PMID- 10358019
OWN - NLM
STAT- MEDLINE
DCOM- 19990706
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 24
DP  - 1999 Jun 11
TI  - EMILIN, a component of the elastic fiber and a new member of the C1q/tumor
      necrosis factor superfamily of proteins.
PG  - 16773-81
AB  - EMILIN (elastin microfibril interface located protein) is an extracellular matrix
      glycoprotein abundantly expressed in elastin-rich tissues such as blood vessels, 
      skin, heart, and lung. It occurs associated with elastic fibers at the interface 
      between amorphous elastin and microfibrils. Avian EMILIN was extracted from
      19-day-old embryonic chick aortas and associated blood vessels and purified by
      ion-exchange chromatography and gel filtration. Tryptic peptides were generated
      from EMILIN and sequenced, and degenerate inosine-containing oligonucleotide
      primers were designed from some peptides. A set of primers allowed the
      amplification of a 360-base pair reverse transcription polymerase chain reaction 
      product from chick aorta mRNA. A probe based on a human homologue selected by
      comparison of the chick sequence with EST data base was used to select
      overlapping clones from both human aorta and kidney cDNA libraries. Here we
      present the cDNA sequence of the entire coding region of human EMILIN
      encompassing an open reading frame of 1016 amino acid residues. There was a high 
      degree of homology (76% identity and 88% similarity) between the chick C terminus
      and the human sequence as well as between the N terminus of the mature chick
      protein where 10 of 12 residues, as determined by N-terminal sequencing, were
      identical or similar to the deduced N terminus of human EMILIN. The domain
      organization of human EMILIN includes a C1q-like globular domain at the C
      terminus, a collagenous stalk, and a longer segment in which at least four heptad
      repeats and a leucine zipper can be identified with a high potential for forming 
      coiled-coil alpha helices. At the N terminus there is a cysteine-rich sequence
      stretch similar to a region of multimerin, a platelet and endothelial cell
      component, containing a partial epidermal growth factor-like motif. The native
      state of the recombinantly expressed EMILIN C1q-like domain to be used in cell
      adhesion was determined by CD spectra analysis, which indicated a high value of
      beta-sheet conformation. The EMILIN C1q-like domain promoted a high cell adhesion
      of the leiomyosarcoma cell line SK-UT-1, whereas the fibrosarcoma cell line
      HT1080 was negative.
FAU - Doliana, R
AU  - Doliana R
AD  - Divisione di Oncologia Sperimentale 2, Centro di Riferimento Oncologico di
      Aviano, 33081 Aviano, Italy.
FAU - Mongiat, M
AU  - Mongiat M
FAU - Bucciotti, F
AU  - Bucciotti F
FAU - Giacomello, E
AU  - Giacomello E
FAU - Deutzmann, R
AU  - Deutzmann R
FAU - Volpin, D
AU  - Volpin D
FAU - Bressan, G M
AU  - Bressan GM
FAU - Colombatti, A
AU  - Colombatti A
LA  - eng
SI  - GENBANK/AF088916
GR  - E.0704/Telethon/Italy
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (DNA, Complementary)
RN  - 0 (Extracellular Matrix Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - 0 (elastin microfibril interface located protein)
RN  - 80295-33-6 (Complement C1q)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Aorta/chemistry
MH  - Base Sequence
MH  - Cell Adhesion Molecules/classification/*genetics/isolation & purification
MH  - Chick Embryo
MH  - Circular Dichroism
MH  - Complement C1q
MH  - DNA, Complementary/genetics
MH  - Extracellular Matrix Proteins/classification/*genetics/isolation & purification
MH  - Gene Library
MH  - Humans
MH  - Leucine Zippers
MH  - Membrane Glycoproteins/classification/*genetics/isolation & purification
MH  - Molecular Sequence Data
MH  - Peptide Fragments/chemistry
MH  - Protein Structure, Secondary
MH  - Recombinant Proteins/classification/isolation & purification
MH  - Repetitive Sequences, Amino Acid
MH  - Sequence Analysis, DNA
MH  - Sequence Homology, Amino Acid
MH  - Species Specificity
MH  - Tumor Necrosis Factor-alpha
EDAT- 1999/06/08 00:00
MHDA- 1999/06/08 00:01
CRDT- 1999/06/08 00:00
PHST- 1999/06/08 00:00 [pubmed]
PHST- 1999/06/08 00:01 [medline]
PHST- 1999/06/08 00:00 [entrez]
AID - 10.1074/jbc.274.24.16773 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Jun 11;274(24):16773-81. doi: 10.1074/jbc.274.24.16773.