NDLI: Evolution of immunoglobulin light chains: cDNA clones specifying sandbar shark constant regions.

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Evolution of immunoglobulin light chains: cDNA clones specifying sandbar shark constant regions.

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Evolution of immunoglobulin light chains: cDNA clones specifying sandbar shark constant regions.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Marchalonis, J. J. Schluter, S. F. Hohman, V. S. Edmundson, A. B.
Description	Author Affiliation: Schluter SF ( Department of Microbiology and Immunology, University of Arizona, College of Medicine, Tucson 85724.);
Abstract	Sharks are living fossils that are indistinguishable morphologically from their Devonian ancestors of approximately equal to 400 million years ago. If parallel conservatism characterizes their biochemical evolution, characterization of their immunoglobulin chains could provide information regarding the primordial features of these essential defense molecules. Shark immunoglobulins are polydisperse like those of mammals, but these species lack homogeneous myeloma proteins. This heterogeneity has precluded direct determination of the sequence of elasmobranch light-chain proteins. We have sequenced four cDNA clones that contain the constant-region sequence as well as varying degrees of variable- or joining-region segments. The sandbar shark (Carcharhinus plumbeus) has at least four distinct light-chain constant regions, and these can be considered homologs of mammalian lambda chains. Approximately 40% identity was found in comparison from sharks to mammals. Certain stretches of sequence were remarkably conserved, whereas others varied in a manner consistent with accepted concepts of speciation. One hexapeptide (Ala-Thr-Leu-Val-Cys-Leu) occurred in lambda constant regions of all vertebrate species. There was a universal conservation of certain cysteines, phenylalanines, tryptophans, and glycines and strong identities in the block of residues from Ser-176 to Trp-186. Comparison of the shark sequence with that of the characterized human lambda myeloma protein Mcg indicates a strong conservation of three-dimensional structure in this light-chain domain representing species whose ancestors diverged early in vertebrate evolution. The shark light-chain sequence contains primordial features shared by mammalian kappa and lambda chains and by T-cell receptor beta chains.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	24
Volume Number	86
Language	English
Publisher	National Academy of Sciences
Publisher Date	1989-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Biological Evolution Cloning, Molecular Genes, Immunoglobulin Immunoglobulin Constant Regions Genetics Immunoglobulin Light Chains Amino Acid Sequence Animals Cross Reactions DNA Fossils Gene Library Immune Sera Mice Models, Structural Molecular Sequence Data Protein Conformation Receptors, Antigen, B-Cell Sequence Homology, Nucleic Acid Immunology Comparative Study Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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