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      Midkine, a heparin-binding cytokine with multiple roles in development, repair and diseases

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          Abstract

          Midkine is a heparin-binding cytokine or a growth factor with a molecular weight of 13 kDa. Midkine binds to oversulfated structures in heparan sulfate and chondroitin sulfate. The midkine receptor is a molecular complex containing proteoglycans. Midkine promotes migration, survival and other activities of target cells. Midkine has about 50% sequence identity with pleiotrophin. Mice deficient in both factors exhibit severe abnormalities including female infertility. In adults, midkine is expressed in damaged tissues and involved in the reparative process. It is also involved in inflammatory reactions by promoting the migration of leukocytes, induction of chemokines and suppression of regulatory T cells. Midkine is expressed in a variety of malignant tumors and promotes their growth and invasion. Midkine appears to be helpful for the treatment of injuries in the heart, brain, spinal cord and retina. Midkine inhibitors are expected to be effective in the treatment of malignancies, rheumatoid arthritis, multiple sclerosis, renal diseases, restenosis, hypertension and adhesion after surgery.

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          Midkine and pleiotrophin: two related proteins involved in development, survival, inflammation and tumorigenesis.

          Takashi Muramatsu (2002)
          Midkine (MK) and pleiotrophin (PTN) are low molecular weight proteins with closely related structures. They are mainly composed of two domains held by disulfide bridges, and there are three antiparallel beta-sheets in each domain. MK and PTN promote the growth, survival, and migration of various cells, and play roles in neurogenesis and epithelial mesenchymal interactions during organogenesis. A chondroitin sulfate proteoglycan, protein-tyrosine phosphatase zeta (PTPzeta), is a receptor for MK and PTN. The downstream signaling system includes ERK and PI3 kinase. MK binds to the chondroitin sulfate portion of PTPzeta with high affinity. Among the various chondroitin sulfate structures, the E unit, which has 4,6-disulfated N-acetylgalactosamine, provides the strongest binding site. The expression of MK and PTN is increased in various human tumors, making them promising as tumor markers and as targets for tumor therapy. MK and PTN expression also increases upon ischemic injury. MK enhances the migration of inflammatory cells, and is involved in neointima formation and renal injury following ischemia. MK is also interesting from the viewpoints of the treatment of neurodegenerative diseases, increasing the efficiency of in vitro development, and the prevention of HIV infection.
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            Cloning and expression of a developmentally regulated protein that induces mitogenic and neurite outgrowth activity.

            M. Watson, S. Li, Andrew R. Hoffman … (1990)
            A heparin binding mitogenic protein isolated from bovine uterus shares NH2-terminal amino acid sequence with a protein isolated from newborn rat brain. The cDNA's of the bovine, human, and rat genes have been isolated and encode extraordinarily conserved proteins unrelated to known growth or neurotrophic factors, although identity of nearly 50 percent has been found with the predicted sequence of a retinoic acid induced transcript in differentiating mouse embryonal carcinoma cells. Lysates of COS-7 cells transiently expressing this protein were mitogenic for NRK cells and initiated neurite outgrowth from mixed cultures of embryonic rat brain cells. RNA transcripts encoding this protein were widely distributed in tissues and were developmentally regulated. This protein, previously designated as heparin binding growth factor (HBGF)-8, is now renamed pleiotrophin (PTN) to reflect its diverse activities. PTN may be the first member of a family of developmentally regulated cytokines.
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              Midkine binds to anaplastic lymphoma kinase (ALK) and acts as a growth factor for different cell types.

              Gerald E Stoica, Angera H Kuo, BENJAMIN POWERS … (2002)
              Midkine (MK) is a developmentally regulated, secreted growth factor homologous to pleiotrophin (PTN). To investigate the potential role of MK in tumor growth, we expressed MK in human SW-13 cells and studied receptor binding, signal transduction, and activity of MK. The MK protein stimulates soft agar colony formation in vitro and tumor growth of SW-13 cells in athymic nude mice, as well as proliferation of human endothelial cells from brain microvasculature and umbilical vein (HUVEC) in the low ng/ml range. MK binds to anaplastic lymphoma kinase (ALK), the receptor for PTN, with an apparent K(d) of 170 pm in intact cells, and this receptor binding of MK is competed by PTN with an apparent K(d) of approximately 20 pm. Monoclonal antibodies raised against the extracellular ligand-binding domain of ALK inhibit ALK receptor binding of MK as well as MK-stimulated colony formation of SW-13 cells. Furthermore, MK stimulates ALK phosphorylation in WI-38 human fibroblasts and activates PI3-kinase and MAP kinase signal transduction in WI-38, HUVEC, neuroblastoma (SH SY-5Y) and glioblastoma (U87MG) cells that express the ALK protein. We conclude that MK can act as a growth, survival, and angiogenic factor during tumorigenesis and signals through the ALK receptor.
              Article 0 comments Cited 68 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Proc Jpn Acad Ser B Phys Biol Sci
                Journal ID (iso-abbrev): Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci
                Journal ID (publisher-id): PJAB
                Title: Proceedings of the Japan Academy. Series B, Physical and Biological Sciences
                Publisher: The Japan Academy (Tokyo, Japan )
                ISSN (Print): 0386-2208
                ISSN (Electronic): 1349-2896
                Publication date (Print): April 2010
                Volume: 86
                Issue: 4
                Pages: 410-425
                Affiliations
                [*1 ]Department of Health Science, Faculty of Psychological and Physical Science, Aichi Gakuin University, Aichi, Japan
                Author notes
                [† ]Correspondence should be addressed: T. Muramatsu, Department of Health Science, Faculty of Psychological and Physical Science, Aichi Gakuin University, 12 Araike, Iwasaki-cho, Nisshin, Aichi 470-0195, Japan (e-mail: tmurama@ 123456dpc.agu.ac.jp ).

                Communicated by Takao S ekiya, m.j.a.

                Article
                Publisher ID: pjab-86-410
                DOI: 10.2183/pjab.86.410
                PMC ID: 3417803
                PubMed ID: 20431264
                SO-VID: bcf2ef3b-98eb-423e-a497-276284941e3a
                Copyright © © 2010 The Japan Academy
                License:

                This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 25 November 2009
                Date accepted : 24 February 2010
                Categories
                Subject: Review

                ScienceOpen disciplines: Life sciences
                Keywords: proteoglycans,inflammation,midkine,cancer,pleiotrophin,repair
                Data availability:
                ScienceOpen disciplines: Life sciences
                Keywords: proteoglycans, inflammation, midkine, cancer, pleiotrophin, repair

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