| First Author | Krejci E | Year | 1997 |
| Journal | J Biol Chem | Volume | 272 |
| Issue | 36 | Pages | 22840-7 |
| PubMed ID | 9278446 | Mgi Jnum | J:54000 |
| Mgi Id | MGI:1333982 | Doi | 10.1074/jbc.272.36.22840 |
| Citation | Krejci E, et al. (1997) The mammalian gene of acetylcholinesterase-associated collagen. J Biol Chem 272(36):22840-7 |
| abstractText | The collagen-tailed or asymmetric forms (A) represent a major component of acetylcholinester-ase (AChE) in the neuromuscular junction of higher vertebrates. They are hetero-oligomeric mol-ecules, in which tetramers of catalytic subunits of type T (AChET) are attached to the subunits of a triple-stranded collagen tail. We report the cloning of a rat AChE-associated collagen subunit, Q. We show that collagen tails are encoded by a single gene, COLQ. The ColQ subunits form homotrimers and readily form collagen-tailed AChE, when coexpressed with rat AChET. We found that the same ColQ subunits are incorporated, in vivo, in asymmetric forms of both AChE and butyrylcholinester-ase. A splice variant from the COLQ gene encodes a proline- rich AChE attachment domain without the collagen domain but does not represent the membrane anchor of the brain tetramer. The COLQ gene is expressed in cholinergic tissues, brain, muscle, and heart, and also in noncholinergic tissues such as lung and testis. |
