Four primordial immunoglobulin light chain isotypes, including lambda and kappa, identified in the most primitive living jawed vertebrates.

Department of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
European Journal of Immunology (Impact Factor: 4.52). 11/2007; 37(10):2683-94. DOI: 10.1002/eji.200737263
Source: PubMed

ABSTRACT The discovery of a fourth immunoglobulin (Ig) light (L) chain isotype in sharks has revealed the origins and natural history of all vertebrate L chains. Phylogenetic comparisons have established orthology between this new shark L chain and the unique Xenopus L chain isotype sigma. More importantly, inclusion of this new L chain family in phylogenetic analyses showed that all vertebrate L chains can be categorized into four ancestral clans originating prior to the emergence of cartilaginous fish: one restricted to elasmobranchs (sigma-cart/type I), one found in all cold-blooded vertebrates (sigma/teleost type 2/elasmobranch type IV), one in all groups except bony fish (lambda/elasmobranch type II), and one in all groups except birds (kappa/elasmobranch type III/teleost type 1 and 3). All four of these primordial L chain isotypes (sigma, sigma-cart, lambda and kappa) have maintained separate V region identities since their emergence at least 450 million years ago, suggestive of an ancient physiological distinction of the L chains. We suggest that, based upon unique, discrete sizes of complementarity determining regions 1 and 2 and other features of the V region sequences, the different L chain isotypes arose to provide different functional conformations in the Ig binding site when they pair with heavy chains.

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    ABSTRACT: Citation: Manohar M, Khan H, Shukla V, Das V, Agarwal A, et al. (2014) Proteomic Identification and Analysis of Human Endometrial Proteins Associated with Unexplained Infertility. J Proteomics Bioinform 7: 359-366. doi:10.4172/ jpb.1000340 Copyright: © 2014 Manohar M, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited Abstract Unexplained infertility (UI) represents about 25-30% of all known types of female infertility. To date, UI remains an unsolved problem in a subgroup of infertile but otherwise healthy women and the molecular causes of UI are not yet known. In the current study, we have compared and analyzed the proteomic profile of receptive phase (LH+7) endometrium from fertile and infertile women, with a view to identify the appropriate protein target signatures that may be responsible for defective endometrial receptivity as a cause of UI. 12 Differentially expressed proteins (8 up-regulated and 4 down-regulated) were identified by Liquid Chromatography-Mass Spectrometric analysis. These differentially expressed proteins were involved in immunological response, glycolytic pathway, lipid metabolism, blood agglutination, protein synthesis, molecular chaperone, antioxidant system, mitochondrial ATP generation, and Ca +2 signalling. The expression of four differentially expressed proteins such as HSPβ-1, Apolipoprotein-A1, IGK@ protein, and RPLP2 were further validated by immunoblotting and immuno-histochemical analysis in separate biopsy samples, and also in in-vitro experimental model of decidualization of human endometrial stromal cells (hESCs). These proteins may have functional significance as regards the initiation and maintenance of the window of receptivity. Results of this study might be helpful in understanding the molecular basis of endometrial defects in a subset of infertile women having normal ovulation and hormonal profile. To our understanding, this is the first study to demonstrate the differential endometrial protein profiling in women with endometrium based-unexplained infertility.
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    ABSTRACT: Although lymphocyte-like cells secreting somatically-recombining receptors have been identified in the jawless fishes (hagfish and lamprey), the cartilaginous fishes (sharks, skates, rays and chimaera) are the most phylogenetically distant group relative to mammals in which bona fide immunoglobulins (Igs) have been found. Studies of the antibodies and humoral immune responses of cartilaginous fishes and other cold-blooded vertebrates (bony fishes, amphibians and reptiles) are not only revealing information about the emergence and roles of the different Ig heavy and light chain isotypes, but also the evolution of specialised adaptive features such as isotype switching, somatic hypermutation and affinity maturation. It is becoming increasingly apparent that while the adaptive immune response in these vertebrate lineages arose a long time ago, it is most definitely not primitive and has evolved to become complex and sophisticated. This review will summarise what is currently known about the immunoglobulins of cold-blooded vertebrates and highlight the differences, and commonalities, between these and more "conventional" mammalian species.
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