Linked Life Data

9245751

Source:http://linkedlifedata.com/resource/pubmed/id/9245751

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-9-17
pubmed:abstractText
Most studies on the interaction of collagen with proteoglycans, two universal components of connective tissues, use technical approaches which substantially modify the shape and size of the proteoglycans themselves. In the present study unfixed, untreated collagen fibrils from rat tail tendon were dehydrated and observed by tapping-mode atomic force microscopy. The surface of collagen fibrils immediately reveals a periodic alternation of gap and overlap zones. A thin, transverse ridge decorates the gap zone, while other filamentous structures run on the fibril surface, either parallel or perpendicular to the fibril axis. These surface structures are much enhanced by Cupromeronic Blue preincubation, while pretreatment with chondroitinase ABC removes them completely, leaving barely detectable transverse ridges. The ridge and filaments are likely to represent, respectively, the core protein and the glycosaminoglycan side chains of proteoglycans, displayed with a far better resolution than with conventional histochemical or immunohistochemical techniques. Our data suggest that proteoglycan molecules are capable of different, multiple interactions with the collagen fibril surface as well as with each other.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1047-8477
pubmed:author
pubmed:issnType
Print
pubmed:volume
119
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
118-22
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Direct visualization of collagen-bound proteoglycans by tapping-mode atomic force microscopy.
pubmed:affiliation
Electron Microscopy Laboratory, Institute of Human Anatomy, Bologna, Italy.
pubmed:publicationType
Journal Article