Relationship between tissue plasminogen activator and the activators in blood and vascular wall

Rijken, D.C.; Wijngaards, G.; Welbergen, J.

doi:10.1016/0049-3848(80)90204-2

Cited by 256 publications

(95 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Authors in [29] reported that cultured bovine endothelial cells synthesized both u-PA and t-PA, while those in [30] found that only antibodies to t-PA, and not antibodies to u-PA, inhibits plasminogen activator activity in human endothelium in tissue sections, as measured by the fibrin overlay method described in [31]. The studies in [30], however, did not exclude that the endothelium still contained considerable amounts of u-PA, because the fibrin overlay method preferenti~ly may detect t-PA, as it is known that the activity of t-PA, in contrast to u-PA, is greatly enhanced by fibrin [32,33]. The present study shows that also on a molar basis the endothelial cells in the intact organism mainly contain t-PA and no demonstrable amounts of u-PA.…”

Section: Discussionmentioning

confidence: 99%

Human endothelial cells contain one type of plasminogen activator

Larsson²,

et al. 1984

View full text Add to dashboard Cite

At least two types of animal plasminogen activating enzymes exist, differing in amino acid sequence, molecular mass and immunological reactivity: the urokinase‐type and the tissue‐type plasminogen activators. By affinity chromatography with monoclonal antibodies, we have purified the human activators of both types to homogeneity. Using immunocytochemistry with rabbit antibodies raised against these preparations, we now demonstrate that the plasminogen activator present in endothelium of veins and other blood vessels is of the tissue‐type. No urokinase‐type plasminogen activator immunoreactivity was detected in endothelial cells in the intact organism. These findings support the assumption that mobilization of plasmin for different purposes may involve different types of plasminogen activators, and that the plasminogen activator involved in thrombolysis is of the tissue‐type.

show abstract

Section: Discussionmentioning

confidence: 99%

Human endothelial cells contain one type of plasminogen activator

Larsson²,

et al. 1984

View full text Add to dashboard Cite

show abstract

“…Human arteries express small amounts of ECP such as MMP-2, tPA, and cathepsins 8,29,30 that participate in tissue homeostasis. Atheromatous plaque, however, shows enhanced expression and activity of many MMPs (1, 2, 3, 7, 8, 9, 11, 12, 13, and 14), 30 -32 ADAMS (9 and 15), 5 papalysins, 6 neutrophil elastase, 33 the fibrinolytic system (tPA and uPA), 34 and cysteine proteases such cathepsin K, S, and V. 8,35 Infiltrating macrophages are the principal and best known protease source, but common components of the vascular wall such as smooth muscle cells, endothelial cells, or fibroblasts also produce ECP such as MMPs, 30,36 ADAMS, 5,37 PAPP-A, 38 tPA, uPA, 34,39 and cathepsins.…”

Section: Extracellular Proteases In the Vasculaturementioning

confidence: 99%

Extracellular Proteases in Atherosclerosis and Restenosis

García‐Touchard

Henry

Sangiorgi

et al. 2005

ATVB

151

106

View full text Add to dashboard Cite

Abstract-Extracellular proteolysis plays a key role in many pathophysiologic processes including cancer, inflammatory diseases, and cardiovascular conditions such as atherosclerosis and restenosis. Whereas matrix metalloproteinases are their best known member, many others are becoming better known. The extracellular proteases are a complex and heterogeneous superfamily of enzymes. They include metalloproteinases (matrix metalloproteinases, adamalysins, or pappalysins), serine proteases (elastase, coagulation factors, plasmin, tissue plasminogen activator, urokinase plasminogen activator), and the cysteine proteases (such cathepsins). In addition to their matrix degradation capabilities, they have other less well known biologic functions that include angiogenesis, growth factor bioavailability, cytokine modulation, receptor shedding, enhancing cell migration, proliferation, invasion, and apoptosis. This review discusses extracellular proteases relevant to the vasculature, their classification and function, and how protease disorders contribute to arterial plaque growth, including chronic atherosclerosis, acute coronary syndromes, restenosis, and vascular remodeling. These broad extracellular protease functions make them potentially interesting therapeutic targets. Key Words: acute coronary syndromes Ⅲ aneurysms Ⅲ athersclerosis Ⅲ proteases Ⅲ restenosis E xtracellular proteolysis is important to many biological processes including tissue remodeling, wound healing, and embryogenesis. It also has a key role in pathophysiologic processes including cancer, chronic inflammatory diseases, and cardiovascular conditions such as atherosclerosis and restenosis.Extracellular proteases (ECP) form a heterogeneous family that is becoming increasingly well understood. Whereas matrix metalloproteinases are the best described, many others are also becoming known. For example, a new protease family, the pappalysins, is now included. Other enzymes such as cysteine proteases were previously considered intracellular enzymes but have recently been shown to function in the extracellular space. In parallel with these discoveries, ECP have generated special interest because they degrade extracellular matrix (ECM). Although recent attention has focused on their impact in vulnerable plaques, promoting weakness and rupture, they are also involved in many other important biological functions.This review discusses extracellular proteases relevant to the vasculature, their function, and how protease disorders contribute to multiple stages of arterial plaque growth, including chronic atherosclerosis, acute coronary syndromes (ACS), restenosis, and vascular remodeling. Extracellular Protease ClassificationProteases or peptidases are enzymes that hydrolyze peptide bonds. They are classified as endopeptidases (cleaving the inner regions of peptide chains) and exopeptidases, which act at or near the peptide ends, liberating a single, dipeptide, or a tripeptide amino acid residue. Endopeptidases are the principal enzymes degrading extracellular prote...

show abstract

“…It is similar or identical to the vascular activator and the activator of the extrinsic fibrinolytic pathway [2]. Native tissue PA (Mr -70 000) is a one-chain polypeptide and has been shown by amino acid and cDNA sequence analysis to be homologous to serine protease zymogens [3,4].…”

Section: Introductionmentioning

confidence: 99%

Isolation of two variants of native one‐chain tissue plasminogen activator

et al. 1982

View full text Add to dashboard Cite

The native one-chain tissue plasminogen activator from the human melanoma cell line (Bowes) occurs in two variants as demonstrated by sodium dodecylsulphate-polyacrylamide gel electrophoresis of reduced and carboxymethylated samples. The two variants were isolated by affinity chromatography on arginineSepharose using a guanidinium-HC1 gradient, in the order of elution, the variants were designated tissue plasminogen activator I and II. Variant I was found to be 3000 Mr larger than variant II and the difference was found to reside in the N-terminal half of the molecule. No substantial difference in carbohydrate content nor in enzymatic activity was demonstrated. Plasminogen activator Tissue plasminogen activator Extrinsic plasminogen activator A rginine-Sepharose chromatographyCarbohydrate Enzymatic activity

show abstract

Relationship between tissue plasminogen activator and the activators in blood and vascular wall

Cited by 256 publications

References 16 publications

Human endothelial cells contain one type of plasminogen activator

Human endothelial cells contain one type of plasminogen activator

Extracellular Proteases in Atherosclerosis and Restenosis

Isolation of two variants of native one‐chain tissue plasminogen activator

Contact Info

Product

Resources

About