Disease relevance of SMOC2

• SMOC-2 adenovirus induced a 3-fold increase in the number of cells invading Matrigel plugs when compared with a control adenoviral vector [1].

High impact information on SMOC2

• SMAP2 colocalized with the adaptor proteins for clathrin AP-1 and EpsinR on the early endosomes/trans-Golgi-network (TGN) [2].
• SMAP2, a novel ARF GTPase-activating protein, interacts with clathrin and clathrin assembly protein and functions on the AP-1-positive early endosome/trans-Golgi network [2].
• Conversely, small interference RNA directed toward SMOC-2 inhibited network formation and proliferation [1].
• In microarray profiling experiments, a recombinant SMOC-2 adenovirus induced the expression of transcripts required for cell cycle progression in HUVECs [1].
• SMOC-2 was localized in the extracellular periphery of cultured human umbilical vein endothelial cells (HUVECs) [1].

Biological context of SMOC2

• The human and mouse SMOC-2 sequences are coded for by genes consisting of 13 exons located on chromosomes 6 and 17, respectively [3].
• The full-length cDNA of smap2 is 2914 base pairs long and contains an open reading frame of 1338 base pairs [4].
• The deduced amino acid sequence of smap2 contains two thyroglobulin type-1 domains, two EF-hand calcium-binding domains and putative signal peptide [4].

Anatomical context of SMOC2

• Identification of a novel smooth muscle associated protein, smap2, upregulated during neointima formation in a rat carotid endarterectomy model [4].

Associations of SMOC2 with chemical compounds

• Analysis of recombinantly expressed protein showed that SMOC-2 is a glycoprotein with a calcium-dependent conformation [3].

Analytical, diagnostic and therapeutic context of SMOC2

• Furthermore, we demonstrated that smap2 mRNA was upregulated during neointima formation in a rat carotid endarterectomy model [4].

References