MDGA1, an IgSF molecule containing a MAM domain, heterophilically associates with axon- and muscle-associated binding partners through distinct structural domains

Fujimura, Yuiko; Iwashita, Misato; Matsuzaki, Fumio; Yamamoto, Tohru

doi:10.1016/j.brainres.2006.05.030

Cited by 24 publications

(34 citation statements)

References 21 publications

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“…Moreover, our results indicate that MDGA1 may interact with this protein through its MAM domain, as cells expressing MAMGPI truncated protein exhibited a significant increase in cell-cell adhesion, compared to IgGPI expressing cells lacking the MAM domain. In the developing chicken nervous system it has been reported that MDGA1 is associated with axon-rich regions mainly through its MAM domain, suggesting that MDGA1 might function as an axon guidance molecule [4]. Furthermore, these authors report that this interaction is at least in part heterophilic in concordance with our results.…”

Section: Discussionsupporting

confidence: 92%

“…MDGA1 has been postulated as a member of the Ig superfamily (IgSF), the largest class of CAMs, and contains both a MAM domain and a GPI anchor [1][2][3][4][5][6]. The presence of these structural features makes it a unique protein, as it is the first GPI-linked IgSF molecule containing a MAM domain described to our knowledge.…”

Section: Introductionmentioning

confidence: 99%

“…Some of the GPIlinked IgSF proteins are involved in a variety of specific cell-cell interactions and/or in migration, such as LAMP, BIG-1, neurotrimin, CEPU-1, GP55 [7][8][9], CEA, CEACAM-6, NCAM p120 [10][11][12], F3/F11/contactin and TAG1/axonin-1 [13,14]. In addition, the presence of the MAM and/or Ig domains confers to these proteins the capacity to interact with other cells through homophilic and/or heterophilic interactions [2,4,15].…”

Section: Introductionmentioning

confidence: 99%

“…It has been reported that the MAM domain mediates lateral (cis) homophilic interactions in PTP μ and κ [15,23] and neuropilin-1 [24,25]. In the developing chicken nervous system MDGA1 heterophilically interacts with axon-rich regions mainly through its MAM domain, and with differentiating muscle through its Ig-repeat-containing Nterminal region [4].…”

Section: Introductionmentioning

confidence: 99%

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Expression of Human MDGA1 Increases Cell Motility and Cell-Cell Adhesion and Reduces Adhesion to Extracellular Matrix Proteins in MDCK Cells

Díaz‐López

Iniesta

Morán

et al. 2010

Cancer Microenvironment

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Characterization of the novel human protein MDGA1 (MAM Domain containing Glycosylphosphatidylinositol Anchor-1) has been reported in our laboratory in the past few years. hMDGA1 is a glycoprotein containing 955 aminoacids (137 kDa) attached to the eukaryotic cell membrane by a GPI (Glycosylphosphatidylinositol) anchor and localized specifically into membrane microdomains known as lipid rafts. Moreover, MDGA1 protein contains structural features found in different types of cell adhesion molecules (CAMs) such as the presence of immunoglobulin domains and a MAM domain (Meprin, A5 protein, receptor protein-tyrosine phosphatase μ), suggesting a role of MDGA1 in cell migration and/or adhesion. In order to investigate this aim, stable MDCK cell lines expressing MDGA1 or the truncated proteins IgGPI (lacking the MAM domain) and MAMGPI (lacking Ig domains) were generated. Our results reveal that MDGA1 increases the ability of MDCK cells to migrate, as it contains both Ig and MAM domains which have been implicated in cell motility. In addition, cell adhesion to extracellular matrix proteins, mainly to collagen IV, is reduced by MDGA1 and the IgGPI and MAMGPI truncated proteins. Accordingly, silencing MDGA1 by siRNA revealed a significant increase in adhesion to collagen IV. Furthermore, MDGA1 expression, through the intrinsic properties of the MAM domain, increases cell-cell adhesion independently of the cell monolayer used, suggesting that MDGA1 mediates cell-cell adhesiveness in a heterophilic manner.

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Section: Discussionsupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Expression of Human MDGA1 Increases Cell Motility and Cell-Cell Adhesion and Reduces Adhesion to Extracellular Matrix Proteins in MDCK Cells

Díaz‐López

Iniesta

Morán

et al. 2010

Cancer Microenvironment

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“…Expression plasmids for PLAP were prepared by inserting a PCR-amplified fragment of chick MDGA1 cDNA encoding its GPI-anchoring signal sequence (amino acids 916-949) (Fujimura et al 2006) into the XhoI site of AP-tag5 (Flanagan et al, 2000).…”

Section: Construction Of Expression Vectorsmentioning

confidence: 99%

Paths, elongation, and projections of ascending chick embryonic spinal commissural neurons after crossing the floor plate

Arakawa

Iwashita²,

Matsuzaki³

et al. 2008

Brain Research

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The paths of embryonic chick spinal commissural neurons originating from the lumbosacral (LS) 2 spinal segment and born around Hamburger-Hamilton stage (HH) 18 were observed by labeling the axons with an in ovo electroporation method designed to limit the electroporated area to ~ one somite length. After crossing the floor plate, these axons followed two major paths, one ventral and one dorsal, and a minor path running between the major ones. These axons reached the brachial region by HH28, passed through the cervical region at HH29, and entered the medullary area by HH30.The dorsal axons entered the developing cerebellum by HH33, crossed the midline again, and spread into the rostral-ipsilateral area of the developing cerebellum so that most of them were confined to lobules II-III by HH39. A small population of ventrally running axons turned to enter the cerebellum, and the rest entered the superior medullary velum between the cerebellum and the midbrain. The LS2-originating axons that ascended ipsilaterally into the cerebellum followed a single path, and their extension was delayed compared with that of the commissural axons. Some of the ipsilateral axons innervated the cerebellum; the rest entered the superior medullary velum. These direct observations of the formation of part of the spinocerebellar projections in chick will be a useful reference for future analyses of the underlying mechanisms.Section: Nervous System Development, Regeneration and Aging.

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Genomewide Association Analysis Followed by a Replication Study Implicates a Novel Candidate Gene for Neuroticism

Oord¹,

Kuo²,

Hartmann³

et al. 2008

Arch Gen Psychiatry

122

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MDGA1, an IgSF molecule containing a MAM domain, heterophilically associates with axon- and muscle-associated binding partners through distinct structural domains

Cited by 24 publications

References 21 publications

Expression of Human MDGA1 Increases Cell Motility and Cell-Cell Adhesion and Reduces Adhesion to Extracellular Matrix Proteins in MDCK Cells

Expression of Human MDGA1 Increases Cell Motility and Cell-Cell Adhesion and Reduces Adhesion to Extracellular Matrix Proteins in MDCK Cells

Paths, elongation, and projections of ascending chick embryonic spinal commissural neurons after crossing the floor plate

Genomewide Association Analysis Followed by a Replication Study Implicates a Novel Candidate Gene for Neuroticism

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