Linked Life Data

9590583

Source:http://linkedlifedata.com/resource/pubmed/id/9590583

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
1998-6-15
pubmed:abstractText
1. Previous studies from our laboratory have suggested that arginine-glycine-aspartic acid (RGD) peptides, serving as a decoy, may prevent tubular obstruction in the ischaemic model of acute renal failure. Specifically, we have demonstrated that: (i) stressed tubular epithelial cells reverse the polarity of integrin receptors from the predominantly basolateral location to the apical cell membrane as a part of a more generalized process of the loss of epithelial cell polarity; (ii) depletion of integrins expressed on the basal cell surface leads to the loss of anchorage to the basement membrane and cell desquamation; (iii) expression of integrin receptors on the apical cell membrane leads to indiscriminate interactions (e.g. the adhesion of desquamated cells to the cells remaining in situ), thus initiating the process of tubular obstruction; and (iv) conglomeration of the desquamated cells via integrin receptors further aggravates tubular obstruction. 2. Importantly, these integrin-based interactions can be blocked by synthetic RGD peptides. The linear RGD peptide injected into the renal artery upon release of the renal artery clamp prevented the elevation of proximal tubular hydrostatic pressure characteristically seen in animals with renal ischaemia that received injection of the vehicle of an inactive peptide. 3. In vivo study of RGD peptides in ischaemic acute renal failure in rats demonstrated attenuation of renal injury and accelerated recovery of renal function. 4. Using linear RGD peptide labelled with 99mTc; we have shown that this probe was retained in ischaemic kidneys. 5. To visualize RGD binding sites at the cellular level, we performed a mapping using fluorescent derivatives of two RGD peptides, a cyclic biotinylated (Bt)-RGD peptide and a linear Rhodamine green-labelled (RhoG)-RGD peptide. 6. The findings suggest that the binding sites for RGD peptide are represented by the alphaVbeta3 integrin in the vasculature and some desquamated cells, whereas the majority of the desquamated cells bind Bt-RGD via beta1 integrins. 7. These findings were further tested using cultured endothelial cells co-incubated with leucocytes. When co-incubation experiments were performed in the presence of cyclic RGD pentapeptide, the adhesion of HL-60 cells to both control and hypoxic endothelial monolayers was significantly reduced.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0305-1870
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
276-9
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:articleTitle
Therapeutic effect of arginine-glycine-aspartic acid peptides in acute renal injury.
pubmed:affiliation
State University of New York, Stony Brook 11794-8152, USA. MGOLIGORSKY@EPO.SUNYSB.EDU
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't