Linked Life Data

8557636

Source:http://linkedlifedata.com/resource/pubmed/id/8557636

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-2-26
pubmed:databankReference
pubmed:abstractText
Together with the 31-kDa microfibril-associated glycoprotein (MAGP), four polypeptides designated MP340 (340 kDa), MP78 (78 kDa), MP70 (70 kDa), and MP25 (25 kDa) have previously been identified in tissue extracts designed specifically to solubilize the microfibrillar component of elastic fibers. In the present study, both MP78 and MP70 were shown to be forms of a protein which is closely related to the human protein beta ig-h3, and MP340 was confirmed to be the bovine form of fibrillin-1. Peptide sequences from MP25 proved to be unique, and affinity-purified anti-MP25 antibodies were shown, by immunofluorescence and immunoelectron microscopy, to localize specifically to the elastin-associated microfibrils. This confirmed that MP25 was a distinct component of these structures. Expression screening of nuchal ligament cDNA libraries yielded a cDNA, cM10A (770 base pairs) which encodes amino acid sequences matching those of the MP25 peptides. Further library screening with cM10A identified cDNAs which encode the complete primary structures of bovine and human MP25. Bovine and human MP25 were found to be around 80% homologous and contain 170 and 173 amino acids, respectively. Data base searches revealed that MP25 had significant similarity of structure only with MAGP, indicating that the two proteins form a new family of microfibrillar proteins. In acknowledgment, MP25 has been formally renamed MAGP-2, and MAGP is referred to as MAGP-1. The close similarity between the two proteins (57%) is confined to a central region of 60 amino acids where there is precise alignment of 7 cysteine residues. Elsewhere the MAGP-2 molecule is rich in serine and threonine residues and contains an RGD motif. MAGP-2 lacks the proline-, glutamine-, and tyrosine-rich sequences and a hydrophobic carboxyl terminus, characteristic of MAGP-1. These structural differences suggest that MAGP-2 has some functions which are distinct from those of MAGP-1. The locus of the human MAGP-2 gene was identified on chromosome 12 in the region of 12p12.3-12p13.1.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1096-103
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8557636-Amino Acid Sequence, pubmed-meshheading:8557636-Animals, pubmed-meshheading:8557636-Base Sequence, pubmed-meshheading:8557636-Cattle, pubmed-meshheading:8557636-Chromosome Mapping, pubmed-meshheading:8557636-Chromosomes, Human, Pair 12, pubmed-meshheading:8557636-Cloning, Molecular, pubmed-meshheading:8557636-Elastic Tissue, pubmed-meshheading:8557636-Extracellular Matrix Proteins, pubmed-meshheading:8557636-Female, pubmed-meshheading:8557636-Glycoproteins, pubmed-meshheading:8557636-Humans, pubmed-meshheading:8557636-Microfilament Proteins, pubmed-meshheading:8557636-Molecular Sequence Data, pubmed-meshheading:8557636-Neoplasm Proteins, pubmed-meshheading:8557636-Pregnancy, pubmed-meshheading:8557636-Sequence Alignment, pubmed-meshheading:8557636-Sequence Analysis, pubmed-meshheading:8557636-Transforming Growth Factor beta
pubmed:year
1996
pubmed:articleTitle
Further characterization of proteins associated with elastic fiber microfibrils including the molecular cloning of MAGP-2 (MP25)
pubmed:affiliation
Department of Pathology, University of Adelaide, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't