Disease relevance of DCBLD2

• Significant up-regulation of a novel gene, CLCP1, in a highly metastatic lung cancer subline as well as in lung cancers in vivo [1].

High impact information on DCBLD2

• Northern blot analysis showed that ESDN mRNA was expressed in various tissues; particularly highly expressed in cultured vascular smooth muscle cells [2].
• A novel cDNA has been isolated from primary culture of human coronary arterial cells by a signal sequence trap method, and designated ESDN (endothelial and smooth muscle cell-derived neuropilin-like molecule) [2].
• Overexpression of ESDN in 293T cells suppressed their bromodeoxyuridine uptake [2].
• Thus, ESDN is considered to play a role in regulation of vascular cell growth and may have a wide variety of functions in other tissues including the nervous system, like neuropilins [2].
• The ESDN expression was up-regulated in platelet-derived growth factor-BB-stimulated vascular smooth muscle cells in vitro and neointima of the balloon-injured carotid artery in vivo [2].

Anatomical context of DCBLD2

• The number of CLCP molecules adsorbed per yeast cell and the loss of colony-forming units are described by an exponential relationship [3].
• Human neutrophils contain a chymotrypsin-like cationic protein (CLCP) that binds to the surface of Candida parapsilosis and is preferentially adsorbed by yeasts mixed with unfractionated extracts of neutrophil granules [3].

Associations of DCBLD2 with chemical compounds

• Irreversible inhibition of the enzymatic site of CLCP by phenylmethylsulfonylfluoride or N-acetyl-Ala-Ala-Phe-chloromethyl ketone did not affect its adsorption by yeast [3].

Regulatory relationships of DCBLD2

• Immunoprecipitation experiments confirmed interaction of CLCP1 with SEMA4B, regulation of CLCP1 protein by ubiquitination and proteasome degradation enhanced in the presence of SEMA4B [4].

References