Linked Life Data

8617343

Source:http://linkedlifedata.com/resource/pubmed/id/8617343

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-6-11
pubmed:abstractText
The interaction of Entamoeba histolytica trophozoites with collagen involves cell adherence, formation, and release of electron dense granules (EDGs) containing collagenase activity leading to the degradation of the bound protein. The binding is thought to be mediated by an "integrin-like" collagen receptor. Since the signal transduction mechanisms triggered by the collagen-trophozoite interaction are unknown, but clearly involve cytoskeletal organization, we decided to explore the role of protein tyrosine phosphorylation in this process. Collagen induces a time-dependent increase in the phosphorylation of several polypeptides migrating around 67 and 110 kDa. One polypeptide of the high-molecular-weight component was identified as a 125-kDa protein with very similar epitopes to the focal treatment was a 42-kDa polypeptide related to the mitogen activated protein kinase (MAPK) family. Our results suggest that tyrosine phosphorylation is involved in collagen signaling in amoebas and that pp125FAK and p42MAPK homologs may play an active role in turning on the genetic program that enables the parasite to invade its host.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-4894
pubmed:author
pubmed:issnType
Print
pubmed:volume
82
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
164-70
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Entamoeba histolytica: involvement of pp125FAK in collagen-induced signal transduction.
pubmed:affiliation
Departamento de Genética y Biología Molecular, CINVESTAV-IPN, Mexico DF, Mexico.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't