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Gene Review

Grem1  -  gremlin 1

Rattus norvegicus

Synonyms: Cktsf1b1, Cysteine knot superfamily 1, BMP antagonist 1, Down-regulated in Mos-transformed cells protein, Drm, Gremlin-1, ...
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Disease relevance of Grem1

  • The toxic effects of drm can be overcome by cotransfection with constructs expressing oncogenic ras; furthermore, cells expressing high levels of drm and conditionally transformed with mos-expressing Moloney murine sarcoma virus rapidly undergo apoptosis when shifted to the nonpermissive temperature [1].

High impact information on Grem1

  • Transfection of a drug-selectable drm expression vector dramatically reduced the efficiency of colony formation in REF-1 and CHO cells, and the drm-transfected REF-1 survivors expressed low or nondetectable levels of exogenous drm mRNA [1].
  • The drm cDNA contains a 184-amino-acid-protein-encoding open reading frame which shows no significant homologies to known genes in DNA databases [1].
  • In situ hybridization analysis in adult rat tissue reveals good correlation with this pattern and indicates that drm mRNA is most highly expressed in nondividing and terminally differentiated cells, such as neurons, type 1 lung cells, and goblet cells [1].
  • Northern analysis of normal adult tissues shows that drm is expressed as a 4.4-kb message in a tissue-specific manner, with high expression in the brain, spleen, kidney, and testis and little or no expression in the heart, liver, and skeletal muscle [1].
  • Taken together, our data suggest that cells expressing high levels of drm undergo apoptotic death in the absence of oncogene-induced transformation and that drm represents a novel gene with potential roles in cell growth control or viability and tissue-specific differentiation [1].

Biological context of Grem1

  • Thus, the results identify that Drm and Dan can interact with Slit proteins and act as inhibitors of monocyte chemotaxis, demonstrating a previously unidentified biological role for these proteins [2].
  • Drm binding to Slits depends on its glycosylation and is not interfered with by bone morphogenic proteins [2].
  • Analysis of different oncogene-transformed cells revealed that drm gene expression was also suppressed in REF-1 cells transformed by v-ras, v-src, v-raf, and v-fos [1].
  • Both forms of Drm are able to undergo phosphorylation [3].

Anatomical context of Grem1

  • Importantly, Drm and Dan function as inhibitors for monocyte migration induced by stromal cell-derived factor 1alpha (SDF-1alpha) or fMLP [2].
  • Confocal immunofluorescent microscopy indicates that Drm is present both on the external surface of expressing cells, as well as within the endoplasmic reticulum and the Golgi [3].
  • We have investigated the biosynthesis and processing of Drm expressed endogenously in rat fibroblasts or overexpressed following transient or stable transfection [3].


  1. Identification of drm, a novel gene whose expression is suppressed in transformed cells and which can inhibit growth of normal but not transformed cells in culture. Topol, L.Z., Marx, M., Laugier, D., Bogdanova, N.N., Boubnov, N.V., Clausen, P.A., Calothy, G., Blair, D.G. Mol. Cell. Biol. (1997) [Pubmed]
  2. Cutting edge: bone morphogenetic protein antagonists Drm/Gremlin and Dan interact with Slits and act as negative regulators of monocyte chemotaxis. Chen, B., Blair, D.G., Plisov, S., Vasiliev, G., Perantoni, A.O., Chen, Q., Athanasiou, M., Wu, J.Y., Oppenheim, J.J., Yang, D. J. Immunol. (2004) [Pubmed]
  3. Biosynthesis, post-translation modification, and functional characterization of Drm/Gremlin. Topol, L.Z., Bardot, B., Zhang, Q., Resau, J., Huillard, E., Marx, M., Calothy, G., Blair, D.G. J. Biol. Chem. (2000) [Pubmed]
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