PubMed
Recent publications
Soltani F, Duval C, Ariens RS, Kaartinen MT (2025) Off-target genomic effects in MRP8-Cre driver mice complicates its use in weight gain and metabolic studies. BioRxiv. https://biorxiv.org/cgi/content/short/2025.01.06.631557v1
Soltani F, Wellman M, Pacis A, Lordkipanidze M, Kaartinen MT (2025) Neutrophil Factor XIII-A transglutaminase contributes to Neutrophil Extracellular Trap (NET)-mediated fibrin network formation. Thromb. Hemost. Jan 20. doi: 10.1055/a-2504-1559
Ebrahimi Samani S, Tatsukawa H, Hitomi K, Kaartinen MT (2024) Transglutaminase 1 - emerging functions beyond skin. Review. Int. J. Med. Sci. (IF 4.9). Sep 25;25(19):10306.
Mahmoodi M, Mirzarazi Dahagi E, Nabavi M-H, Ylauna Penalva, Gosaine A, Murshed M, Couldwell S, Lisa Munter, Kaartinen MT (2024) Circulating plasma fibronectin affects tissue insulin sensitivity, adipocyte differentiation and transcriptional landscape of adipose tissue in mice. Phys. Rep. (IF 2.4), Jul;12(14):e16152.
Soltani F, Kaartinen MT (2023) Transglutaminases in fibrosis – overview and recent advances. Am J Pathol - Cell Physiology. (IF 5.5) Oct 1;325(4):C885-C894
Jääskelainen I, Petäisto T, Mirzarazi Dahagi E, Mahmoodi M, Pihjalaniemi T, Kaartinen MT, Heljesvaara R (2023) Collagens in adipose tissue formation and function. Biomedicines. May 10;11(5):1412.
Ebrahimi-Samani S, Kaartinen MT (2023) Increased osteoclastogenesis in the absence of TG2 is reversed by transglutaminase inhibition - evidence for the roles of TG1 and FXIII-A and their regulation by TG2. Cells, 12, 2139
Gates EW, Mansour K, Ebrahimi-Samani S, Shad S, Kaartinen MT, Keillor JW (2023) Peptidic inhibitors and fluoresencent probe for the selective inhibition and labelling of coagulation Factor XIIIa transglutaminase. Molecules Feb 8;28(4):1634
Kaartinen MT, Hang A, Barry A, Arora M, Heinonen S, Lundholm J, Hakkarainen A, Rissanen A, Kaprio J, Pietilainen K (2022). Matrisome alterations in in obesity – a transcriptomics study on weight-discordant monozygotic twins. Matrix Biology. 108, 1-19.
Al-Hameda, FS, Abu-Nadaa L, Rodan R, Sarrigiannidisb S, Ramirez-Garcialunac JL, Mousa H , ElkashtyaO, Goaa Q, Basiria T, Tran SD, Lordkipanidzé, Kaartinen MT, Badrana Z, Tamimi F (2021). Differences in platelet concentrate composition influence bone healing. J Clin Periodontol. Dec;48(12):1613-1623.
Al-Hameda, FS, Rodan R, Ramirez-Garcialunac JL, Elkashty O, Goaa Q, Al-Shahrani N, Tran SD, Lordkipanidzé M, Kaartinen MT, Badran Z, Tamimi F (2021). The effect of aging on the bone healing properties of blood plasma. Injury. Jul;52(7):1697-1708.
Kaartinen MT, Arora M, Heinonen S, Rissanen A, Kaprio J, Pietilainen K. Transglutaminases and obesity: association of F13A1 to adipocyte hypetrophy and adipose tissue inflammation. Int. J Med. Sci. 21(21):8289.
Kaartinen MT, Arora M, Heinonen S, Hang A, Barry A, Lundholm J, Hakkarainen A, Kaprio J, Pietilainen K (2021). F13A1 transglutaminase in human adipose tissue associated with weight gain, and inflammatory status of adipocytes. Int J Obesity 45(3):577-587.
Mansour A, Abu Nada L, Elhahad A, Mezour MA, Al-Subaie A, Mussa Hanan, Laurenti M, Kaartinen MT, Tamimi F (2021). Biomimetic concentrations of trace elements improve bone regenerative properties of dicalcium phosphate bioceramics. J Biomed Mater Res A. 109(5):666-681.
Sun H and Kaartinen MT (2020). Assessment of activities of TG1, TG2 and Factor XIII-A during osteoclastogenesis. Analytical Biochem. 591:113512.
Chicatun F, Muja N, Rezabiegi E, Kaartinen MT, McKee MD Showan N. Nazhat SN (2019) A bilayered dense collagen/chitosan hydrogel to model the osteochondral interface. Emergent Materials. 2: 245-262.
Mansour A, Abu Nada L, Al-Waeli H, Mezour MA, Al-Abdallah MN, Kinsella JM, Kort Mascort J, Henderson JE, Ramirez-Garcialuna JL, El-Kashty O, Taqi, D, Alageel O, Kaartinen MT, Tamimi F (2019). Bone extracts immunomodulate and enhance the regenerative performance of dicalcium phosphates bioceramics. Acta Biomaterialia. 89:343-358.
Sun H and Kaartinen MT (2018). Transglutaminases in monocytes and macrophages. Med Sci. 6(4).
Sun H and Kaartinen MT (2018). Transglutaminase activity regulates differentiation, migration and fusion of osteoclasts via affecting actin dynamics. J. Cell Phys. 233(9):7497-7513.
Mousa A, Cui C, Song A, Myneni VD, J. Li, Murshed M, Melino G, Kaartinen MT (2017). Transglutaminases Factor XIII-A and TG2 regulate resorption, adipogenesis and plasma fibronectin homeostasis in bone and bone marrow. Cell Death Diff. 24(5):844-854.
Hoac B, Nelea V, Jiang W, Kaartinen MT, McKee MD (2017) Mineralization-inhibiting effects of transglutaminase-crosslinked polymeric osteopontin. Bone. 101:37-48
Myneni VD, Kaartinen MT (2016). Factor XIII-A deficient mice show signs of metabolically healthy obesity on high fat diet. Sci Rep. 6:35574.
Myneni VD, Kaartinen MT (2015). Transglutaminase 2 - A novel inhibitor of adipogenesis. Cell Death & Dis. 6:e1868.
Wang S, Kaartinen MT (2015). Cellular Factor XIIIA transglutaminase localizes in caveolae and regulates caveolin-1 phosphorylation, homo-oligomerization and c-Src signaling in osteoblasts. J. Histochem Cytochem. 63(11):829-41.
Cui C, Kaartinen MT (2015). Monoamines serotonin, inhibit plasma fibronectin assembly into extracellular matrix by acting as a competitive inhibitor to its transglutaminase mediated crosslinking. Bone. 72:43-52.
Addison WN, Nelea V, Chicatun F, Chien Y-C, Vali H, Tran-Khanh N, Buschmann MD, Nazhat SN, Kaartinen MT, Vali H, Tecklenburg M, Franceschi RT and McKee MD (2015). Extracellular matrix mineralization in murine MC3T3-E1 osteoblast cultures: An ultrastructural, compositional and comparative analysis with mouse bone. Bone. 71C:244-256.
Dargahi M, Nelea V, Mousa A, Omanovic S, Kaartinen MT (2014) Electrochemical modulation of plasma fibronectin surface conformation enables filament formation and control of endothelial cell-surface interactions. RSC Adv. 4 (88): 47769 - 47780.
Myneni VD, Hitomi K, Kaartinen MT (2014). Factor XIII-A transglutaminase acts as a switch between preadipocyte proliferation and differentiation. Blood. 124(8):1344-53.
Wang S, Cui C, Hitomi K, Kaartinen MT (2014). Detyrosinated Glu-tubulin is a substrate for cellular Factor XIIIA transglutaminase in differentiating osteoblasts. Amino Acids. 46(6):1513-26.
Ka K, Nicolau B, Henderson M, Tran S, Kaartinen MT, Myneni VD, Rousseau M-C (2014). Circulating uncarboxylated osteocalcin and gingival crevicular fluid tumour necrosis factor-α in children. J. Clin. Periodont. 41(5):467-72.
Eckert R, Kaartinen MT, Nurminskaya M, Belkin A, Colak G, Johnson GCW, Mehta K (2014). Transglutaminase regulation of cell function. Physiol. Reviews. 94, 383-417.
Cui C, Wang S, Myneni VD, Hitomi K, Kaartinen MT (2014). Transglutaminase activity is required for stabilization and conversion of plasma FN into permanent osteoblast matrix. Bone 59, 127-138.
Javaid M, Kaartinen MT (2013) Mesenchymal stem cell-based bone tissue engineering. Review. Int. Dental Journal of Students’ Research.1 (3), 24-35.
Dastjerdi AK, Pagano M, McKee MD, Kaartinen MT and Barthelat F (2012). The cohesive behavior of soft biological "glues": Experiments and modeling. Acta Biomater. 8: 3349–3359.
Piercy-Kotb SA, Mousa A, Al-Jallad HF, Myneni VD, Chicatun F, Nazhat SN, Kaartinen MT (2012). Factor XIIIA expression and secretion in osteoblast cultures is regulated by extracellular collagen network and MAP kinase pathway. J Cell Physiol. 227(7):2936-46.
Recent reviews
Transglutaminase 1: Emerging Functions beyond Skin
Sahar Ebrahimi Samani 1 , Hideki Tatsukawa 2 , Kiyotaka Hitomi 2 , Mari T Kaartinen 1 3
1 Division of Experimental Medicine, Faculty of Medicine and Health Sciences, McGill University, Montreal, QC H3A 0C7, Canada.
2 Department of Basic Medicinal Sciences, Graduate School of Pharmaceutical Sciences, Nagoya University, Nagoya 464-8601, Japan.
3 Faculty of Dental Medicine and Oral Health Sciences, McGill University, Montreal, QC H3A 1G1, Canada.
Transglutaminase enzymes catalyze Ca2+- and thiol-dependent posttranslational modifications of glutamine-residues that include esterification, hydrolysis and transamidation, which results in covalent protein-protein crosslinking. Among the eight transglutaminase family members in mammals, transglutaminase 1 (TG1) plays a crucial role in skin barrier formation via crosslinking and insolubilizing proteins in keratinocytes. Despite this established function in skin, novel functions have begun merging in normal tissue homeostasis as well as in pathologies. This review summarizes our current understanding of the structure, activation, expression and activity patterns of TG1 and discusses its putative novel role in other tissues, such as in vascular integrity, and in diseases, such as cancer and fibrosis.
Transglutaminases in fibrosis - overview and recent advances
Fatemeh Soltani 1 , Mari T Kaartinen 1 2
1 Division of Experimental Medicine, Faculty of Medicine and Health Sciences, McGill University, Montreal, QC H3A 0C7, Canada.
2 Faculty of Dental Medicine and Oral Health Sciences, McGill University, Montreal, QC H3A 1G1, Canada.
Transglutaminases (TGs) are a family of protein cross-linking enzymes that are capable of stiffening and insolubilizing proteins and creating protein networks, and thereby altering biological functions of proteins. Their role in fibrosis progression has been widely investigated with a focus on kidney, lung, liver, and heart where activity is triggered by various stimuli including hypoxia, inflammation, and hyperglycemia. TG2 has been considered one of the key enzymes in the pathogenesis of fibrosis mainly through transforming growth factor beta (TGF-beta) signaling and matrix cross-linking mechanisms. Although TG2 has been most widely studied in this context, the involvement of other TGs, TG1 and Factor XIII-A (FXIII-A), is beginning to emerge. This mini-review highlights the major steps taken in the TG and fibrosis research and summarizes the most recent advances and contributions of TG2, TG1, and FXIII-A to the progression of fibrosis in various animal models. Also, their mechanisms of action as well as therapeutic prospects are discussed.
Our research would have not been possible without funding from: