Disease relevance of Con

• Semaphorin-1a acts in concert with the cell adhesion molecules fasciclin II and connectin to regulate axon fasciculation in Drosophila [1].
• Proteins were extracted from rat pheochromocytoma cells, PC12, and various tissue of rat and bovine origin, and further purified by successive chromatography with Con A-Sepharose and anti-HRP glycopeptide antibody-Sepharose [2].

High impact information on Con

• This phenotype is suppressed by mutations in FasII and conn, two genes encoding cell adhesion molecules expressed on motor axons, suggesting that beat provides an antiadhesive function. beat encodes a novel secreted protein that is expressed by motoneurons during outgrowth [3].
• Connectin is expressed on the surface of eight muscles, the motoneurons that innervate them, and several glial cells along the pathways leading to them [4].
• Engrailed negatively regulates the expression of cell adhesion molecules connectin and neuroglian in embryonic Drosophila nervous system [5].
• The data suggest that Engrailed is normally a negative regulator of Connectin and neuroglian [5].
• While a previous study interpreted similar defects as indicating a repulsion role for connectin, we argue that the phenotypes are consistent with connectin's adhesion role [6].

Biological context of Con

• Connectin: a homophilic cell adhesion molecule expressed on a subset of muscles and the motoneurons that innervate them in Drosophila [4].
• A 4 kb DNA fragment, including the immunopurified binding site, is sufficient to reproduce the appropriate homeotic control within a subset of the full tissue distribution of connectin [7].
• Connectin, a target of homeotic gene control in Drosophila [7].
• This 110 bp fragment maps within a regulatory region of a gene under homeotic control, connectin [7].

Anatomical context of Con

• It has been demonstrated that the trunk visceral mesoderm parasegment is subdivided into at least two domains by connectin expression, which is regulated by Hedgehog and Wingless emanating from the ectoderm [8].
• The effect of Con A on the surface morphology of cultured cells of Drosophila melanogaster growing on coverglasses was examined by scanning electron microscopy [9].
• The extent of binding of Con A, WGA, s-WGA, and GSA-I A4 over the acrosomal region was greater than over nonacrosomal regions, indicating the concentration of alpha-mannose/alpha-glucose, beta-N-acetylglucosamine, and alpha-N-acetylgalactosamine residues in this area of the plasma membrane [10].
• These results reveal a repulsive function for Connectin during motoneuron growth cone guidance and synapse formation [11].
• We have shown that invertebrate connectin is also present in flexor muscle sarcomeres, although in very low abundance [12].

Associations of Con with chemical compounds

• Connectin contains a signal sequence, ten leucine-rich repeats, and a putative phosphatidylinositol membrane linkage; in S2 cells, connectin can mediate homophilic cell adhesion [4].
• The purification procedures involved ammonium sulfate fractionation, Con A-Sepharose 4B affinity chromatography, DEAE-Sepharose CL-6B ion exchange chromatography, Sephacryl S-200 gel filtration, and preparative gel electrophoresis [13].

Other interactions of Con

• As VM progenitors merge to form a continuous band running anterior to posterior along the embryo, expression of connectin (con) in 11 metameric patches within the VM reveals VM subdivisions analagous to ectodermal compartments [14].
• Titin/connectin is a giant muscle protein with a highly modular architecture consisting of multiple repeats of two sequence motifs, named type I and type II [15].

Analytical, diagnostic and therapeutic context of Con

• These morphologic effects were not apparent if Con A binding sites were blocked by preincubation with alpha-methyl-D-mannopyranoside before application to the cell cultures [9].
• 3. Purification of the more abundant 24 kD PSP variant was accomplished by Concanavalin A (Con A) sepharose B affinity chromatography followed by DEAE column chromatography [16].
• The distribution of alpha-D-mannose/alpha-D-glucose terminal residues in the plasma membrane of Drosophila melanogaster spermatozoon has been investigated by fluorescence and electron microscopy using concanavalin A (Con A) labeling [17].

References