Dimerization of Midkine by Tissue Transglutaminase and Its Functional Implication

Kojima, Soichi; Inui, Tatsuya; Muramatsu, Hisako; Suzuki, Yohko; Kadomatsu, Kenji; Yoshizawa, Misako; Hirose, Shigehisa; Kimura, Terutoshi; Sakakibara, Shumpei; Muramatsu, Takashi

doi:10.1074/jbc.272.14.9410

Cited by 94 publications

(71 citation statements)

References 51 publications

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“…The biological activity of TG2 has been implicated in extracellular matrix organization (1), activation of cytokines and growth factors such as transforming growth factor-β (19) and midkine (18). As shown in Fig.…”

Section: Measurement Of Tg2 Activity After the Digitonin/ Discussionmentioning

confidence: 99%

Effect of retinoic acid-induced transglutaminase on cell growth in regenerating liver

et al. 2006

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Transglutaminase 2 (TG2) is implicated in the inhibitory regulation of the hepatocyte growth in vitro. In vivo, however, the role of TG2 in liver regeneration after partial hepatectomy (PH) is almost unknown. A dramatic increase of TG2 expression and activation is induced by retinoic acid (RA). Here we show the effect of the RA-induced overexpression of TG2 on liver regeneration after PH. Regenerating rat liver was prepared by 70% PH. RA was intraperitoneally injected immediately after PH. TG2 activity was determined by incorporation of 14 C-putrescine into dimethylcasein. Cell cycle was evaluated for incorporation of BrdU into hepatocytes and detected by a flow cytometric analysis. The treatment of RA greatly increased TG2 activity at 1 day after PH. At that time, DNA synthesis was significantly reduced by the treatment of RA. The recovery of liver weight after PH was significantly delayed by the treatment of RA. These results suggested that TG2 was involved in growth capacity in regenerating rat liver after PH.Liver regeneration following 70% partial hepatectomy (PH) leads to rapid restoration and gains its lost mass within a week after surgery. Liver regeneration is regulated by several factors, including cytokines (9), growth factors (20), and post-translational modifications of several proteins (4, 6). Transglutaminase 2 (TG2; EC 2.3.2.13) catalyzes Ca 2+

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Section: Measurement Of Tg2 Activity After the Digitonin/ Discussionmentioning

confidence: 99%

Effect of retinoic acid-induced transglutaminase on cell growth in regenerating liver

et al. 2006

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“…The bands of 100 and ϳ66 kDa appeared also in controls and were nonspecific. The cross-linked 130-kDa band was broad, partly due to the broad nature of neuroglycan C before cross-linking and probably also due to the fact that in addition to MK monomer, its dimer is present in significant amounts (34) and may be involved in binding to NGC. Similar results were obtained from cross-linking of MK-HA to NGC-III (data not shown).…”

Section: Binding Of Ngc-i and Ngc-iii To Mk-mentioning

confidence: 99%

Neuroglycan C Is a Novel Midkine Receptor Involved in Process Elongation of Oligodendroglial Precursor-like Cells

Ichihara-Tanaka

Oohira

Rumsby

et al. 2006

Journal of Biological Chemistry

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Midkine is a heparin-binding growth factor that promotes cell attachment and process extension in undifferentiated bipolar CG-4 cells, an oligodendroglial precursor cell line. We found that CG-4 cells expressed a non-proteoglycan form of neuroglycan C, known as a part-time transmembrane proteoglycan. We demonstrated that neuroglycan C before or after chondroitinase ABC treatment bound to a midkine affinity column. Neuroglycan C lacking chondroitin sulfate chains was eluted with 0.5 M NaCl as a major fraction from the column. We confirmed that CG-4 cells expressed two isoforms of neuroglycan C, I, and III, by isolating cDNA. Among three functional domains of the extracellular part of neuroglycan C, the chondroitin sulfate attachment domain and acidic amino acid cluster box domain showed affinity for midkine, but the epidermal growth factor domain did not. Furthermore, cell surface neuroglycan C could be cross-linked with soluble midkine. Process extension on midkine-coated dishes was inhibited by either a monoclonal antineuroglycan C antibody C1 or a glutathione S-transferase-neuroglycan C fusion protein. Finally, stable transfectants of B104 neuroblastoma cells overexpressing neuroglycan C-I or neuroglycan C-III attached to the midkine substrate, spread well, and gave rise to cytoskeletal changes. Based on these results, we conclude that neuroglycan C is a novel component of midkine receptors involved in process elongation. Midkine (MK),2 a heparin-binding growth factor, is strongly expressed at the mid-embryonic stage of development and is preferentially expressed in the kidney after birth (1, 2). MK is a 13-kDa protein with about 50% sequence identity to pleiotrophin (PTN), which is also called heparin-binding growth-associated molecule (3, 4). MK promotes neurite outgrowth and migration in neuronal cells isolated from the embryonic brain (5-7) and prevents apoptosis (8, 9). MK also promotes the migration of inflammatory leukocytes (10) and thereby plays a key role in the etiology of neointima formation (10), renal injury (11, 12), rheumatoid arthritis (13), and intraperitoneal adhesion after surgery (14). So far, protein-tyrosine phosphatase (7, 15), anaplastic lymphoma kinase (16), low density-lipoprotein receptor-related protein-1 (17), low density lipoprotein receptor-related protein 6 (9), and integrin ␣4␤1 and ␣6␤1 (18) have been identified as MK receptors. These molecules cooperate during MK signaling, possibly as a receptor complex (18). However, not all the molecules serving as MK receptors have been clarified. Importantly, we do not know whether a function specific to a class of cells such as neurite extension requires another receptor to transmit the specific signal or not. Here, we report that a cell surface molecule is specifically expressed in the nervous system as a component of the MK receptor in cells extending processes.When undifferentiated CG-4 cells, an oligodendrocyte precursor cell line, are cultured on dishes coated with MK or PTN, they quickly extend processes and adopt bipolar shapes ...

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“…Both midkine (Kojima et al, 1997) and vitronectin (Sane et al, 1990) are much more readily cross-linked by TG in the presence of sulfaterich glycosaminoglycans. Interestingly, the content of sulfated glycosaminoglycans is reduced in the cap of the unstable plaque (Davies et al, 1994).…”

Section: Tg In Atherosclerosismentioning

confidence: 99%

Localization of Tissue Transglutaminase in Human Carotid and Coronary Artery Atherosclerosis: Implications for Plaque Stability and Progression

Haroon

Wannenburg

Gupta

et al. 2001

Laboratory Investigation

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SUMMARY:Although atherosclerosis progresses in an indolent state for decades, the rupture of plaques creates acute ischemic syndromes that may culminate in myocardial infarction and stroke. Mechanical forces and matrix metalloproteinase activity initiate plaque rupture, whereas tissue inhibitors of metalloproteinases have an important (albeit indirect) role in plaque stabilization. In this paper, an enzyme that could directly stabilize the plaque is described. Tissue transglutaminase (TG) catalyzes the formation of ⑀(␥-glutamyl)lysine isopeptide bonds that are resistant to enzymatic, mechanical, and chemical degradation. We performed immunohistochemistry for TG in atherosclerotic human coronary and carotid arteries. TG was most prominent along the luminal endothelium and in the medium of the vessels with a distribution mirroring that of smooth muscle cells. Variable, often prominent, immunoreactivity for TG was also seen in the intima, especially in regions with significant neovascularization. Additionally, TG was detected in fibrous caps and near the "shoulder regions" of some plaques. A monoclonal antibody to the transglutaminase product ⑀(␥-glutamyl)lysine isopeptide demonstrated co-localization with TG antigen. Transglutaminase activity was found in 6 of 14 coronary artery atherectomy samples. Cross-linking of TG substrates such as fibrinogen, fibronectin, vitronectin, collagen type I, and protease inhibitors stabilized the plaque. Furthermore, the activation of transforming growth factor-beta-1 by TG might be an additional mechanism for the promotion of plaque stabilization and progression by increasing the synthesis of extracellular matrix components. (Lab Invest 2001, 81:83-93).

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Dimerization of Midkine by Tissue Transglutaminase and Its Functional Implication

Abstract: Midkine (MK),Tissue type II transglutaminase (R-glutaminylpeptide: amine ␥-glutamyltransferase, EC 2.3.2.13) is a member of the transglutaminase family that catalyzes Ca 2ϩ

Cited by 94 publications

References 51 publications

Effect of retinoic acid-induced transglutaminase on cell growth in regenerating liver

Effect of retinoic acid-induced transglutaminase on cell growth in regenerating liver

Neuroglycan C Is a Novel Midkine Receptor Involved in Process Elongation of Oligodendroglial Precursor-like Cells

Localization of Tissue Transglutaminase in Human Carotid and Coronary Artery Atherosclerosis: Implications for Plaque Stability and Progression

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