Linked Life Data

19903549

Source:http://linkedlifedata.com/resource/pubmed/id/19903549

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2009-11-11
pubmed:abstractText
To shed light on the mechanism underlying the active morphogenesis of living cells in relation to the organization of internal cytoskeletal networks, the development of new methodologies to construct artificial cell models is crucial. Here, we describe the successful construction of cell-sized liposomes entrapping cytoskeletal proteins. We discuss experimental protocols to prepare giant liposomes encapsulating desired amounts of actin and cross-linking proteins including molecular motor proteins, such as fascin, alpha-actinin, filamin, myosin-I isolated from brush border (BBMI), and heavy meromyosin (HMM). Subfragment 1 (S-1) is also studied in comparison to HMM, where S-1 and HMM are single-headed and double-headed derivatives of conventional myosin (myosin-II), respectively. In the absence of cross-linking proteins, actin filaments (F-actin) are distributed homogeneously without any order within the liposomes. In contrast, when actin is encapsulated together with an actin-cross-linking protein, mesh structures emerge that are similar to those in living motile cells. Optical microscopic observations on the active morphological changes of the liposomes are reported.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1557-7988
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
464
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31-53
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Chapter 3 - Construction of cell-sized liposomes encapsulating actin and actin-cross-linking proteins.
pubmed:affiliation
Division of Biological Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't