Regular ArticleCloning and Expression of VEMA: A Novel Ventral Midline Antigen in the Rat CNS
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Early eukaryotic origins and metazoan elaboration of MAPR family proteins
2020, Molecular Phylogenetics and EvolutionCitation Excerpt :Reviews have been published on neural and cancer functions of MAPR (Cahill et al., 2016a; Kimura et al., 2012; Kimura et al., 2013; Petersen et al., 2013a, b), their interactions with cytochrome P450 proteins (Ryu et al., 2017), and as potential drug targets (Hasegawa et al., 2016). Under the synonym ventral midline antigen A (VEMA) PGRMC1 was identified as directing early embryonic nerve cord axon guidance (Runko and Kaprielian, 2002, 2004; Runko et al., 1999). Both NENF and NEUFC were identified as secreted neurotrophic factors with extracellular heme-binding MAPR domains (Kimura et al., 2010; Kimura et al., 2005), but can be post-translationally modified in a manner consistent with a cytoplasmic topology for the MAPR domain (Cahill and Medlock, 2017), and the NEUFC MAPR domain is cytoplasmic in HeLa cells (Bruce and Rybak, 2014).
The emerging role of progesterone receptor membrane component 1 (PGRMC1) in cancer biology
2016, Biochimica et Biophysica Acta - Reviews on CancerCitation Excerpt :To understand this concept, we now below consider evidence that PGRMC1 is involved in vesicle trafficking. Runko et al., cloned rat PGRMC1 as a ventral midline antigen (which they called VEMA) that was involved in axon guidance in the developing rat central neural system [83]. They later showed that the Caenorhabditis elegans homologue to PGRMC1, which they called Vem-1, played a conserved role in nematode embryological axon guidance, where VEM-1 interacted with a cell surface protein related to the mammalian netrin receptors deleted in colorectal cancer (DCC) and neogenin [84].
PGRMC2, a yet uncharacterized protein with potential as tumor suppressor, migration inhibitor, and regulator of cytochrome P450 enzyme activity
2013, SteroidsCitation Excerpt :No functional studies were carried out in this study, so that the function of PGRMC2 in pigs remains obscure. Variants of PGRMC2 were identified which were named VemaB in rat and mouse, and Vem-1 in Caenorhabditis elegans [24–27]. The protein was shown to be localized to midline-associated targets in the developing rodent brain [25,26].
Candidates for membrane progestin receptors-Past approaches and future challenges
2008, Comparative Biochemistry and Physiology - C Toxicology and PharmacologyThe membrane-associated progesterone-binding protein 25-Dx: Expression, cellular localization and up-regulation after brain and spinal cord injuries
2008, Brain Research ReviewsCitation Excerpt :From its structure, IZAg was classed as a member of a protein family containing a heme-binding domain, and progesterone was proposed to be a ligand of this domain (Min et al., 2005). In 1999, Runko et al. identified a protein in the developing rat nervous system that is similar to 25-Dx (Runko et al., 1999). This study reported the protein as a novel, ventral, midline-associated protein, termed VEMA (ventral midline antigen) and suggested a role for it in regulating axon guidance.
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