PubMed Health⌕ Search

PubMed · 10761632

Interaction between cells and elastin, the elastin-receptor.

Abstract

This article dedicated to Ines Mandl at her 80th birthday is a short review of the recent work of our team on the elastin receptor. Our studies started in the early nineteen eighties aimed at the understanding of cell-elastin interactions. The first experiments reviewed demonstrated the inducible interaction of cells--smooth muscle cells, fibroblasts--with elastic fibers. Their strong adhesion was accelerated and amplified by elastin peptides and cell adhesion to elastin needed protein neosynthesis. The demonstration of the presence of the elastin receptor on leukocytes facilitated the detailed description of the transmission pathway from receptor to the intracellular sites activated by the receptor: modifications of ion fluxes, increase of elastase production and excretion of reactive oxygen species, superoxide and NO*. The calcium transients triggered by elastin peptides acting on the receptor decrease with age, the receptor appears to be uncoupled from the G-proteins, but superoxide release is increased. As circulating blood was shown to contain elastin peptides at concentrations saturating for the receptor (microg/ml conc-s for a Kd in the nanomolar range), the receptor on cells in contact with excess agonists is constantly overstimulated. The continuous release of lytic enzymes and free radicals might well be involved in cell damage. This was demonstrated with human lymphocytes undergoing cell death by necrosis and apoptosis in presence of higher concentrations of elastin peptides.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

L Robert. 1999. Interaction between cells and elastin, the elastin-receptor.. https://doi.org/10.3109/03008209909029103

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Stabilization of globular proteins via introduction of temperature-activated elastin-based switches.

To investigate whether swapping native turns of a globular protein with an elastin-based turn sequence (VPGVG) can increase its thermostability, we have performed molecular dynamics simulations of wild-type chymotrypsin inhibitor 2 (CI2) and variants containing elastin-based turns at 10 degrees C and 40 degrees C. Wild-type CI2 is more stable at 10 degrees C, while both of the variant forms are more stable at 40 degrees C. Detailed analyses indicate that the elastin-based turns do indeed contribute to the inverse temperature behavior of the modified proteins. Therefore, swapping a wild-type turn sequence with an elastin-based turn provides a novel way to both improve stability of target proteins at body temperature and to possibly introduce a temperature-sensitive switch.

Elastin↗

Elastin distribution in the myometrial and vascular smooth muscle of the human uterus.

Magnetic resonance imaging and transvaginal ultrasonography in women of reproductive age suggest that the myometrium consists of inner and outer layers. It was hypothesized that these structural and functional differences in the myometrium might be associated with a variation in elastin distribution. Fifty-one hysterectomy specimens representing all phases of the normal menstrual cycle were studied by immunocytochemistry, orcein staining and image analysis. Elastin was present within the outer myometrial smooth muscle, but was less widely distributed in the inner smooth muscle. Immunoreactivity and staining were observed in the myometrial arteries and arterioles and within the basal portions of endometrial arterioles. Elastin was also present in perivascular tissue, particularly near the large vessels. More extravascular (i.e. perivascular and smooth muscle) elastin was present in the outer myometrium in all cases, although no distinct layering was observed. Semi-quantitative analysis of the elastin distribution in 11 full thickness specimens demonstrated a decreasing gradient from outer to inner myometrium rather than distinct layering. Contrary to previous reports, these data suggest that the external region of the myometrium is more elastic than the inner region and that elastin is found throughout the arteriolar tree of the human uterus.

Elastin↗

Raman spectroscopy of secondary structure of elastinlike polymer poly(GVGVP).

Raman spectra of the elastinlike polypentapeptide poly(GVGVP) were measured in H(2)O and D(2)O as solutions and, after increasing the temperature, as suspensions and sediments. In addition, spectra of the polypentapeptide in the solutions of increasing concentration and in the solid state were also investigated by gradually evaporating the water. Significant changes in band frequencies, intensities, and shapes were found for selected Raman bands in the measured spectra, particularly for the C-H stretching, the glycine CH(2) wagging, and some amide vibrations. The C-H stretching vibrations are influenced predominantly by the presence of water, the glycine CH(2) wagging vibrations are associated with conformational transitions. Three possible types of poly(GVGVP)s in the presence of water were indicated: polymer chains in a relatively extended state in the solution, a beta-spiral structure in the suspension, and irregularly bent chains in the sediment.

Elastin↗