Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2005-3-24
pubmed:abstractText
Tendon remodeling occurs in response to changes in loading and mobilization. Though the normal mechanical function depends on precise alignment of collagen fibrils, it is proteoglycans that regulate collagen fibrillogenesis and thus, indirectly, tendon function. In this paper we discuss the basic biochemical structure of several members of two proteoglycans families. Decorin, biglycan, fibromodulin and lumican, all members of the small leucine-rich proteoglycans family, bind to collagen fibrils and are active participants in fibrillogenesis. Aggrecan and versican, two members of large modular proteoglycans or lecticans, and their partner hyaluronan likely provide tendon tissues with a high capacity to resist high compressive and tensile forces associated with loading and mobilization. We present data from our laboratory showing that proteoglycans and glycosaminoglycan content increases not only with growth but also with loading of young avian gastrocnemius tendons. Specifically, an increase in the content of keratan sulfate, chondroitin sulfate and hyaluronan was observed. Moderate exercise for several weeks led not only to a further increase in total proteoglycans content but also to qualitative changes in proteoglycan make up.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1108-7161
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
22-34
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Tendon proteoglycans: biochemistry and function.
pubmed:affiliation
Virginia Bioinformatics Institute, Virginia Polytechnic Institute, Blacksburg, VA, USA.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't