Disease relevance of EMILIN1

• 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 [1].
• The frequency distribution curves of EMI numbers within the lung fields of patients who proved to have centri-acinar emphysema differed significantly from those of the group who did not, there being more pixels in the EMI range -450 to -500 in the emphysematous group (p less than 0.001) [2].
• Comparative clinical impact of endoscopic pancreatography, grey-scale ultrasonography, and computed tomography (EMI scanning) in pancreatic disease: preliminary report [3].
• The European Myocardial Infarction Project (EMIP) should go far towards answering the question [4].
• Resolution of the low-density abnormally seen on serial EMI scanning and resolution of the vasculitis demonstrated in the post-therapy brain biopsy specimen was dramatic [5].

Psychiatry related information on EMILIN1

• Seventeen schizophrenic patients with tardive dyskinesia (TD) and 33 schizophrenics without tardive dyskinesia were examined by psychological tests of intellectual function and EMI scans were performed [6].
• OBJECTIVES: The objective of this study is to examine the association between Alzheimer's disease and head injury in elderly patients referred to an EMI unit [7].

High impact information on EMILIN1

• Emilin1 knockout mice display elevated blood pressure due to increased TGF-beta signaling in the vasculature [8].
• In both post- and pre-embedding immunolabeling emilin was mainly associated with regions where elastin and microfibrils are in close contact, such as the periphery of the fibers [9].
• Emilin, a component of elastic fibers preferentially located at the elastin-microfibrils interface [9].
• The name of the protein was derived from its localization at sites where elastin and microfibrils are in proximity (emilin, elastin microfibril interface located protein) [9].
• Immunofluorescence studies have shown that emilin produced by chick embryo aorta cells in culture is strictly associated with elastin and that the process of elastin deposition is severely altered by the presence of antiemilin antibodies in the culture medium [9].

Chemical compound and disease context of EMILIN1

• The CT patterns of 295 glioblastomas examined with pre- and postcontrast scans using an EMI scanner Mark I (Matrix 160/160) have been reviewed and compared with the CT appearances of other brain tumors, metastases and abscesses [10].
• This is the first case report of pituitary tumor associated with angioid streaks documented by fluorescein angiography, EMI scan, and histopathologic diagnosis of the tumor, and also in which pseudoxanthoma elasticum was ruled out, both clinically and by a negative skin biopsy [11].

Biological context of EMILIN1

• The entire gene (localized on chromosome 18p11.3) was isolated from a BAC clone, and it is structurally almost identical to that of EMILIN (8 exons, 7 introns with identical phases at the exon/intron boundaries) but much larger (about 40 versus 8 kilobases) than that of EMILIN [12].
• The detection of EMILIN1, a connective tissue glycoprotein associated with elastic fibers, at the level of the ectoplacental cone and trophoblast giant cells of developing mouse embryos (Braghetta et al., 2002) favored the idea of a structural as well as a functional role for this protein in the process of placentation [13].
• 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 [1].
• The 3'-end of the EMILIN gene overlaps with the 5'-end of the promoter region of the ketohexokinase gene, whose chromosomal position is between markers D2S305 and D2S165 on chromosome 2 [14].
• This pattern was in accord with the ability of EMILIN-1 to promote cell movement [15].

Anatomical context of EMILIN1

• EMILIN (elastin microfibril interfase located Protein) is an elastic fiber-associated glycoprotein consisting of a self-interacting globular C1q domain at the C terminus, a short collagenous stalk, an extended region of potential coiled-coil structure, and an N-terminal cysteine-rich domain (EMI domain) [12].
• The mRNA expression of EMILIN-2 is more restricted compared with that of EMILIN-1; highest levels are present in fetal heart and adult lung, whereas, differently from EMILIN-1, adult aorta, small intestine, and appendix show very low expression, and adult uterus and fetal kidney are negative [12].
• In this study we show that EMILIN1, produced by decidual stromal and smooth muscle uterine cells, is expressed in the stroma and in some instances as a gradient of increasing concentration in the perivascular region of modified vessels [13].
• EMILIN, a component of the elastic fiber and a new member of the C1q/tumor necrosis factor superfamily of proteins [1].
• Avian EMILIN was extracted from 19-day-old embryonic chick aortas and associated blood vessels and purified by ion-exchange chromatography and gel filtration [1].

Associations of EMILIN1 with chemical compounds

• Function-blocking monoclonal antibodies against alpha4-integrin chain and against EMILIN1 as well as the use of EMILIN1-specific short interfering RNA confirmed that trophoblasts interact with EMILIN1 and/or its functional gC1q1 domain via alpha4beta1 integrin [13].
• Tryptic peptides were generated from EMILIN and sequenced, and degenerate inosine-containing oligonucleotide primers were designed from some peptides [1].
• Postpartum, her evaluation included normal thyroid function studies, a normal thyroid-stimulating hormone response to protirelin (thyrotropin-releasing hormone), normal serum and urine gonadotropin levels, normal serum prolactin, normal sella turcica tomograms, and a normal EMI brain scan [16].
• The effect of the kVp level on EMI values. Selective imaging of various materials with different kVp settings [17].
• The CT values of a variety of materials were studied in an EMI and a Syntex head scanner [18].

Other interactions of EMILIN1

• Isolation and characterization of EMILIN-2, a new component of the growing EMILINs family and a member of the EMI domain-containing superfamily [12].
• The domain organization is superimposable, one important difference being a proline-rich (41%) segment of 56 residues between the potential coiled-coil region and the collagenous domain absent in EMILIN [12].
• 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 [1].
• The primary structure of human Elastin microfibril interface-located protein (EMILIN), an elastic fiber-associated glycoprotein, consists of a globular C1q domain (gC1q) at the C terminus, a short collagenous stalk, a long region with a high potential for forming coiled-coil alpha helices, and a cysteine-rich N-terminal sequence [19].
• The gene for EMILIN-1 was mapped on chromosome 2p23 overlapping with the promoter region of the ketohexokinase gene [20].

Analytical, diagnostic and therapeutic context of EMILIN1

• Finally, membrane type I-matrix metalloproteinase (MT1-MMP) and MMP-2 were upregulated in co-cultures of trophoblast cells and stromal cells, suggesting a contributing role in the haptotactic process towards EMILIN1 [13].
• Based on peptide sequences, chicken and human cDNAs coding for EMILIN were isolated by RT/PCR by screening kidney and heart cDNA libraries [20].
• This localization of emilin in aorta has been confirmed by quantitative evaluation of the distribution of gold particles within elastic fibers [9].
• Molecular cloning and characterization of EndoGlyx-1, an EMILIN-like multisubunit glycoprotein of vascular endothelium [21].
• Using pneumoencephalography and computerized axial tomography (EMI scanning) Polaroid pictures, the relationship between ventricular size and cerebral size was investigated in 35 patients [22].

References