Disease relevance of CPAMD8

• A new vasoactive intestinal peptide antagonist discriminates VIP receptors on guinea pig trachea and human neuroblastoma cells [1].

High impact information on CPAMD8

• In this study we demonstrate a novel function for adducin; it completely blocks elongation and depolymerization at the barbed (fast growing) ends of actin filaments, thus functioning as a barbed end capping protein (Kcap approximately 100 nM) [2].
• The Kazal domain of CPAMD8 binds to heparin, and subcellular fractionation shows that CPAMD8 is membrane associated via ionic interaction [3].
• In addition, CPAMD8 has a Kazal-type serine proteinase inhibitor/follistatin-like domain at the C-terminus [3].
• Thus, CPAMD8 may, like other members of the C3/alpha(2)M family, function in innate immunity but in a localized manner [3].
• RT-PCR and immunoblot assays showed that CPAMD8 is expressed in a number of human tissues, most abundantly in the kidney, brain, and testis and at lower levels in heart, liver, and small intestine [3].

Biological context of CPAMD8

• The deduced amino acid sequence of this putative FAOMeT protein contained two copies of a conserved approximately 135 amino acid domain we term the CF (CPAMD8/FAOMeT) domain; single copies of this domain also occur in the human CPAMD8 protein (a member of the alpha-2 macroglobulin family) and an uncharacterized Drosophila protein [4].
• Gene expression and transcript size of the prepro-peptide VIP/PHM-27 in normal human tissue [5].

Anatomical context of CPAMD8

• VIP/PHM-27 transcript in human brain and gut was a single band of 1.7 kb; by contrast, a 7.0-kb transcript was detected in striated skeletal muscle [5].

Analytical, diagnostic and therapeutic context of CPAMD8

• The intact CPAMD8 protein generated by in vitro transcription and translation resolved as a single band of about 200 kDa on SDS-PAGE [3].

References