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The Joining (J) Chain Is Present in Invertebrates That Do Not Express

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The Joining (J) Chain Is Present in Invertebrates That Do Not Express Proc. Natl. Acad. Sci. USA Vol. 93, pp. 1886-1891, March 1996 Immunology The joining (J) chain is present in invertebrates that do not express immunoglobulins TOMIHISA TAKAHASHI*, TAKASHI IWASE*, NOBUKO TAKENOUCHI*, MANABU SAITO*, KUNIHIKO KOBAYASHIt, ZINA MOLDOVEANUt, JIRI MESTECKYt, AND ITARU MORO*§ *Department of Pathology, School of Dentistry, Nihon University, 1-8-13, Kanda-Surugadai, Chiyoda-ku, Tokyo 101, Japan; tDepartment of Pediatrics, Hokkaido University, School of Medicine, Kita 15 Jyo-Nishi 7, Kita-ku, Sapporo 060, Japan; and tDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294 Communicated by Marion E. Koshland, University of California, Berkeley, CA, November 22, 1995 (received for review August 19, 1995) ABSTRACT Joining (J) chain is a component of poly- These findings indicate that the J chain may possess functions meric, but not monomeric, immunoglobulin (Ig) molecules in addition to Ig polymerization. and may play a role in their polymerization and transport In human ontogeny, the J chain has been detected in fetal across epithelial cells. To date, study of the J chain has been liver at the sixth gestational week (18), and its expression was confined to vertebrates that produce Ig and in which the J found to precede synthesis of the ,u chain at least by 1 week. chain displays a considerable degree of structural homology. Phylogenetically, the J chain has been detected in many The role of the J chain in Ig polymerization has been ques- vertebrates including fish, amphibia, reptiles, birds, and mam- tioned and, since the J chain can be expressed in lymphoid mals, all ofwhich produce Ig (1-3, 19). In mammals, nucleotide cells that do not produce Ig, it is possible that the J chain may sequences encoding human (4), mouse (20), and bovine (21) have other functions. To explore this possibility, we have J chains, as well as the amino acid sequences of rabbit (22) and surveyed J-chain gene, mRNA, and protein expression by bullfrog (23) J chains have been reported. However, expression using reverse transcriptase-coupled PCR, Northern blot anal- of the J chain has not been investigated in invertebrate species and in invertebrate species that do in which the defense systems against foreign antigens are ysis, immunoblot analysis considerably different from those in vertebrates. Therefore, we not produce Ig. We report that the J-chain gene is expressed have examined the phylogeny of J chains in various animal in invertebrates (Mollusca, Annelida, Arthropoda, Echino- species, especially in invertebrates that do not produce Ig. dermata, and Holothuroidea), as well as in representative We detected the J-chain gene in various invertebrates and vertebrates (Mammalia, Teleostei, Amphibia). Furthermore, compared the earthworm J-chain DNA sequence with those of J-chain cDNA from the earthworm has a high degree of mammals. The J-chain gene was detected in 12 invertebrate homology (68-76%) to human, mouse, and bovine J chains. species but not in the sea anemone or amoeba. Furthermore, Immunohistochemical studies reveal that the J chain is local- the J-chain cDNA sequence determined from earthworm ized in the mucous cells of body surfaces, intestinal epithelial RNA by reverse transcriptase (RT)-coupled PCR displayed a cells, and macrophage-like cells of the earthworm and slug. high degree of homology to J chains from mammals, which are This study suggests that the J chain is a primitive polypeptide known to produce Ig. These results indicate that the J chain is that arose before the evolution of Ig molecules and remains a primitive protein that is highly conserved in invertebrates and highly conserved in extant invertebrates and vertebrates. vertebrates. The joining (J) chain was first identified as an additional MATERIALS AND METHODS component of human colostral secretory IgA (1-3). An acidic polypeptide with a molecular mass of 15 kDa, it is covalently Invertebrate and Vertebrate Species and Human Cell Lines. linked to the penultimate Cys residues of the a and ,i chains The following invertebrate and vertebrate species were used in of dimeric IgA and pentameric IgM molecules (1-3). The J this study: amoeba (Acanthamoeba castellani), sea anemone chain has been detected by a variety of techniques in mam- (Metridium senile), sea cucumber (Stichopus japonica), slug malian stem cells, pro-B, pre-B, and B cells, plasma cells, and (Incilaria bilineata), snail (Gastropoda littorinidae), oyster thymic T cells (4-13). Furthermore, recombinant technologies (Crassostrea gigas), clam (Meretrix lusoria), earthworm (Eisenia using insects (14) and plants (15) have demonstrated that the foetida), sea squirt (Ascidia japonica OKA), shrimp (Penaeus chain an role in the formation of secreted japonicus), crab (Portunus trituberculatus), silkworm (Bombyx J plays important mori), spider (Nepila clavata), butterfly (Artogenia rapae- dimeric IgA. Accordingly, the J chain is associated with crucivora), lamprey (Lampetra japonica), sardine (Sardinops extracellularly secreted polymeric immunoglobulin (Ig) and is melanostictus), and lizard (Eumeces latiscutatus). The Epstein- thought to function in the polymerization of Ig molecules and Barr virus-transformed human B-cell line Daudi was used as in their ability to bind the polymeric Ig receptor (pIg-R) on a J-chain-positive control (24), and the erythroleukemia cell epithelial cells (1-3). line K562 was a negative control. However, it has been reported that IgG-secreting cells and RT-PCR Procedure. Oligonucleotide primers were synthe- B-cell precursors in which Ig gene rearrangement did not occur sized by using a DNA synthesizer (Applied 13iosystems) from are able to produce the J chain (4-7, 10-12). Other studies the regions of the published DNA and amino acid sequences revealed that polymeric IgM is secreted by a glioma cell line common to human (4), mouse (20), rabbit (22), and bullfrog transfected with IgM heavy and light chain cDNA, even though (23) J chains. Primer sites were determined by using GenBank this cell line does not produce J chains (16). In IgM, substi- and EMBL data bases (GENETYX-MAC Software Develop- tution of a Ser for the Cys involved in J-chain binding results ment, Tokyo). Primer sequences designed for RT-PCR were in the formation of polymeric IgM without a J chain (17). as follows: pJ-1, 5'-GAGGACATTGTGGAGAGAAA-3'; The publication costs of this article were defrayed in part by page charge Abbreviations: J chain, joining chain; RT-PCR, reverse transcriptase- payment. This article must therefore be hereby marked "advertisement" in coupled PCR; Ig, immunoglobulin. accordance with 18 U.S.C. §1734 solely to indicate this fact. §To whom reprint requests should be addressed. 1886 Downloaded by guest on October 1, 2021 Immunology: Takahashi et al. Proc. Natl. Acad. Sci. USA 93 (1996) 1887 pJ-2, 5'-TAGCACTTGTTTCTGTCATA-3'; pJ-3, 5'- CTGTAAAAAATGTGATCC-3'; pJ-4, 5'-GTCAGGATG- GCAGGCAT-3'; ,B-actin, 5'-CCTTCCTGGGCATG- GAGTCCTG-3' and 5'-GGAGCAATGATCTTGATCTTC- 3'. To test the ability of each primer to detect the J-chain gene in earthworm RNA, several sets of synthesized primers were used in RT-PCRs. Total RNA was extracted from -1.0 g of earthworm tissue or 1 x 106 Daudi cells by the acid guani- dinium thiocyanate/phenol/chloroform method (25). RT- B 1 1) I A 7 Q 110)11 111 1A 1 PCR was performed as follows: random-hexamer-primed sin- gle-stranded cDNA was synthesized from 1.0 j,g of total RNA in a final volume of 10 ,ul with 2 units of Rous sarcoma- 310 bp -- associated virus 2 reverse transcriptase (Takara Shuzo, Kyoto) at 42°C for 60 min. An aliquot (1.0 t,l) of the reaction mixture was diluted with 50 ,ul of PCR buffer containing the various primer sets described above. The PCR was then performed by 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 using 2.5 units of Thermus aquaticus DNA polymerase (Strat- agene). The procedure for PCR was as follows: denaturing, 1 min at 95°C; annealing, 2 min at 55°C; extension, 3 min at 72°C. 310 bp -O PS a This cycle was repeated 35 times. The amplified DNA was electrophoresed on a 1.7% agarose gel, stained with ethidium bromide, and visualized and then photographed on a UV illuminator. After electrophoresis, the blot was transferred to C 1 2 3 4 5 6 7 8 9 10 a Hybond nylon membrane (Amersham) under standard con- ditions (26). Hybridization was performed in hybridization 1.4 Kb- buffer containing salmon sperm DNA (100 ,tg/ml), 6x SSC, 0.5% SDS, and 5x Denhardt's solution at 55°C for 16 h by using a human J-chain cDNA (kindly provided by E. E. Max, Laboratory of Cell and Viral Regulation, Food and Drug D 1 2 3 4 5 6 7 Administration Center for Biologics Evaluation and Research, Bethesda) encoding exons 1-4 labeled with [a-32P]dCTP by a 1.4Kb * random priming kit (Takara Shuzo). After hybridization, the membrane was washed three times at a high stringency (0.1 x SSC/0.2% SDS) at 55°C for 15 min and then exposed to Kodak FIG. 1. J-chain gene expression in earthworm by RT-PCR. (A) X-Omat film for 16 h at -80°C. 4X174/Hae III DNA as size marker (lanes 1 and 16); PCR products DNA Sequencing Analysis of the Earthworm J Chain. The from earthworm (lanes 2, 5, 8, and 11), from Daudi cells as a earthworm J chain was sequenced by using the TA cloning kit J-chain-positive control (lanes 3, 6, 9, 12, and 14), and from K562 cells (Invitrogen). Briefly, the RT-PCR product amplified by as a J-chain-negative control (lanes 4, 7, 10, 13, and 15). Combinations primer set pJ-1 and pJ-4 (Fig.
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