scholarly journals Non-light-chain immunoglobulin amyloidosis: time to expand or refine the spectrum to include light+heavy chain amyloidosis?

2013 ◽  
Vol 83 (3) ◽  
pp. 353-356 ◽  
Author(s):  
Maria M. Picken
Keyword(s):  
Heavy Chain ◽  
Light Chain ◽  
Light Chain Immunoglobulin

LIPOPOLYSACCHARIDE-SENSITIVE SERINE-PROTEASE ZYMOGEN (FACTOR C) OF LIMULUS HEMOCYTES: IDENTIFICATION AND ALIGNMENT OF PROTEOLYTIC FRAGMENTS PRODUCED DURING THE ACTIVATION SHOW THAT IT IS A NOVEL TYPE OF SERINE-PROTEASE

1987 ◽  
Author(s):  
F Tokunaga ◽  
T Miyata ◽  
T Nakamura ◽  
T Morita ◽  
S Iwanaga
Keyword(s):  
Serine Protease ◽  
Heavy Chain ◽  
Light Chain ◽  
Interleukin 2 ◽  
Coagulation Factor ◽  
Clotting Factor ◽  
Single Chain ◽  
Terminal Sequence ◽  
A Chain ◽  
Factor C

Limulus clotting factor, factor C, is a lipopolysaccharide (LPS)-sensitive serine-protease zymogen present in the hemocytes. It is a two-chain glycoprotein (M.W. = 123,000) composed of a heavy chain (M.W. = 80,000) and a light chain (M.W. = 43,000) T. Nakamura et al. (1986) Eur. J. Biochem. 154, 511-521 .On further studies of this zymogen, a single-chain factor C (M.W. = 123,000) was identified by Western blotting technique. The heavy chain had an NH2-terminal sequence of Ser-Gly-Val-Asp-, which was consistent with the NH2-terminal sequence of the single-chain factor C, indicating that the heavy chain is located in the NH2-terminal part of the zymogen. The light chain had an NH22-terminal sequence of Ser-Ser-Gln-Pro-. Incubation of the two-chain zymogen with LPS resulted in the cleavage of a Phe-Ile bond between residues 72 and 73 of the light chain. Concomitant with this cleavage, the A (72.amino acids) and B chains derived from the light chain was formed. The complete amino acid sequence of the A chain was determined by automated Edman degradation. The A chain contained a typical segment which is similar structuraly to those a family of repeats in human β2 -glycoprotein I, complement factors B, Clr, Cls, H, C4b-binding protein, 02, coagulation factor XIII b subunit, haptoglobin a chain, and interleukin 2 receptor. The NH2-terminal sequence of the B chain was Ile-Trp-Asn-Gly-. This chain contained the serine-active site sequence of -ASP-Ala-Cys-Ser-Gly-Asp-SER-Gly-Gly-Pro-.These results indicate that limulus factor C exists in the hemocytes in a single-chain zymogen form and is converted to an active serine-protease by hydrolysis of a specific Phe-Ile peptide bond. The correlation of limulus factor C and mammalian complement proteins was also suggested.

scholarly journals Myosin heavy chain-light chain recombinations and interactions between the two classes of light chains.

1983 ◽  
Vol 258 (14) ◽  
pp. 8876-8882 ◽  
Author(s):  
P D Wagner ◽  
D B Stone
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Light Chain ◽  
Light Chains

scholarly journals Variance analysis of immunoglobulin alleles in natural populations of rabbit (Oryctolagus cuniculus): the extensive interallelic divergence at the b locus could be the outcome of overdominance-type selection.

Genetics ◽  
1993 ◽  
Vol 135 (1) ◽  
pp. 171-187 ◽  
Author(s):  
W van der Loo
Keyword(s):  
Heavy Chain ◽  
Light Chain ◽  
Gene Diversity ◽  
Natural Populations ◽  
Constant Region ◽  
Immunoglobulin Light Chain ◽  
Evolutionary Patterns ◽  
B Locus ◽  
Type Selection ◽  
Predominant Allele

Abstract Population genetic data are presented which should contribute to evaluation of the hypothesis that the extraordinary evolutionary patterns observed at the b locus of the rabbit immunoglobulin light chain constant region can be the outcome of overdominance-type selection. The analysis of allele correlations in natural populations revealed an excess of heterozygotes of about 10% at the b locus while heterozygote excess was not observed at loci determining the immunoglobulin heavy chain. Data from the published literature, where homozygote advantage was suggested, were reevaluated and found in agreement with data here presented. Gene diversity was evenly distributed among populations and showed similarities with patterns reported for histocompatibility loci. Analysis of genotypic disequilibria revealed strong digenic associations between the leading alleles of heavy and light chain constant region loci in conjunction with trigenic disequilibria corresponding to a preferential association of b locus heterozygosity with the predominant allele of the heavy chain e locus. It is argued that this may indicate compensatory or nonadditive aspects of a putative heterozygosity enhancing mechanism, implying that effects at the light chain might be more pronounced in populations fixed for the heavy chain polymorphism.

scholarly journals The Drosophila kinesin light chain. Primary structure and interaction with kinesin heavy chain

1993 ◽  
Vol 268 (18) ◽  
pp. 13657-13666
Author(s):  
A.K. Gauger ◽  
L.S. Goldstein
Keyword(s):  
Heavy Chain ◽  
Light Chain ◽  
Primary Structure ◽  
Kinesin Light Chain ◽  
Kinesin Heavy Chain

scholarly journals Surrogate Light Chain Expression Is Required to Establish Immunoglobulin Heavy Chain Allelic Exclusion during Early B Cell Development

Immunity ◽  
1996 ◽  
Vol 4 (2) ◽  
pp. 133-144 ◽  
Author(s):  
Dirk Löffert ◽  
Andreas Ehlich ◽  
Werner Müller ◽  
Klaus Rajewsky
Keyword(s):  
B Cell ◽  
Heavy Chain ◽  
Light Chain ◽  
Immunoglobulin Heavy Chain ◽  
Cell Development ◽  
B Cell Development ◽  
Allelic Exclusion ◽  
Surrogate Light Chain

scholarly journals Critical roles of the immunoglobulin intronic enhancers in maintaining the sequential rearrangement of IgH and Igk loci

2006 ◽  
Vol 203 (7) ◽  
pp. 1721-1732 ◽  
Author(s):  
Matthew A. Inlay ◽  
Tongxiang Lin ◽  
Heather H. Gao ◽  
Yang Xu
Keyword(s):  
B Cells ◽  
Developmental Stage ◽  
Heavy Chain ◽  
Light Chain ◽  
Matrix Attachment Region ◽  
Cis Elements ◽  
Wild Type ◽  
Intronic Enhancer ◽  
Attachment Region

V(D)J recombination of immunoglobulin (Ig) heavy (IgH) and light chain genes occurs sequentially in the pro– and pre–B cells. To identify cis-elements that dictate this order of rearrangement, we replaced the endogenous matrix attachment region/Igk intronic enhancer (MiEκ) with its heavy chain counterpart (Eμ) in mice. This replacement, denoted EμR, substantially increases the accessibility of both Vκ and Jκ loci to V(D)J recombinase in pro–B cells and induces Igk rearrangement in these cells. However, EμR does not support Igk rearrangement in pre–B cells. Similar to that in MiEκ−/− pre–B cells, the accessibility of Vκ segments to V(D)J recombinase is considerably reduced in EμR pre–B cells when compared with wild-type pre–B cells. Therefore, Eμ and MiEκ play developmental stage-specific roles in maintaining the sequential rearrangement of IgH and Igk loci by promoting the accessibility of V, D, and J loci to the V(D)J recombinase.

scholarly journals Increased transcription and coordinate stabilization of mRNAs for secreted immunoglobulin alpha heavy chain and kappa light chain following stimulation of immunoglobulin A expressing B cells

1994 ◽  
Vol 269 (52) ◽  
pp. 33102-33108
Author(s):  
L Eckmann ◽  
G T Huang ◽  
J R Smith ◽  
E Morzycka-Wroblewska ◽  
M F Kagnoff
Keyword(s):  
B Cells ◽  
Heavy Chain ◽  
Light Chain ◽  
Immunoglobulin A ◽  
Kappa Light Chain ◽  
Immunoglobulin Alpha ◽  
Stimulation Of
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