmed-article:3360762 | pubmed:meshHeading | pubmed-meshheading:3360762-... | lld:pubmed |
| pubmed-article:3360762 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3360762 | pubmed:articleTitle | Beta-actinin: a capping protein at the pointed end of thin filaments in skeletal muscle. | lld:pubmed |
| pubmed-article:3360762 | pubmed:affiliation | Department of Physics, School of Science and Engineering, Waseda University, Tokyo. | lld:pubmed |
| pubmed-article:3360762 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3360762 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3360762 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3360762 | lld:pubmed |
