Osteopontin, a substrate for transglutaminase and Factor XIII activity

Prince, Charles W.; Dickie, Diccie; Krumdieck, Carlos L.

doi:10.1016/0006-291x(91)90669-x

Cited by 119 publications

(75 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Furthermore, the predominant form of secreted OPN present in the conditioned media of the 21T series cell lines was of high molecular weight (*97 kDa), whereas MDA-MB-435 cells in addition show signi®cant accumulation of lower molecular weight forms (including a major 66 kDa band). The high molecular weight species may represent either a very heavily post-translationally modi®ed, or conjugated (by transglutaminase) form (Prince et al, 1991;Beninati et al, 1994;Sorensen et al, 1994;Sorensen and Petersen, 1995;Aeschlimann et al, 1996). In keeping with this interpretation is our ®nding that the major intracellular form of OPN present in cell lysates (of both 21T series cells and MDA-MB-435 cells) is the low molecular weight, 66 kDa form.…”

Section: Discussionsupporting

confidence: 52%

Osteopontin induces increased invasiveness and plasminogen activator expression of human mammary epithelial cells

et al. 1999

View full text Add to dashboard Cite

Osteopontin (OPN) has been associated with enhanced malignancy in breast cancer, but its functional role in this disease is poorly understood. To study the e ect of OPN on cellular invasiveness, basal OPN expression was ®rst assessed in members of a progression series of human mammary epithelial cell lines (21PT: immortalized, non-tumorigenic; 21NT: weakly tumorigenic; 21MT-1: tumorigenic, weakly metastatic; MDA-MB-435 cells: tumorigenic, highly metastatic). The two lines which expressed lowest basal levels of OPN (21PT, 21NT) were then examined for up-regulation of invasive behavior in response to exogenous or transfected (endogenous) OPN. Both 21PT and 21NT showed increased invasiveness through Matrigel when human recombinant (hr)OPN was added to the lower chamber of transwells. Both also showed a cell migration response to hrOPN. Populations of 21PT and 21NT cells stably transfected with an OPN-expression vector showed higher levels of cell invasiness than control vector transfectants. Examination of transfectants for mRNA of a number of secreted proteases showed that only urokinase-type plasminogen activator (uPA) expression was closely associated with OPN expression and cellular invasiveness. Treatment of the parental 21PT and 21NT cells with exogenous hrOPN resulted in increased uPA mRNA expression and increased urokinase activity of the conditioned media. Both increased cell migration and induction of uPA expression are thus potential mechanisms of increased invasiness of breast epithelial cells in response to OPN.

show abstract

Section: Discussionsupporting

confidence: 52%

Osteopontin induces increased invasiveness and plasminogen activator expression of human mammary epithelial cells

et al. 1999

View full text Add to dashboard Cite

show abstract

“…This could potentially result in a more resilient barrier at the blood-vessel interface. Other substrates, such as vitronectin (Sane et al, 1990), osteopontin (Prince et al, 1991), thrombospondin (Bale and Mosher 1986), fibronectin (Martinez et al, 1994), dermatan sulfate proteoglycan (Kinsella and Wight, 1990), and apo(a) (Borth et al, 1991), are often increased in the atheromatous plaque (Dufourcq et al, 1998;Giachelli et al, 1995;Hajjar and Nachman, 1996;Riessen et al, 1994;Shekhonin et al, 1987;Wight et al, 1985).…”

Section: Discussionmentioning

confidence: 99%

Localization of Tissue Transglutaminase in Human Carotid and Coronary Artery Atherosclerosis: Implications for Plaque Stability and Progression

Haroon

Wannenburg

Gupta

et al. 2001

Laboratory Investigation

View full text Add to dashboard Cite

SUMMARY:Although atherosclerosis progresses in an indolent state for decades, the rupture of plaques creates acute ischemic syndromes that may culminate in myocardial infarction and stroke. Mechanical forces and matrix metalloproteinase activity initiate plaque rupture, whereas tissue inhibitors of metalloproteinases have an important (albeit indirect) role in plaque stabilization. In this paper, an enzyme that could directly stabilize the plaque is described. Tissue transglutaminase (TG) catalyzes the formation of ⑀(␥-glutamyl)lysine isopeptide bonds that are resistant to enzymatic, mechanical, and chemical degradation. We performed immunohistochemistry for TG in atherosclerotic human coronary and carotid arteries. TG was most prominent along the luminal endothelium and in the medium of the vessels with a distribution mirroring that of smooth muscle cells. Variable, often prominent, immunoreactivity for TG was also seen in the intima, especially in regions with significant neovascularization. Additionally, TG was detected in fibrous caps and near the "shoulder regions" of some plaques. A monoclonal antibody to the transglutaminase product ⑀(␥-glutamyl)lysine isopeptide demonstrated co-localization with TG antigen. Transglutaminase activity was found in 6 of 14 coronary artery atherectomy samples. Cross-linking of TG substrates such as fibrinogen, fibronectin, vitronectin, collagen type I, and protease inhibitors stabilized the plaque. Furthermore, the activation of transforming growth factor-beta-1 by TG might be an additional mechanism for the promotion of plaque stabilization and progression by increasing the synthesis of extracellular matrix components. (Lab Invest 2001, 81:83-93).

show abstract

“…OPN is a substrate of tissue transglutaminase (Prince et al, 1991). Investigations of polymeric OPN showed a 5-fold increase in OPN binding to collagen type I when it was a polymer than when it was a monomer (Kaartinen et al, 1999), which indicates that there is a conformational change in OPN upon cross-linking.…”

Section: Opnmentioning

confidence: 99%