Linked Life Data

7686157

Source:http://linkedlifedata.com/resource/pubmed/id/7686157

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1993-7-27
pubmed:databankReference
pubmed:abstractText
We have previously identified and purified transforming growth factor-beta 1 (TGF-beta 1)-binding proteins from porcine uterus membranes (Ichijo, H., Rönnstrand, L., Miyagawa, K., Ohashi, H., Heldin, C.-H., and Miyazono, K. (1991) J. Biol. Chem. 266, 22459-22464). One of these TGF-beta 1-binding proteins, with a molecular weight of 40,000, was purified to homogeneity and subjected to amino acid sequence analysis. The amino acid sequences obtained were used to isolate two closely related cDNA clones from a porcine uterus cDNA library. The deduced amino acid sequences revealed that both cDNAs encoded proteins that were mainly composed of fibrinogen-like and collagen-like domains. Therefore, they were denoted ficolin-alpha and ficolin-beta. Expression of ficolin-alpha and -beta cDNA in mammalian cells revealed that ficolin forms dimers, trimers, and several higher order of oligomers, whose molecular weights fit well with those of the purified TGF-beta 1-binding proteins from porcine uterus. Moreover, immunoblotting analysis using a peptide anti-serum against ficolin indicated that the TGF-beta 1-binding proteins identified in porcine uterus are ficolin-alpha, -beta, and their oligomers or closely related molecules. However, recombinant ficolin-alpha and -beta did not bind TGF-beta 1, despite the similarities in molecular weights and immunoreactivity with the material from the natural source. It is possible that a specific posttranslational modification of ficolin or interaction with another component is needed for TGF-beta 1 binding. Analysis by Northern blotting revealed that the expression of ficolin-alpha mRNA is relatively restricted and most abundant in placenta and lung. On the other hand, ficolin-beta was mainly expressed in skeletal muscle. The in vivo functions of ficolin will be discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14505-13
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7686157-Amino Acid Sequence, pubmed-meshheading:7686157-Animals, pubmed-meshheading:7686157-Base Sequence, pubmed-meshheading:7686157-Blotting, Northern, pubmed-meshheading:7686157-Carrier Proteins, pubmed-meshheading:7686157-Chromatography, Affinity, pubmed-meshheading:7686157-Cloning, Molecular, pubmed-meshheading:7686157-Collagen, pubmed-meshheading:7686157-DNA, pubmed-meshheading:7686157-Female, pubmed-meshheading:7686157-Fibrinogen, pubmed-meshheading:7686157-Gene Expression, pubmed-meshheading:7686157-Gene Library, pubmed-meshheading:7686157-Humans, pubmed-meshheading:7686157-Lectins, pubmed-meshheading:7686157-Macromolecular Substances, pubmed-meshheading:7686157-Molecular Sequence Data, pubmed-meshheading:7686157-Molecular Weight, pubmed-meshheading:7686157-Peptide Fragments, pubmed-meshheading:7686157-Poly A, pubmed-meshheading:7686157-RNA, pubmed-meshheading:7686157-RNA, Messenger, pubmed-meshheading:7686157-Sequence Homology, Amino Acid, pubmed-meshheading:7686157-Swine, pubmed-meshheading:7686157-Transfection, pubmed-meshheading:7686157-Transforming Growth Factor beta, pubmed-meshheading:7686157-Uterus
pubmed:year
1993
pubmed:articleTitle
Molecular cloning and characterization of ficolin, a multimeric protein with fibrinogen- and collagen-like domains.
pubmed:affiliation
Ludwig Institute for Cancer Research, Uppsala, Sweden.
pubmed:publicationType
Journal Article, Comparative Study