Thrombospondin-1 (TSP-1), an adhesive glycoprotein, plays an important role in platelet adhesion, inflammation, cell-to-cell interaction, and angiogenesis. TSP-1 is expressed by endothelial cells, fibroblasts, and macrophages. TSP-1's unique cysteine-serine-valine-threonine-cysteine-glycine (CSVTCG) specific receptor plays an important role in the binding and modulation of cellular adhesion and invasion. This article histologically and quantitatively evaluates TSP-1 and its CSVTCG receptor in adult burn wounds over time. Tissue was obtained from burn wounds on several days and samples that were 5 microns thick were placed on slides. Expression of TSP-1 and its CSVTCG receptor were evaluated immunohistochemically and quantitated by computer image analysis in units of absorbance. Immunoglobin G (IgG) (negative) controls were performed and subtracted from the TSP-1 sample to eliminate background absorbance readings. Serum (negative) control was used for the CSVTCG receptor. Platelet concentrates were used as the positive control. A quantitative examination of the results yielded the following information, expressed as absorbance +/- standard error of the mean: TSP-1: day 1, 62.0 +/- 10.13; day 3, 76.2 +/- 6.90; day 5, 36.0 +/- 3.96; day 7, 60.4 +/- 5.67; and day 9, 29.5 +/- 2.91. TSP-1 displays an early peak, followed by a steep decrease over the time period studied. The readings for the CSVTCG receptor are as follows: day 1, 33.8 +/- 1.87; day 3, 34.5 +/- 5.39; day 7, 39.1 +/- 1.93; day 21, 39.1 +/- 1.93; day 28, 34.8 +/- 3.67. In contrast, the CVSTCG receptor continues to be present in the wound over time. Histologic findings are reported, and photographs and a histopathologic analysis are included. The information presented in this article leads to the conclusion that temporal and histologic differences exist in the localization and expression of TSP-1 and its CSVTCG receptor. TSP-1 is up-regulated in injured tissues immediately after the injury; it is rapidly down-regulated as the tissue heals. In contrast, the levels of the CSVTCG receptor remain relatively constant during the healing process. These data are consistent with TSP-1's known role in cell-to-cell interaction, including the modulation of the growth factor and protease activity.
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http://dx.doi.org/10.1097/00004630-199811000-00006 | DOI Listing |
J Cell Sci
May 2004
Institut für Physiologische Chemie und Pathobiochemie, Abteilung Angewandte Molekularbiologie, Johannes Gutenberg-Universität Mainz, 55099 Mainz, Germany.
Sponges (Porifera), represent the phylogenetically oldest metazoan phylum still extant today. Recently, molecular biological studies provided compelling evidence that these animals share basic receptor/ligand systems, especially those involved in bodyplan formation and in immune recognition, with the higher metazoan phyla. An in vitro cell/organ-like culture system, the primmorphs, has been established that consists of proliferating and differentiating cells, but no canals of the aquiferous system.
View Article and Find Full Text PDFJ Surg Res
November 2002
Department of Surgical Oncology, University of Texas M.D. Anderson Cancer Center, Houston 77030, USA.
Background: Matrix metalloproteinase 9 (MMP-9) plays a key role in tumor cell invasion. It was recently reported that plasma levels of MMP-9 in patients with gastric cancer correlate with the tumors' metastatic potential. We previously demonstrated that thrombospondin 1 (TSP-1) up-regulates MMP-9 expression by endothelial cells and promotes tumor cell invasion.
View Article and Find Full Text PDFHistol Histopathol
April 2001
MCP Hahnemann University, Department of Pathology, Philadelphia, PA 19102, USA.
Thrombospondin-1 (TSP-1) is a 450 kDa matrix bound glycoprotein involved in tumor invasion, metastasis, and angiogenesis. One of the receptors involved in TSP-1 mediated tumor cell adhesion and metastasis is the cysteine-serine-valine-threonine-cysteine-glycine (CSVTCG) receptor. One mechanism of TSP-1 in promoting tumor cell metastasis involves the up-regulation of matrix metalloproteinase-9 (MMP-9) expression, specifically through the CSVTCG TSP-1 receptor.
View Article and Find Full Text PDFBiochem Biophys Res Commun
April 2000
Human Bone Cell Research Group, Department of Human Anatomy and Cell Biology, New Medical School, University of Liverpool, Ashton Street, Liverpool, L69 3GE, United Kingdom.
Thrombospondin-1 (TSP-1), purified from platelets, stimulates resorption by avian osteoclasts in an in vitro resorption assay. TSP-1 binds to a number of different cellular receptors via different domains of the molecule and several short receptor-binding sequences have been identified within the TSP-1 molecule. In this study, we have used synthetic peptides representing these various sequences in order to identify the cellular receptor and TSP domain responsible for stimulation of resorption.
View Article and Find Full Text PDFAnn Plast Surg
May 1999
Department of Surgery, Allegheny University of the Health Sciences, Medical College of Pennsylvania and Hahnemann University School of Medicine, Philadelphia 19102-1192, USA.
Thrombospondin 1 (TSP-1), an adhesive glycoprotein, plays an important role in platelet adhesion, inflammation, cell-cell interaction, and angiogenesis. TSP-1 is expressed by endothelial cells, fibroblasts, and macrophages. The unique cysteine-serinevaline-threonine-cysteine-glycine (CSVTCG) binding domain of TSP-1 also plays an important role in cell binding and modulation of cellular processes.
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