Identification of a substrate site for liver transglutaminase on the aminopropeptide of type III collagen.

Bowness, J. M.; Folk, J.E.; Timpl, Rupert

doi:10.1016/s0021-9258(19)75743-3

Cited by 101 publications

(21 citation statements)

References 22 publications

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“…coordinate expression of a 1 (XVI) and FXIIIa in the monocytederived dendritic cells led us to investigate whether the a 1 (XVI) chain can be a potential substrate for FXIIIa. We determined the incorporation of [ 3 H]putrescine by FXIIIa into two different domains (COL1´NC1 and NC11) of the a 1 (XVI) polypeptide with BSA and type I and type III collagens as negative controls (Bowness et al, 1987), and two well-characterized transglutaminase substrates N,N¢-dimethylcasein and plasma ®bronectin as positive controls (Fesus et al, 1986;Bowness et al, 1987;Aeschlimann and Paulsson, 1991). Incubation of COL1´NC1 domain of a 1 (XVI) with FXIIIa gave only background levels of incorporation, comparable with the reaction with BSA and type I and type III collagens.…”

Section: Resultsmentioning

confidence: 99%

“…The previous reports that wound healing is impaired in FXIII-de®cient patients (Lorand et al, 1980), FXIII stimulates ®broblast proliferation and suppresses collagen biosynthesis by ®broblasts (Beck et al, 1961;Paye et al, 1989), FXIIIa catalyzes the cross-linking of ®brin(ogen), ®bronectin itself, and ®bronectin to collagens type I, II, III, and V (Mosher et al, 1980;Mosher, 1984) may support this idea. By contrast, it has been demonstrated that FXIIIa, unlike tissue transglutaminase, does not catalyze the cross-linking of aminopropeptide of type III collagen (Bowness et al, 1987) or the cross-linking between collagens (Mosher, 1984). Intermolecular cross-linking of a 1 (XVI) molecule catalyzed by FXIIIa therefore may be unique in FXIIIa + DD, suggesting that the cross-linking may stabilize and support the placement of DD in the extracellular tissue.…”

Section: Discussionmentioning

confidence: 97%

“…N,N¢dimethylcasein, BSA and thrombin were obtained from Sigma. Incorporation of [1,4-3 H]putrescine (1.0 TBq per mmol; Amersham) by FXIIIa into various collagenous and noncollagenous polypeptides was determined according to the method of Bowness et al (1987). Activation of FXIIIa was performed by incubating 1 mg of FXIII per ml with 0.1 mg thrombin per ml at 37°C for 15 min in 0.1 M Tris±HCl, pH 8.5, 5 mM CaCl 2 in a total volume of 40 ml.…”

Section: Methodsmentioning

confidence: 99%

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Type XVI Collagen is Expressed in Factor XIIIa+ Monocyte-Derived Dermal Dendrocytes and Constitutes a Potential Substrate for Factor XIIIa

Akagi

Tajima

Ishibashi

et al. 2002

Journal of Investigative Dermatology

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We have previously reported that connective tissue cells in the superficial dermis preferentially express alpha1(XVI) collagen rather than those in the lower dermis. Double immunofluorescence labeling using the antibodies for alpha1(XVI) collagen and factor XIIIa (plasma transglutaminase), which is a marker of dermal dendrocytes, demonstrated that both antibodies reacted with the same cells in the superficial dermis of normal skin as well as the lesional skins of dermal dendrocyte-related disorders, dermatofibroma, and psoriasis. Dermal dendrocytes are considered to be established by a culture of peripheral blood monocytes in the presence of granulocyte macrophage-colony stimulating factor and interleukin-4. Reverse transcription--polymerase chain reaction, metabolic labeling, and immunofluorescence studies demonstrated that treatment of CD14+ peripheral blood monocytes with granulocyte macrophage-colony stimulating factor/interleukin-4 over a period of 8 d resulted in the induction of alpha1(XVI) collagen as well as factor XIIIa. The physiologic significance of colocalization of alpha1(XVI) collagen and factor XIIIa in the tissue and their coordinate induction in CD14+ monocyte-derived dendritic cells in vitro was studied. Considerable incorporation of [3H]putrescine by factor XIIIa into recombinant noncollagenous domain (NC) 11 but not into collagenous domain (COL) 1.NC1 domain of the alpha1(XVI) polypeptide was found. Incubation of recombinant NC11 of alpha1(XVI) polypeptide with factor XIIIa in vitro produced a covalent cross-linking complex on sodium dodecylsulfate-polyacrylamide gel electrophoresis. The results indicate that alpha1(XVI) collagen is constitutively expressed by most dermal dendrocytes in the skin and dendritic cells differentiated from peripheral blood monocytes in vitro. Type XVI collagen is expressed in factor XIIIa+ dermal dendrocytes and may form an intermolecular cross-linking through NC11 domain by the reaction catalyzed by factor XIIIa contributing to the structural integrity of factor XIIIa+ dendritic cell-rich tissues.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 97%

Section: Methodsmentioning

confidence: 99%

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Type XVI Collagen is Expressed in Factor XIIIa+ Monocyte-Derived Dermal Dendrocytes and Constitutes a Potential Substrate for Factor XIIIa

Akagi

Tajima

Ishibashi

et al. 2002

Journal of Investigative Dermatology

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“…The search for cross-linked peptides against a whole human proteome database is a very challenging task that has not been resolved [43]. Therefore, we restricted our search to a database containing ECM proteins that are known to be TG2 targets, including collagen type I, III and V [44][45][46], fibrinogen [47] and fibronectin [48]. Minimum score thresholds were established based on typical MassMatrix scores obtained from a tryptic, transglutaminase cross-linked control peptide (manuscript submitted).…”

Section: Identification Of Transglutaminase Cross-linking Sites In Tgfβ-1 Stimulated Dermal Fibroblast Ecmmentioning

confidence: 99%

TGFβ-1 Induced Cross-Linking of the Extracellular Matrix of Primary Human Dermal Fibroblasts

Semkova

Hsuan

2021

IJMS

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Excessive cross-linking is a major factor in the resistance to the remodelling of the extracellular matrix (ECM) during fibrotic progression. The role of TGFβ signalling in impairing ECM remodelling has been demonstrated in various fibrotic models. We hypothesised that increased ECM cross-linking by TGFβ contributes to skin fibrosis in Systemic Sclerosis (SSc). Proteomics was used to identify cross-linking enzymes in the ECM of primary human dermal fibroblasts, and to compare their levels following treatment with TGFβ-1. A significant upregulation and enrichment of lysyl-oxidase-like 1, 2 and 4 and transglutaminase 2 were found. Western blotting confirmed the upregulation of lysyl hydroxylase 2 in the ECM. Increased transglutaminase activity in TGFβ-1 treated ECM was revealed from a cell-based assay. We employed a mass spectrometry-based method to identify alterations in the ECM cross-linking pattern caused by TGFβ-1. Cross-linking sites were identified in collagens I and V, fibrinogen and fibronectin. One cross-linking site in fibrinogen alpha was found only in TGFβ-treated samples. In conclusion, we have mapped novel cross-links between ECM proteins and demonstrated that activation of TGFβ signalling in cultured dermal fibroblasts upregulates multiple cross-linking enzymes in the ECM.

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“…It is often highly expressed at sites of pathologic injury where it acts together with factor XIIIa, the plasma transglutaminase (Weinberg et al, 1991;Wiebe et al, 1991). Several extracellular proteins like fibrin(ogen) (Achyuthan et al, 1988;Shainoff et al, 1991), fibronectin (F6sus et al, 1986), vitronectin (Sane et al, 1988;Skorstengaard et al, 1990), nidogen/entactin (Aeschlimann and Paulsson, 1991;Aeschlimann et al, 1992), collagen type III N-propeptide (Bowness et al, 1987) and osteopontin (Prince et al, 1991) have been identified as specific glutaminyl substrates for tissue transglutaminase. Together with the observed association of tissue transglutaminase expression with programmed cell death and pathologic injury, the cross-linking of extracellular matrix components indicates a physiological function of the enzyme in maintaining the integrity of the tissue by fixation of the matrix at the site of the lesion (Upchurch et al, 1991).…”

mentioning

confidence: 99%

Expression of tissue transglutaminase in skeletal tissues correlates with events of terminal differentiation of chondrocytes.

Aeschlimann

Wetterwald

Fleisch

et al. 1993

The Journal of Cell Biology

174

194

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Identification of a substrate site for liver transglutaminase on the aminopropeptide of type III collagen.

Cited by 101 publications

References 22 publications

Type XVI Collagen is Expressed in Factor XIIIa+ Monocyte-Derived Dermal Dendrocytes and Constitutes a Potential Substrate for Factor XIIIa

Type XVI Collagen is Expressed in Factor XIIIa+ Monocyte-Derived Dermal Dendrocytes and Constitutes a Potential Substrate for Factor XIIIa

TGFβ-1 Induced Cross-Linking of the Extracellular Matrix of Primary Human Dermal Fibroblasts

Expression of tissue transglutaminase in skeletal tissues correlates with events of terminal differentiation of chondrocytes.

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