EMB Membrane Protein Introduction

Introduction of EMB

EMB is encoded by the EMB gene which is located at 5q11.1. Embigin belongs to the immunoglobulin superfamily expressed in embryonic cells and originally identified to express during mouse embryogenesis. Embigin is also detected in cancer cell lines, such as breast cancer cells MDA-MB-231 and MCF7. And EMB is highly glycosylated in embryonal carcinoma cells, the molecular weight is about 30 KDa, but the glycosylated form has a molecular mass of 62-90 KDa.

Function of EMB Membrane Protein

EMB is a single-pass type I membrane protein, with its N-terminus on the extracellular side of the membrane and removal of its signal sequence. EMB can be detected in many tissues including heart, liver, lung, and brain, and involved in prostate and mammary gland development. Accordingly, it also expressed in mammalian skeletal muscle. EMB can enhance cell-substratum adhesion which is Ca²⁺ dependent and inhibited by an arginine-glycine-aspartic acid peptide and by anti-integrin antiserum. EMB also serves as a carrier of a developmentally regulated carbohydrate marker found in early embryonic cells. Beyond that, EMB is transcriptionally regulated by Homeobox C8 (HOXC8) in breast cancer cells and EMB expression suppresses breast tumorigenesis. HOXC8-EMB pathway is involved in proliferation, anchorage-independent cell growth and migration of breast cancer cells. Besides, EMB enhances neural cell adhesion molecule-dependent neuromuscular adhesion and thereby modulates neuromuscular junction formation and plasticity. It perhaps plays a role in targeting the monocarboxylate transporters SLC16A1 and SLC16A7 to the cell membrane.

Fig.1 Comparison of the structures of Neuroplastin, Basigin, and EMB. (Fong, 2018)

Application of EMB Membrane Protein in Literature

1. Jung D. E., et al. Embigin is overexpressed in pancreatic ductal adenocarcinoma and regulates cell motility through epithelial to mesenchymal transition via the TGF‐β pathway. Molecular Carcinogenesis. 2016, 55(5): 633. PubMed ID: 25773908
   
   

   This article reports for the first time that EMB expression is elevated in PDAC, It can also regulate cell motility through epithelial to mesenchymal transition via the TGF-β pathway. Authors propose that therapeutic targeting of EMB may contribute to the repression of pancreatic cancer progression.

2. Lain E., et al. A Novel Role for Embigin to Promote Sprouting of Motor Nerve Terminals at the Neuromuscular Junction. Journal of Biological Chemistry. 2009, 284(13): 8930-9. PubMed ID: 19164284
   
   

   This article reveals that EMB enhances neural cell adhesion molecule-dependent neuromuscular adhesion and thereby modulates neuromuscular junction formation and plasticity.

3. Chao F., et al. Embigin, Regulated by HOXC8, Plays a Suppressive Role in Breast Tumorigenesis. Oncotarget. 2015, 6(27): 23496-23509. PubMed ID: 26090721
   
   

   This article suggests that EMB is transcriptionally regulated by HOXC8 protein and its low/loss expression may play an important role in the progression of breast cancers. EMB can be used for a prognostic biomarker in breast cancers, at least the subset of breast basal-like cancers.

4. Huang R. P., et al. Embigin, a member of the immunoglobulin superfamily expressed in embryonic cells, enhances cell-substratum adhesion. Developmental Biology. 1993, 155(2): 307-14. 8432389
   
   

   Authors in this article introduced an EMB cDNA under the control of the β-actin promoter and Rous sarcoma virus enhancer into L cells to explore EMB function. They found that one role of EMB appears to be the promotion of integrin-mediated cell-substratum adhesion.

5. Little N. Characterization of Basigin and the Interaction Between Embigin and Monocarboxylate Transporter-1, -2, and -4 (MCT1, MCT2, MCT4) in the Mouse Brain. Investigative Ophthalmology. 2011, 12(10): 771-6.
   
   

   This article reveals that the cell adhesion molecules Basigin and EMB may be co-expressed in the same cells as the MCT2 and MCT4 transporter proteins. What’ s more, EMB transmembrane domain does not interact with the MCTs. The data suggest that MCTs do not require Basigin or EMB for plasma membrane expression in mouse brain.

EMB Preparation Options

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Reference

1. Fong and Joseph D., (2018) "The Distinction of the Interactions Between the Transmembrane Domains of Basigin Gene Products and Monocarboxylate Transporters". UNF Graduate Theses and Dissertations. 788.

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