Disease relevance of F13a1

• Factor XIIIa-positive dendrocytes are abundant within the dermis and have been implicated in the pathogenesis of various disorders, including AIDS-related Kaposi's sarcoma [1].
• Molecular imaging of factor XIIIa activity in thrombosis using a novel, near-infrared fluorescent contrast agent that covalently links to thrombi [2].
• Soluble fibronectin interacts with denatured collagen, heparin, fibrin, and Staphylococcus aureus, and is a substrate for thrombin, plasma and factor XIIIa [3].

High impact information on F13a1

• We report here that intracellular factor XIIIA transglutaminase crosslinks agonist-induced AT1 receptor homodimers via glutamine315 in the carboxyl-terminal tail of the AT1 receptor [4].
• In agreement with this finding, factor XIIIA-deficient individuals lacked crosslinked AT1 dimers [4].
• Factor XIIIA transglutaminase crosslinks AT1 receptor dimers of monocytes at the onset of atherosclerosis [4].
• 12E2 is a cloned cell line derived from superficial murine dermis where factor XIIIa-positive dendrocytes are abundant [1].
• Additional mutation of the glutamine at position 16, however, eliminates >99% of cross-linking suggesting that it also may be factor XIIIa reactive [5].

Biological context of F13a1

• The purpose of this study was to determine the amino acid requirements at the active site of FXIIIa for catalysis [6].

Anatomical context of F13a1

• We revealed the expression of FXIIIA in the epiphyseal growth plate, where FXIIIA appears first intracellularly in the zone of proliferation/maturation, and remains intra- and extracellularly throughout the hypertrophic zone [7].
• We conclude, that coagulation factor FXIIIA is expressed by chondrocytes of embryonic mouse long bone cartilages in a strictly regulated pattern, which correlates with chondrocyte differentiation and matrix mineralization [7].
• At day 7 post-BLM, 48% of CD11b+ BAMC displayed features of DC differentiation, as judged by dendritic morphology, expression of class II MHC, 33D1, Factor XIIIa, CD80, and CD86 antigens, and the ability to support a primary allogeneic lymphocyte response (MLR) [8].
• Double-labelling experiments showed that a proportion (approximately 20%) of PKC-beta+ dendritic cells also expressed factor XIIIa [9].
• Expression of the A subunit of factor XIII is restricted to megakaryocytes in the bone marrow cavity, and factor XIIIa is abundant in platelets that probably provide the major source for factor XIII in plasma [10].

Associations of F13a1 with chemical compounds

• Inhibition of angiotensin II release or of factor XIIIA activity prevented formation of crosslinked AT1 receptor dimers [4].
• FXIIIa activity was assessed by measuring the incorporation of 5-(biotinamido)pentylamine into N,N'-dimethylcasein in a solid-phase microtiter plate assay [6].
• The other five mutations near the active-site Cys resulted in FXIIIa molecules in which the activity was reduced > 95% [6].
• FXIIIa catalyzed polymerization of pp-vWF as well as the incorporation of monodansylcadaverine and [14C]putrescine into pp-vWF in a Ca(2+)- and time-dependent manner [11].
• Taking all the data together it can be concluded that both pp-vWF and laminin have glutamine and lysine residues responsive to FXIIIa and make copolymers by virtue of FXIIIa [11].

Analytical, diagnostic and therapeutic context of F13a1

• Analysis of the catalytic activity of human factor XIIIa by site-directed mutagenesis [6].
• These cells express Factor XIIIa and VCAM-1 by immunohistochemistry and by Western blot analysis of 12E2 cell lysates [1].
• Sections were stained with specific antibodies to PKC-alpha, PKC-beta, CD1a, T cells, B cells and dermal dendritic cells (factor XIIIa), using an immunoperoxidase technique [9].

References