Transglutaminase-catalysed cross-linking: A potential mechanism for the interaction of fibrinogen, low density lipoprotein and arterial type III procollagen

Bowness, J. M.; Tarr, Alan H.; Wiebe, Rick

doi:10.1016/0049-3848(89)90094-7

Cited by 32 publications

(19 citation statements)

References 20 publications

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“…This mechanism may be the case if ECM polymers were formed with a high proportion of bonds resistant to proteolytic degradation, such as ⑀-(␥-glutamyl) lysine bonds formed by transglutaminase (9). Such a mechanism has been postulated to explain the fibrotic process taking place within the walls of atherosclerotic vessels where the cross-linking of matrix proteins is increased (6)(7)(8). The process also is similar to the cross-linking of fibrin by Factor XIII, which makes the crosslinked fibrin much more resistant to plasmin.…”

Section: Discussionmentioning

confidence: 99%

“…Another factor in the pathogenesis of renal fibrosis may be the resistance of the deposited ECM to breakdown. This resistance has been put forward as a contributing factor in the development of other fibrogenic processes, including lung fibrosis and atherosclerosis (5)(6)(7)(8). Tissue transglutaminase-induced cross-linking of the ECM may underlie its resistance to breakdown.…”

Section: Introductionmentioning

confidence: 99%

“…Involvement in ECM diseases has also been noted (5), as raised tissue transglutaminase levels have been detected in paraquat-induced pulmonary fibrosis. Since then, transglutaminase has been ascribed roles in atherosclerosis (6)(7)(8), cataract formation (23), and neurofibrillary tangles in Alzheimer's disease (24) and tau-containing polymers (25).…”

Section: Introductionmentioning

confidence: 99%

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The role of transglutaminase in the rat subtotal nephrectomy model of renal fibrosis.

Johnson¹,

Griffin²,

Thomas³

et al. 1997

J. Clin. Invest.

119

141

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Tissue transglutaminase is a calcium-dependent enzyme that catalyzes the cross-linking of polypeptide chains, including those of extracellular matrix (ECM) proteins, through the formation of ⑀ -( ␥ -glutamyl) lysine bonds. This crosslinking leads to the formation of protein polymers that are highly resistant to degradation. As a consequence, the enzyme has been implicated in the deposition of ECM protein in fibrotic diseases such as pulmonary fibrosis and atherosclerosis.In this study, we have investigated the involvement of tissue transglutaminase in the development of kidney fibrosis in adult male Wistar rats submitted to subtotal nephrectomy (SNx). Groups of six rats were killed on days 7, 30, 90, and 120 after SNx. As previously described, these rats developed progressive glomerulosclerosis and tubulo-interstitial fibrosis. The tissue level of ⑀ -( ␥ -glutamyl) lysine cross-link (as determined by exhaustive proteolytic digestion followed by cation exchange chromatography) increased from 3. 47

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The role of transglutaminase in the rat subtotal nephrectomy model of renal fibrosis.

Johnson¹,

Griffin²,

Thomas³

et al. 1997

J. Clin. Invest.

119

141

View full text Add to dashboard Cite

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“…Clearly, the mechanism does not require apolipoproteins, since SMase induces aggregation of protein-free emulsions (Fig. 2), though the initial retention to arterial proteoglycans (40) or collagen (44) or the interaction with lipoprotein lipase (41) in vivo presumably does require apolipoprotein B. Moreover, other apolipoproteins, such as apolipoprotein AI, may prevent lipoprotein aggregation (45); in fact, we found that SMase-induced aggregation of LDL is completely blocked by free apo AI or apo AI-containing HDL 3 when added to LDL at an apo AI:apo B-100 molar ratio of 0.5 2 .…”

Section: Discussionmentioning

confidence: 99%

Rabbit aorta and human atherosclerotic lesions hydrolyze the sphingomyelin of retained low-density lipoprotein. Proposed role for arterial-wall sphingomyelinase in subendothelial retention and aggregation of atherogenic lipoproteins.

Schissel

Tweedie-Hardman²,

Rapp³

et al. 1996

J. Clin. Invest.

320

248

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Aggregation and retention of LDL in the arterial wall are key events in atherogenesis, but the mechanisms in vivo are not known. Previous work from our laboratories has shown that exposure of LDL to bacterial sphingomyelinase (SMase) in vitro leads to the formation of LDL aggregates that can be retained by extracellular matrix and that are able to stimulate macrophage foam cell formation. We now provide evidence that retained LDL is hydrolyzed by an arterial-wall SMase activity. First, we demonstrated that SMase-induced aggregation is caused by an increase in particle ceramide content, even in the presence of excess sphingomyelin (SM). This finding is compatible with previous data showing that lesional LDL is enriched in SM, though its ceramide content has not previously been reported. To address this critical compositional issue, the ceramide content of lesional LDL was assayed and, remarkably, found to be 10-50-fold enriched compared with plasma LDL ceramide. Furthermore, the ceramide was found exclusively in lesional LDL that was aggregated; unaggregated lesional LDL, which accounted for 20-25% of the lesional material, remained ceramide poor. When

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“…The isopeptidic crosslinked amino acids produced in man by factor XIIIa remain intact after the proteolysis of the clot by plasmin and are excreted with the urine [11,12]. If this is the general fate of Glu Lys(N 6 -γ-glutamyllysine), a possible function of the new enzyme could be the salvage of lysin and glutamic acid during the long storage of the blood in the gut of the leech.…”

Section: Resultsmentioning

confidence: 99%

An isopeptide bond splitting enzyme from Hirudo medicinalis similar to γ‐glutamyl transpeptidase

Friedrich

Kröger

Koerwer

et al. 1998

European Journal of Biochemistry

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A new enzyme from Hirudo medicinalis capable of splitting γ-glutamyl-p-nitroanilide and Glu Lys-(N 6 -γ-glutamyllysine) (isopeptidic bond between the ε-amino group of lysine and the γ-carboxylic group of glutamic acid) isopeptide bonds was purified. The protein was partially sequenced at the amino acid level, and the complete nucleotide and amino acid sequences were determined after cDNA cloning. The new enzyme has more than 60% similarity at the amino acid level to vertebrate γ-glutamyl transpeptidase (γ-GT). According to the cDNA, the new protein has a molecular mass of 65521 Da and a length of 600 amino acids.

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Transglutaminase-catalysed cross-linking: A potential mechanism for the interaction of fibrinogen, low density lipoprotein and arterial type III procollagen

Cited by 32 publications

References 20 publications

The role of transglutaminase in the rat subtotal nephrectomy model of renal fibrosis.

The role of transglutaminase in the rat subtotal nephrectomy model of renal fibrosis.

Rabbit aorta and human atherosclerotic lesions hydrolyze the sphingomyelin of retained low-density lipoprotein. Proposed role for arterial-wall sphingomyelinase in subendothelial retention and aggregation of atherogenic lipoproteins.

An isopeptide bond splitting enzyme from Hirudo medicinalis similar to γ‐glutamyl transpeptidase

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