Linked Life Data

17516569

Source:http://linkedlifedata.com/resource/pubmed/id/17516569

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-6-4
pubmed:abstractText
Hydroxylysine and its glycosylated forms, galactosylhydroxylysine and glucosylgalactosylhydroxylysine, are post-translational modifications unique to collagenous sequences. They are found in collagens and in many proteins having a collagenous domain in their structure. Since the last published reviews, significant new data have accumulated regarding these modifications. One of the lysyl hydroxylase isoforms, lysyl hydroxylase 3 (LH3), has been shown to possess three catalytic activities required sequentially to produce hydroxylysine and its glycosylated forms, that is, the lysyl hydroxylase (LH), galactosyltransferase (GT), and glucosyltransferase (GGT) activities. Studies on mouse models have revealed the importance of these different activities of LH3 in vivo. LH3 is the main molecule responsible for GGT activity in mouse embryos. A lack of this activity causes intracellular accumulation of type IV collagen, which disrupts the formation of basement membranes (BMs) during mouse embryogenesis and leads to embryonic lethality. The specific inactivation of the LH activity of LH3 causes minor alterations in the structure of the BM and collagen fibril organization, but does not affect the lifespan of mutated mice. Recent data from zebrafish demonstrate that growth cone migration depends critically on the LH3 glycosyltransferase domain. LH3 is located in the ER loosely associated with the membranes, but, unlike the other isoforms, LH3 is also found in the extracellular space in some tissues. LH3 is able to adjust the amount of hydroxylysine and hydroxylysine-linked carbohydrates of extracellular proteins in their native conformation, suggesting that it may have a role in matrix remodeling.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9541
pubmed:author
pubmed:issnType
Print
pubmed:volume
212
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
323-9
pubmed:meshHeading
pubmed-meshheading:17516569-Amino Acid Sequence, pubmed-meshheading:17516569-Animals, pubmed-meshheading:17516569-Basement Membrane, pubmed-meshheading:17516569-Catalytic Domain, pubmed-meshheading:17516569-Collagen, pubmed-meshheading:17516569-Embryonic Development, pubmed-meshheading:17516569-Endoplasmic Reticulum, pubmed-meshheading:17516569-Extracellular Space, pubmed-meshheading:17516569-Galactosyltransferases, pubmed-meshheading:17516569-Glucosyltransferases, pubmed-meshheading:17516569-Glycosylation, pubmed-meshheading:17516569-Humans, pubmed-meshheading:17516569-Hydroxylysine, pubmed-meshheading:17516569-Mice, pubmed-meshheading:17516569-Molecular Sequence Data, pubmed-meshheading:17516569-Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase, pubmed-meshheading:17516569-Protein Processing, Post-Translational, pubmed-meshheading:17516569-Sequence Homology, Amino Acid, pubmed-meshheading:17516569-Substrate Specificity
pubmed:year
2007
pubmed:articleTitle
Expanding the lysyl hydroxylase toolbox: new insights into the localization and activities of lysyl hydroxylase 3 (LH3).
pubmed:affiliation
Department of Biochemistry, Biocenter Oulu, University of Oulu, Finland. raili.myllyla@oulu.fi
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't