α2-Plasmin Inhibitor is a Substrate for Tissue Transglutaminase

Hevessy, Zsuzsanna; Patthy, András; Kárpáti, Levente; Muszbek, László

doi:10.1016/s0049-3848(00)00261-9

Cited by 16 publications

(18 citation statements)

References 31 publications

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“…The above results are consistent with the finding that TG2 and FXIIIa both preferentially modify Gln2 of Asn-␣2-antiplasmin, the major serpin-type plasmin inhibitor of blood plasma (8,38,61). ␣2-Anti-plasmin also circulates as Met-␣2-anti-plasmin, i.e.…”

Section: Discussionsupporting

confidence: 91%

“…The two enzymes have different specificities for fibrinogen and casein (8, 34 -37). On the other hand, Gln-2 of Asn-␣2-anti-plasmin is the preferred target of both TG2 and FXIIIa (8,38). This finding is consistent with the conclusion that glutamines in unstructured regions like N termini or flexible loops are reactive to transglutaminases (2).…”

supporting

confidence: 87%

“…␣2-Anti-plasmin also circulates as Met-␣2-anti-plasmin, i.e. 12 residues at its N terminus are removed by anti-plasmin-converting enzyme to yield Asn-␣2-anti-plasmin (8,38). Gln-14 of Met-␣2-anti-plasmin (the same as Gln-2 of Asn-␣2-anti-plasmin) remains the major glutamine modified by FXIIIa (38).…”

Section: Discussionmentioning

confidence: 99%

“…12 residues at its N terminus are removed by anti-plasmin-converting enzyme to yield Asn-␣2-anti-plasmin (8,38). Gln-14 of Met-␣2-anti-plasmin (the same as Gln-2 of Asn-␣2-anti-plasmin) remains the major glutamine modified by FXIIIa (38). Similarly, Gln-7 of recombinant N-3 F3t (the same as Gln-3 of FN) was the preferred target of FXIII and TG2 despite the extra 4 residues at the N terminus (Table 3).…”

Section: Discussionmentioning

confidence: 99%

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Reactivity of the N-terminal Region of Fibronectin Protein to Transglutaminase 2 and Factor XIIIA

Annis

Mosher

2011

Journal of Biological Chemistry

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Transglutaminase 2 (TG2) is secreted by a non-classical pathway into the extracellular space, where it has several activities pertinent to fibronectin (FN), including binding to the gelatinbinding domain of FN and acting as an integrin co-receptor. Glutamines in the N-terminal tail of FN are known to be susceptible to transamidation by both TG2 and activated blood coagulation factor XIII (FXIIIa). We used immunoblotting, limited proteolysis, and mass spectrometry to localize glutamines within FN that are subject to TG2-catalyzed incorporation of dansylcadaverine in comparison to residues modified by FXIIIa. Such analysis of plasma FN indicated that Gln-3, Gln-7, and Gln-9 in the N-terminal tail and Gln-246 of the linker between fifth and sixth type I modules ( 5 F1 and 6 F1) are transamidated by both enzymes. Only minor incorporation of dansylcadaverine was detected elsewhere. Labeling of C-terminally truncated FN constructs revealed efficient TG2-or FXIIIa-catalyzed dansylcadaverine incorporation into the N-terminal residues of constructs as small as the 29-kDa fragment that includes 1-5 F1 and lacks modules from the adjacent gelatin-binding domain. However, when only 1-3 F1 were present, dansylcadaverine incorporation into the N-terminal residues of FN was lost and instead was in the enzymes, near the active site of TG2 and terminal domains of FXIIIa. Thus, these results demonstrate that FXIIIa and TG2 act similarly on glutamines at either end of 1-5 F1 and transamidation specificity of both enzymes is achieved through interactions with the intact 29K fragment.

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Section: Discussionsupporting

confidence: 91%

supporting

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Reactivity of the N-terminal Region of Fibronectin Protein to Transglutaminase 2 and Factor XIIIA

Annis

Mosher

2011

Journal of Biological Chemistry

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“…The total volume of reaction mixture was 200 ml containing 10 mM dithiotreitol (DTT), 30 mM ethyl-amine, 0.75 mM adenosine 5 0 -diphosphate, 7.5 mM a-ketoglutarate, 0.8 mM NADPH, 22.5 U/ml glutamate dehydrogenase (EC 1.4.1.4, Roche, Mannheim, Germany), 5 mM CaCl 2 , 5 mM glutamine substrate peptide (representing a sequence from a 2 -plasmin inhibitor; provided by L Kárpáti, Dept. of Clinical Biochemistry and Molecular Pathology, University of Debrecen, Debrecen, Hungary), 2 mg GST-fused TG2 and 150 mg/ml or ten times of normalised concentrations of IgA or IgG in 120 mM HEPES buffer, pH 7.5 [27]. After 10 min preincubation at room temperature (enzyme and antibodies in the buffer) the reaction was performed at 37 C for 30 or 40 min.…”

Section: Kinetic Assay To Measure Deamidating Activity Of Tg2 (Uv-test)mentioning

confidence: 99%

Coeliac autoantibodies can enhance transamidating and inhibit GTPase activity of tissue transglutaminase: Dependence on reaction environment and enzyme fitness

Király¹,

Vecsei²,

Deményi³

et al. 2006

Journal of Autoimmunity

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A coagulation factor becomes useful in the study of acute leukemias: Studies with blood coagulation factor XIII

et al. 2007

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The intracellular form of the coagulation factor XIII has previously been identified by immunomorphological techniques using polyclonal antibodies. In these studies, only the A subunit (FXIII-A) was detectable in megakaryocytes/platelets and in monocytes/ macrophages. We developed several novel monoclonal antibody clones directed to both subunits (FXIII-A and FXIII-B) and investigated their appearance in normal and leukemic cells. By using 3-and 4-color flow cytometry FXIII expression was investigated in normal peripheral blood and bone marrow samples and in acute myeloblastic (AML) and lymphoblastic (ALL) leukemia cases. Samples were studied by Western blotting and confocal laser scanning microscopy. With a previously published ELISA assay applying two monoclonal antibodies directed to different epitopes in FXIII-A, we were able to measure the intracytoplasmic content of FXIII-A in normal cells and leukemic blasts. FXIII-A was detectable in normal peripheral blood monocytes and in large quantities in platelets, but both cell types were negative for FXIII-B. There was no surface staining for FXIII-A, it only appeared intracellularly. In samples derived from patients with AML M4 and M5, FXIII-A sensitively identified blast cells. Although normal lymphocytes do not express FXIII-A, 40% of ALL cases showed significant FXIII-A expression as determined by flow cytometry. FXIII-A positivity of lymphoblasts was verified by Western blotting, ELISA, and confocal laser scanning microscopy cytometry. These data provide evidence that FXIII-A is a sufficiently sensitive marker in differentiating myeloblasts and monoblasts and is suitable for identifying leukemia-associated phenotypes in ALL. ' International Society for Analytical CytologyKey terms factor XIII; flow cytometry; acute leukemia phenotype HEMATOLOGICAL malignancies are exceptional in the sense that unlike solid tumors, right from the beginning they are spread all over the body since cancer cells appear in the blood. Acute leukemias represent 85% of all leukemias in children and 45% in adults. In childhood, $80% of acute leukemias are lymphoblastic and 15-20% are myeloblastic (1), whereas this proportion is basically reversed in adults. Leukemic cells display phenotypes that are either present in normal precursors or is unique for the leukemic population also referred to as leukemia-associated immunophenotype (LAIP) or aberrant phenotype. Several publications described LAIP on blasts in acute leukemias (2-5). The major features are lineage infidelity and lineage promiscuity, where leukemic cells express antigens associated with a different cell line, e.g., CD13 and CD33 myeloid-associated antigens in precursor-B acute lymphoblastic leukemia (ALL) (6) or CD7 T-cell marker expression in neoplastic myeloblasts (7). In case of asynchronous differentiation, markers of different maturational stages are expressed simultaneously, like the coexpression of CD10 and CD20 in B-ALL (8) or CD117/CD15 coexpression in acute myeloid leukemia (AML) (9). Antigen

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α2-Plasmin Inhibitor is a Substrate for Tissue Transglutaminase

Cited by 16 publications

References 31 publications

Reactivity of the N-terminal Region of Fibronectin Protein to Transglutaminase 2 and Factor XIIIA

Reactivity of the N-terminal Region of Fibronectin Protein to Transglutaminase 2 and Factor XIIIA

Coeliac autoantibodies can enhance transamidating and inhibit GTPase activity of tissue transglutaminase: Dependence on reaction environment and enzyme fitness

A coagulation factor becomes useful in the study of acute leukemias: Studies with blood coagulation factor XIII

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