Midkine

From Wikipedia, the free encyclopedia

Midkine (neurite growth-promoting factor 2)

PDB rendering based on 1mkc.

Available structures: 1mkc, 1mkn

Identifiers

Symbol(s)

MDK; MK; FLJ27379; NEGF2

External IDs

OMIM: 162096 MGI: 96949 HomoloGene: 1792

Gene ontology
Molecular Function:	• cytokine activity • growth factor activity • heparin binding
Cellular Component:	• extracellular region • extracellular space
Biological Process:	• regulation of progression through cell cycle • signal transduction • cell-cell signaling • multicellular organismal development • nervous system development • cell proliferation • response to wounding • cell differentiation • adrenal gland development

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001012333 (mRNA)
NP_001012333 (protein)

NM_001012335 (mRNA)
NP_001012335 (protein)

Location

Chr 11: 46.36 - 46.36 Mb

Chr 2: 91.73 - 91.73 Mb

Pubmed search

[1]

[2]

Midkine (MK, MDK), or Neurite Growth-promoting Factor 2, ^[1] is a basic heparin-binding growth factor of low molecular weight, a member of the NEGF family founded by Pleiotrophin (NEGF1, 46% homologous with MK). It is a nonglycosylated protein, composed of two domains held by disulfide bridges. It is a developmentally important retinoic acid-responsive gene product strongly induced during mid-gestation, hence the name midkine . Restricted mainly to certain tissues in the normal adult, it is strongly induced during oncogenesis, inflammation and tissue repair.

MK is pleiotropic, capable of exerting activities such as cell proliferation, cell migration, angiogenesis and fibrinolysis. A molecular complex containing receptor-type tyrosine phosphatase zeta (PTPζ), low density lipoprotein receptor-related protein (LRP), anaplastic leukemia kinase (ALK) and syndecans is considered to be its receptor.^[2]

[edit] References

^ http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=162096 NEGF2
^ Muramatsu Takashi (2002). "Midkine and pleiotrophin: two related proteins involved in development, survival, inflammation and tumorigenesis". J. Biochem. (Tokyo) 132 (3): 359–71. PMID 12204104.

[edit] Further reading

Uehara K, Matsubara S, Kadomatsu K, et al. (1992). "Genomic structure of human midkine (MK), a retinoic acid-responsive growth/differentiation factor.". J. Biochem. 111 (5): 563–7. PMID 1639750.
Wujek JR, Haleem-Smith H, Yamada Y, et al. (1991). "Evidence that the B2 chain of laminin is responsible for the neurite outgrowth-promoting activity of astrocyte extracellular matrix.". Brain Res. Dev. Brain Res. 55 (2): 237–47. PMID 1701366.
Kretschmer PJ, Fairhurst JL, Decker MM, et al. (1992). "Cloning, characterization and developmental regulation of two members of a novel human gene family of neurite outgrowth-promoting proteins.". Growth Factors 5 (2): 99–114. PMID 1768439.
Shoyab M, McDonald VL, Dick K, et al. (1991). "Amphiregulin-associated protein: complete amino acid sequence of a protein produced by the 12-0-tetradecanoylphorbol-13-acetate-treated human breast adenocarcinoma cell line MCF-7.". Biochem. Biophys. Res. Commun. 179 (1): 572–8. PMID 1883381.
Tsutsui J, Uehara K, Kadomatsu K, et al. (1991). "A new family of heparin-binding factors: strong conservation of midkine (MK) sequences between the human and the mouse.". Biochem. Biophys. Res. Commun. 176 (2): 792–7. PMID 2025291.
O'Hara B, Jenkins NA, Gilbert DJ, et al. (1995). "Chromosomal assignment of the heparin-binding cytokine genes MDK and PTN in mouse and man.". Cytogenet. Cell Genet. 69 (1-2): 40–3. PMID 7835084.
Kaname T, Kuwano A, Murano I, et al. (1993). "Midkine gene (MDK), a gene for prenatal differentiation and neuroregulation, maps to band 11p11.2 by fluorescence in situ hybridization.". Genomics 17 (2): 514–5. doi:10.1006/geno.1993.1359. PMID 8406506.
Fairhurst JL, Kretschmer PJ, Kovacs E, et al. (1993). "Structure of the gene coding for the human retinoic acid-inducible factor, MK.". DNA Cell Biol. 12 (2): 139–47. PMID 8471163.
Kojima T, Katsumi A, Yamazaki T, et al. (1996). "Human ryudocan from endothelium-like cells binds basic fibroblast growth factor, midkine, and tissue factor pathway inhibitor.". J. Biol. Chem. 271 (10): 5914–20. PMID 8621465.
Mahoney SA, Perry M, Seddon A, et al. (1996). "Transglutaminase forms midkine homodimers in cerebellar neurons and modulates the neurite-outgrowth response.". Biochem. Biophys. Res. Commun. 224 (1): 147–52. doi:10.1006/bbrc.1996.0998. PMID 8694802.
Nakanishi T, Kadomatsu K, Okamoto T, et al. (1997). "Expression of syndecan-1 and -3 during embryogenesis of the central nervous system in relation to binding with midkine.". J. Biochem. 121 (2): 197–205. PMID 9089390.
Iwasaki W, Nagata K, Hatanaka H, et al. (1998). "Solution structure of midkine, a new heparin-binding growth factor.". EMBO J. 16 (23): 6936–46. doi:10.1093/emboj/16.23.6936. PMID 9384573.
Ratovitski EA, Kotzbauer PT, Milbrandt J, et al. (1998). "Midkine induces tumor cell proliferation and binds to a high affinity signaling receptor associated with JAK tyrosine kinases.". J. Biol. Chem. 273 (6): 3654–60. PMID 9452495.
Maeda N, Ichihara-Tanaka K, Kimura T, et al. (1999). "A receptor-like protein-tyrosine phosphatase PTPzeta/RPTPbeta binds a heparin-binding growth factor midkine. Involvement of arginine 78 of midkine in the high affinity binding to PTPzeta.". J. Biol. Chem. 274 (18): 12474–9. PMID 10212223.
Meng K, Rodriguez-Peña A, Dimitrov T, et al. (2000). "Pleiotrophin signals increased tyrosine phosphorylation of beta beta-catenin through inactivation of the intrinsic catalytic activity of the receptor-type protein tyrosine phosphatase beta/zeta.". Proc. Natl. Acad. Sci. U.S.A. 97 (6): 2603–8. doi:10.1073/pnas.020487997. PMID 10706604.
Muramatsu H, Zou K, Sakaguchi N, et al. (2000). "LDL receptor-related protein as a component of the midkine receptor.". Biochem. Biophys. Res. Commun. 270 (3): 936–41. doi:10.1006/bbrc.2000.2549. PMID 10772929.
Kato M, Maeta H, Kato S, et al. (2001). "Immunohistochemical and in situ hybridization analyses of midkine expression in thyroid papillary carcinoma.". Mod. Pathol. 13 (10): 1060–5. doi:10.1038/modpathol.3880195. PMID 11048798.
Hayashi K, Kadomatsu K, Muramatsu T (2002). "Requirement of chondroitin sulfate/dermatan sulfate recognition in midkine-dependent migration of macrophages.". Glycoconj. J. 18 (5): 401–6. PMID 11925507.
Sumi Y, Muramatsu H, Takei Y, et al. (2002). "Midkine, a heparin-binding growth factor, promotes growth and glycosaminoglycan synthesis of endothelial cells through its action on smooth muscle cells in an artificial blood vessel model.". J. Cell. Sci. 115 (Pt 13): 2659–67. PMID 12077357.
Stoica GE, Kuo A, Powers C, et al. (2002). "Midkine binds to anaplastic lymphoma kinase (ALK) and acts as a growth factor for different cell types.". J. Biol. Chem. 277 (39): 35990–8. doi:10.1074/jbc.M205749200. PMID 12122009.