@article{(Open Science Index):https://publications.waset.org/pdf/15615,
	  title     = {Evolutionary Origin of the αC Helix in Integrins},
	  author    = {B. Chouhan and  A. Denesyuk and  J. Heino and  M. S. Johnson and  K. Denessiouk},
	  country	= {},
	  institution	= {},
	  abstract     = {Integrins are a large family of multidomain α/β cell
signaling receptors. Some integrins contain an additional inserted I
domain, whose earliest expression appears to be with the chordates,
since they are observed in the urochordates Ciona intestinalis (vase
tunicate) and Halocynthia roretzi (sea pineapple), but not in integrins
of earlier diverging species. The domain-s presence is viewed as a
hallmark of integrins of higher metazoans, however in vertebrates,
there are clearly three structurally-different classes: integrins without
I domains, and two groups of integrins with I domains but separable
by the presence or absence of an additional αC helix. For example,
the αI domains in collagen-binding integrins from Osteichthyes
(bony fish) and all higher vertebrates contain the specific αC helix,
whereas the αI domains in non-collagen binding integrins from
vertebrates and the αI domains from earlier diverging urochordate
integrins, i.e. tunicates, do not. Unfortunately, within the early
chordates, there is an evolutionary gap due to extinctions between the
tunicates and cartilaginous fish. This, coupled with a knowledge gap
due to the lack of complete genomic data from surviving species,
means that the origin of collagen-binding αC-containing αI domains
remains unknown. Here, we analyzed two available genomes from
Callorhinchus milii (ghost shark/elephant shark; Chondrichthyes –
cartilaginous fish) and Petromyzon marinus (sea lamprey;
Agnathostomata), and several available Expression Sequence Tags
from two Chondrichthyes species: Raja erinacea (little skate) and
Squalus acanthias (dogfish shark); and Eptatretus burgeri (inshore
hagfish; Agnathostomata), which evolutionary reside between the
urochordates and osteichthyes. In P. marinus, we observed several
fragments coding for the αC-containing αI domain, allowing us to
shed more light on the evolution of the collagen-binding integrins.},
	    journal   = {International Journal of Biotechnology and Bioengineering},
	  volume    = {6},
	  number    = {5},
	  year      = {2012},
	  pages     = {300 - 303},
	  ee        = {https://publications.waset.org/pdf/15615},
	  url   	= {https://publications.waset.org/vol/65},
	  bibsource = {https://publications.waset.org/},
	  issn  	= {eISSN: 1307-6892},
	  publisher = {World Academy of Science, Engineering and Technology},
	  index 	= {Open Science Index 65, 2012},
	}