Linked Life Data

8179615

Source:http://linkedlifedata.com/resource/pubmed/id/8179615

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-6-3
pubmed:abstractText
A naturally occurring splice variant of hepatocyte growth factor (HGF) lacks a 5-amino acid sequence in the first kringle domain. Comparison of HGF and the deletion variant (dHGF) revealed that the deletion significantly altered the biological activities, solubility, and immunological property of HGF. HGF was respectively about 20-, 10-, and 2-fold more potent than dHGF in the stimulation of DNA synthesis in human umbilical vein endothelial cells, human aorta smooth muscle cells, and NSF-60 (murine myeloblastic cells). Conversely, dHGF was respectively about 3-, 2-, and 2-fold more potent than HGF in the stimulation of DNA synthesis in LLC-PK1 (pig kidney epithelial cells), OK (American opossum kidney epithelial cells), and rat hepatocytes. Moreover, HGF was over 70-fold more soluble than dHGF in PBS. Several monoclonal antibodies raised against dHGF recognized only dHGF and neither HGF nor reduced dHGF, demonstrating that the deletion caused a tertiary structural change. The structural change in HGF may be responsible for its altered biological activities and solubility.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
200
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
808-15
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Hepatocyte growth factor and its variant with a deletion of five amino acids are distinguishable in their biological activity and tertiary structure.
pubmed:affiliation
Research Institute of Life Science, Snow Brand Milk Products, Co., Ltd., Tochigi, Japan.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro