Skip to main content
NCBI home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1992 Nov 1;119(3):679–693. doi: 10.1083/jcb.119.3.679

A truncated laminin chain homologous to the B2 chain: structure, spatial expression, and chromosomal assignment

PMCID: PMC2289671  PMID: 1383240

Abstract

We describe the identification of a novel laminin chain. Overlapping clones were isolated from a human fibrosarcoma HT1080 cell cDNA library spanning a total of 5,200 bp. A second set of clones contained an alternative 3' end sequence giving a total of 4,316 bp. The longer sequence contained an open reading frame for a 1,193-residue-long polypeptide. The alternative sequence was shortened at the carboxyl- terminal end coding for a 1,111-residue-long polypeptide. The amino acid sequence contained 21 amino acids of a putative signal peptide and 1,172 residues or alternatively 1,090 residues of a sequence with five distinct domains homologous to domains I-V in laminin chains. Comparison of the amino acid sequences showed that the novel laminin chain is homologous to the laminin B2 chain. However, the structure of the novel laminin chain isolated here differs significantly from that of the B2 chain in that it has no domain VI and domains V, IV, and III are shorter, resulting in a truncated laminin chain. The alternative sequence had a shortened domain I/II. In accordance with the current nomenclature, the chain characterized here is termed B2t. Calculation of possible chain interactions of laminin chains with the B2t chain domain I/II indicated that the B2t chain can replace the B2 chain in some laminin molecules. The gene for the laminin B2t chain (LAMB2T) was localized to chromosome 1q25-q31 in close proximity to the laminin B2 chain gene. Northern analysis showed that the B2t chain is expressed in several human fetal tissues but differently from the laminin B1 and B2 chains. By in situ hybridization expression of the B2t chain was localized to specific epithelial cells in skin, lung, and kidney as opposed to a general epithelial and endothelial cell expression of the laminin B2 chain in the same tissues.

Full Text

The Full Text of this article is available as a PDF (4.0 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Barlow D. P., Green N. M., Kurkinen M., Hogan B. L. Sequencing of laminin B chain cDNAs reveals C-terminal regions of coiled-coil alpha-helix. EMBO J. 1984 Oct;3(10):2355–2362. doi: 10.1002/j.1460-2075.1984.tb02140.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Beck K., Hunter I., Engel J. Structure and function of laminin: anatomy of a multidomain glycoprotein. FASEB J. 1990 Feb 1;4(2):148–160. doi: 10.1096/fasebj.4.2.2404817. [DOI] [PubMed] [Google Scholar]
  3. Boot-Handford R. P., Kurkinen M., Prockop D. J. Steady-state levels of mRNAs coding for the type IV collagen and laminin polypeptide chains of basement membranes exhibit marked tissue-specific stoichiometric variations in the rat. J Biol Chem. 1987 Sep 15;262(26):12475–12478. [PubMed] [Google Scholar]
  4. Bouzon M., Dussert C., Lissitzky J. C., Martin P. M. Spreading of B16 F1 cells on laminin and its proteolytic fragments P1 and E8: involvement of laminin carbohydrate chains. Exp Cell Res. 1990 Sep;190(1):47–56. doi: 10.1016/0014-4827(90)90142-w. [DOI] [PubMed] [Google Scholar]
  5. Boyd C. D., Weliky K., Toth-Fejel S., Deak S. B., Christiano A. M., Mackenzie J. W., Sandell L. J., Tryggvason K., Magenis E. The single copy gene coding for human alpha 1 (IV) procollagen is located at the terminal end of the long arm of chromosome 13. Hum Genet. 1986 Oct;74(2):121–125. doi: 10.1007/BF00282074. [DOI] [PubMed] [Google Scholar]
  6. Bruch M., Landwehr R., Engel J. Dissection of laminin by cathepsin G into its long-arm and short-arm structures and localization of regions involved in calcium dependent stabilization and self-association. Eur J Biochem. 1989 Nov 6;185(2):271–279. doi: 10.1111/j.1432-1033.1989.tb15112.x. [DOI] [PubMed] [Google Scholar]
  7. Carter W. G., Ryan M. C., Gahr P. J. Epiligrin, a new cell adhesion ligand for integrin alpha 3 beta 1 in epithelial basement membranes. Cell. 1991 May 17;65(4):599–610. doi: 10.1016/0092-8674(91)90092-d. [DOI] [PubMed] [Google Scholar]
  8. Cavener D. R., Ray S. C. Eukaryotic start and stop translation sites. Nucleic Acids Res. 1991 Jun 25;19(12):3185–3192. doi: 10.1093/nar/19.12.3185. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Charonis A. S., Tsilibary E. C., Yurchenco P. D., Furthmayr H. Binding of laminin to type IV collagen: a morphological study. J Cell Biol. 1985 Jun;100(6):1848–1853. doi: 10.1083/jcb.100.6.1848. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Chi H. C., Hui C. F. Primary structure of the Drosophila laminin B2 chain and comparison with human, mouse, and Drosophila laminin B1 and B2 chains. J Biol Chem. 1989 Jan 25;264(3):1543–1550. [PubMed] [Google Scholar]
  11. Cooper A. R., Kurkinen M., Taylor A., Hogan B. L. Studies on the biosynthesis of laminin by murine parietal endoderm cells. Eur J Biochem. 1981 Sep;119(1):189–197. doi: 10.1111/j.1432-1033.1981.tb05593.x. [DOI] [PubMed] [Google Scholar]
  12. Cooper A. R., MacQueen H. A. Subunits of laminin are differentially synthesized in mouse eggs and early embryos. Dev Biol. 1983 Apr;96(2):467–471. doi: 10.1016/0012-1606(83)90183-5. [DOI] [PubMed] [Google Scholar]
  13. Cox K. H., DeLeon D. V., Angerer L. M., Angerer R. C. Detection of mrnas in sea urchin embryos by in situ hybridization using asymmetric RNA probes. Dev Biol. 1984 Feb;101(2):485–502. doi: 10.1016/0012-1606(84)90162-3. [DOI] [PubMed] [Google Scholar]
  14. Dean J. W., 3rd, Chandrasekaran S., Tanzer M. L. A biological role of the carbohydrate moieties of laminin. J Biol Chem. 1990 Jul 25;265(21):12553–12562. [PubMed] [Google Scholar]
  15. Dennis J. W., Waller C. A., Schirrmacher V. Identification of asparagine-linked oligosaccharides involved in tumor cell adhesion to laminin and type IV collagen. J Cell Biol. 1984 Oct;99(4 Pt 1):1416–1423. doi: 10.1083/jcb.99.4.1416. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Ehrig K., Leivo I., Argraves W. S., Ruoslahti E., Engvall E. Merosin, a tissue-specific basement membrane protein, is a laminin-like protein. Proc Natl Acad Sci U S A. 1990 May;87(9):3264–3268. doi: 10.1073/pnas.87.9.3264. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Ekblom M., Klein G., Mugrauer G., Fecker L., Deutzmann R., Timpl R., Ekblom P. Transient and locally restricted expression of laminin A chain mRNA by developing epithelial cells during kidney organogenesis. Cell. 1990 Jan 26;60(2):337–346. doi: 10.1016/0092-8674(90)90748-4. [DOI] [PubMed] [Google Scholar]
  18. Engel J., Hunter I., Schulthess T., Beck K., Dixon T. W., Parry D. A. Assembly of laminin isoforms by triple- and double-stranded coiled-coil structures. Biochem Soc Trans. 1991 Nov;19(4):839–843. doi: 10.1042/bst0190839. [DOI] [PubMed] [Google Scholar]
  19. Engvall E., Earwicker D., Haaparanta T., Ruoslahti E., Sanes J. R. Distribution and isolation of four laminin variants; tissue restricted distribution of heterotrimers assembled from five different subunits. Cell Regul. 1990 Sep;1(10):731–740. doi: 10.1091/mbc.1.10.731. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Fan Y. S., Davis L. M., Shows T. B. Mapping small DNA sequences by fluorescence in situ hybridization directly on banded metaphase chromosomes. Proc Natl Acad Sci U S A. 1990 Aug;87(16):6223–6227. doi: 10.1073/pnas.87.16.6223. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Fox J. W., Mayer U., Nischt R., Aumailley M., Reinhardt D., Wiedemann H., Mann K., Timpl R., Krieg T., Engel J. Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV. EMBO J. 1991 Nov;10(11):3137–3146. doi: 10.1002/j.1460-2075.1991.tb04875.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Frenette G. P., Ruddon R. W., Krzesicki R. F., Naser J. A., Peters B. P. Biosynthesis and deposition of a noncovalent laminin-heparan sulfate proteoglycan complex and other basal lamina components by a human malignant cell line. J Biol Chem. 1989 Feb 25;264(6):3078–3088. [PubMed] [Google Scholar]
  23. Fukushima Y., Pikkarainen T., Kallunki T., Eddy R. L., Byers M. G., Haley L. L., Henry W. M., Tryggvason K., Shows T. B. Isolation of a human laminin B2 (LAMB2) cDNA clone and assignment of the gene to chromosome region 1q25----q31. Cytogenet Cell Genet. 1988;48(3):137–141. doi: 10.1159/000132610. [DOI] [PubMed] [Google Scholar]
  24. Garrison K., MacKrell A. J., Fessler J. H. Drosophila laminin A chain sequence, interspecies comparison, and domain structure of a major carboxyl portion. J Biol Chem. 1991 Dec 5;266(34):22899–22904. [PubMed] [Google Scholar]
  25. Gehlsen K. R., Dickerson K., Argraves W. S., Engvall E., Ruoslahti E. Subunit structure of a laminin-binding integrin and localization of its binding site on laminin. J Biol Chem. 1989 Nov 15;264(32):19034–19038. [PubMed] [Google Scholar]
  26. Gerl M., Mann K., Aumailley M., Timpl R. Localization of a major nidogen-binding site to domain III of laminin B2 chain. Eur J Biochem. 1991 Nov 15;202(1):167–174. doi: 10.1111/j.1432-1033.1991.tb16358.x. [DOI] [PubMed] [Google Scholar]
  27. Goodman S. L., Aumailley M., von der Mark H. Multiple cell surface receptors for the short arms of laminin: alpha 1 beta 1 integrin and RGD-dependent proteins mediate cell attachment only to domains III in murine tumor laminin. J Cell Biol. 1991 May;113(4):931–941. doi: 10.1083/jcb.113.4.931. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Griffin C. A., Emanuel B. S., Hansen J. R., Cavenee W. K., Myers J. C. Human collagen genes encoding basement membrane alpha 1 (IV) and alpha 2 (IV) chains map to the distal long arm of chromosome 13. Proc Natl Acad Sci U S A. 1987 Jan;84(2):512–516. doi: 10.1073/pnas.84.2.512. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Haaparanta T., Uitto J., Ruoslahti E., Engvall E. Molecular cloning of the cDNA encoding human laminin A chain. Matrix. 1991 Jun;11(3):151–160. doi: 10.1016/s0934-8832(11)80153-8. [DOI] [PubMed] [Google Scholar]
  30. Heremans A., van der Schueren B., de Cock B., Paulsson M., Cassiman J. J., van den Berghe H., David G. Matrix-associated heparan sulfate proteoglycan: core protein-specific monoclonal antibodies decorate the pericellular matrix of connective tissue cells and the stromal side of basement membranes. J Cell Biol. 1989 Dec;109(6 Pt 1):3199–3211. doi: 10.1083/jcb.109.6.3199. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Hunter D. D., Shah V., Merlie J. P., Sanes J. R. A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction. Nature. 1989 Mar 16;338(6212):229–234. doi: 10.1038/338229a0. [DOI] [PubMed] [Google Scholar]
  32. Hunter I., Schulthess T., Bruch M., Beck K., Engel J. Evidence for a specific mechanism of laminin assembly. Eur J Biochem. 1990 Mar 10;188(2):205–211. doi: 10.1111/j.1432-1033.1990.tb15391.x. [DOI] [PubMed] [Google Scholar]
  33. Hunter I., Schulthess T., Engel J. Laminin chain assembly by triple and double stranded coiled-coil structures. J Biol Chem. 1992 Mar 25;267(9):6006–6011. [PubMed] [Google Scholar]
  34. Kallunki P., Eddy R. L., Byers M. G., Kestilä M., Shows T. B., Tryggvason K. Cloning of human heparan sulfate proteoglycan core protein, assignment of the gene (HSPG2) to 1p36.1----p35 and identification of a BamHI restriction fragment length polymorphism. Genomics. 1991 Oct;11(2):389–396. doi: 10.1016/0888-7543(91)90147-7. [DOI] [PubMed] [Google Scholar]
  35. Kallunki T., Ikonen J., Chow L. T., Kallunki P., Tryggvason K. Structure of the human laminin B2 chain gene reveals extensive divergence from the laminin B1 chain gene. J Biol Chem. 1991 Jan 5;266(1):221–228. [PubMed] [Google Scholar]
  36. Klein G., Ekblom M., Fecker L., Timpl R., Ekblom P. Differential expression of laminin A and B chains during development of embryonic mouse organs. Development. 1990 Nov;110(3):823–837. doi: 10.1242/dev.110.3.823. [DOI] [PubMed] [Google Scholar]
  37. Kleinman H. K., Ebihara I., Killen P. D., Sasaki M., Cannon F. B., Yamada Y., Martin G. R. Genes for basement membrane proteins are coordinately expressed in differentiating F9 cells but not in normal adult murine tissues. Dev Biol. 1987 Aug;122(2):373–378. doi: 10.1016/0012-1606(87)90302-2. [DOI] [PubMed] [Google Scholar]
  38. Kramer R. H., Vu M. P., Cheng Y. F., Ramos D. M., Timpl R., Waleh N. Laminin-binding integrin alpha 7 beta 1: functional characterization and expression in normal and malignant melanocytes. Cell Regul. 1991 Oct;2(10):805–817. doi: 10.1091/mbc.2.10.805. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Laurie G. W., Bing J. T., Kleinman H. K., Hassell J. R., Aumailley M., Martin G. R., Feldmann R. J. Localization of binding sites for laminin, heparan sulfate proteoglycan and fibronectin on basement membrane (type IV) collagen. J Mol Biol. 1986 May 5;189(1):205–216. doi: 10.1016/0022-2836(86)90391-8. [DOI] [PubMed] [Google Scholar]
  40. Liesi P., Närvänen A., Soos J., Sariola H., Snounou G. Identification of a neurite outgrowth-promoting domain of laminin using synthetic peptides. FEBS Lett. 1989 Feb 13;244(1):141–148. doi: 10.1016/0014-5793(89)81180-9. [DOI] [PubMed] [Google Scholar]
  41. Mecham R. P. Receptors for laminin on mammalian cells. FASEB J. 1991 Aug;5(11):2538–2546. doi: 10.1096/fasebj.5.11.1651264. [DOI] [PubMed] [Google Scholar]
  42. Montell D. J., Goodman C. S. Drosophila laminin: sequence of B2 subunit and expression of all three subunits during embryogenesis. J Cell Biol. 1989 Nov;109(5):2441–2453. doi: 10.1083/jcb.109.5.2441. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Montell D. J., Goodman C. S. Drosophila substrate adhesion molecule: sequence of laminin B1 chain reveals domains of homology with mouse. Cell. 1988 May 6;53(3):463–473. doi: 10.1016/0092-8674(88)90166-3. [DOI] [PubMed] [Google Scholar]
  44. Nakai H., Byers M. G., Shows T. B., Taggart R. T. Assignment of the pepsinogen gene complex (PGA) to human chromosome region 11q13 by in situ hybridization. Cytogenet Cell Genet. 1986;43(3-4):215–217. doi: 10.1159/000132324. [DOI] [PubMed] [Google Scholar]
  45. Nissinen M., Vuolteenaho R., Boot-Handford R., Kallunki P., Tryggvason K. Primary structure of the human laminin A chain. Limited expression in human tissues. Biochem J. 1991 Jun 1;276(Pt 2):369–379. doi: 10.1042/bj2760369. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Paulsson M., Deutzmann R., Timpl R., Dalzoppo D., Odermatt E., Engel J. Evidence for coiled-coil alpha-helical regions in the long arm of laminin. EMBO J. 1985 Feb;4(2):309–316. doi: 10.1002/j.1460-2075.1985.tb03630.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Pikkarainen T., Eddy R., Fukushima Y., Byers M., Shows T., Pihlajaniemi T., Saraste M., Tryggvason K. Human laminin B1 chain. A multidomain protein with gene (LAMB1) locus in the q22 region of chromosome 7. J Biol Chem. 1987 Aug 5;262(22):10454–10462. [PubMed] [Google Scholar]
  48. Pikkarainen T., Kallunki T., Tryggvason K. Human laminin B2 chain. Comparison of the complete amino acid sequence with the B1 chain reveals variability in sequence homology between different structural domains. J Biol Chem. 1988 May 15;263(14):6751–6758. [PubMed] [Google Scholar]
  49. Pöschl E., Pollner R., Kühn K. The genes for the alpha 1(IV) and alpha 2(IV) chains of human basement membrane collagen type IV are arranged head-to-head and separated by a bidirectional promoter of unique structure. EMBO J. 1988 Sep;7(9):2687–2695. doi: 10.1002/j.1460-2075.1988.tb03122.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Rentrop M., Knapp B., Winter H., Schweizer J. Aminoalkylsilane-treated glass slides as support for in situ hybridization of keratin cDNAs to frozen tissue sections under varying fixation and pretreatment conditions. Histochem J. 1986 May;18(5):271–276. doi: 10.1007/BF01676237. [DOI] [PubMed] [Google Scholar]
  51. Rousselle P., Lunstrum G. P., Keene D. R., Burgeson R. E. Kalinin: an epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments. J Cell Biol. 1991 Aug;114(3):567–576. doi: 10.1083/jcb.114.3.567. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Sanes J. R., Engvall E., Butkowski R., Hunter D. D. Molecular heterogeneity of basal laminae: isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere. J Cell Biol. 1990 Oct;111(4):1685–1699. doi: 10.1083/jcb.111.4.1685. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Sasaki M., Kato S., Kohno K., Martin G. R., Yamada Y. Sequence of the cDNA encoding the laminin B1 chain reveals a multidomain protein containing cysteine-rich repeats. Proc Natl Acad Sci U S A. 1987 Feb;84(4):935–939. doi: 10.1073/pnas.84.4.935. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Sasaki M., Kleinman H. K., Huber H., Deutzmann R., Yamada Y. Laminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the laminin B chains. J Biol Chem. 1988 Nov 15;263(32):16536–16544. [PubMed] [Google Scholar]
  56. Sasaki M., Yamada Y. The laminin B2 chain has a multidomain structure homologous to the B1 chain. J Biol Chem. 1987 Dec 15;262(35):17111–17117. [PubMed] [Google Scholar]
  57. Schittny J. C., Yurchenco P. D. Terminal short arm domains of basement membrane laminin are critical for its self-assembly. J Cell Biol. 1990 Mar;110(3):825–832. doi: 10.1083/jcb.110.3.825. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Shows T. B., Sakaguchi A. Y., Naylor S. L. Mapping the human genome, cloned genes, DNA polymorphisms, and inherited disease. Adv Hum Genet. 1982;12:341–452. doi: 10.1007/978-1-4615-8315-8_5. [DOI] [PubMed] [Google Scholar]
  59. Shows T., Eddy R., Haley L., Byers M., Henry M., Fujita T., Matsui H., Taniguchi T. Interleukin 2 (IL2) is assigned to human chromosome 4. Somat Cell Mol Genet. 1984 May;10(3):315–318. doi: 10.1007/BF01535253. [DOI] [PubMed] [Google Scholar]
  60. Soininen R., Huotari M., Hostikka S. L., Prockop D. J., Tryggvason K. The structural genes for alpha 1 and alpha 2 chains of human type IV collagen are divergently encoded on opposite DNA strands and have an overlapping promoter region. J Biol Chem. 1988 Nov 25;263(33):17217–17220. [PubMed] [Google Scholar]
  61. Sonnenberg A., Gehlsen K. R., Aumailley M., Timpl R. Isolation of alpha 6 beta 1 integrins from platelets and adherent cells by affinity chromatography on mouse laminin fragment E8 and human laminin pepsin fragment. Exp Cell Res. 1991 Dec;197(2):234–244. doi: 10.1016/0014-4827(91)90428-w. [DOI] [PubMed] [Google Scholar]
  62. Sonnenberg A., Linders C. J., Modderman P. W., Damsky C. H., Aumailley M., Timpl R. Integrin recognition of different cell-binding fragments of laminin (P1, E3, E8) and evidence that alpha 6 beta 1 but not alpha 6 beta 4 functions as a major receptor for fragment E8. J Cell Biol. 1990 Jun;110(6):2145–2155. doi: 10.1083/jcb.110.6.2145. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Timpl R., Rohde H., Robey P. G., Rennard S. I., Foidart J. M., Martin G. R. Laminin--a glycoprotein from basement membranes. J Biol Chem. 1979 Oct 10;254(19):9933–9937. [PubMed] [Google Scholar]
  64. Timpl R. Structure and biological activity of basement membrane proteins. Eur J Biochem. 1989 Apr 1;180(3):487–502. doi: 10.1111/j.1432-1033.1989.tb14673.x. [DOI] [PubMed] [Google Scholar]
  65. Vuolteenaho R., Chow L. T., Tryggvason K. Structure of the human laminin B1 chain gene. J Biol Chem. 1990 Sep 15;265(26):15611–15616. [PubMed] [Google Scholar]
  66. Yurchenco P. D., Cheng Y. S., Colognato H. Laminin forms an independent network in basement membranes. J Cell Biol. 1992 Jun;117(5):1119–1133. doi: 10.1083/jcb.117.5.1119. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Zabel B. U., Naylor S. L., Sakaguchi A. Y., Bell G. I., Shows T. B. High-resolution chromosomal localization of human genes for amylase, proopiomelanocortin, somatostatin, and a DNA fragment (D3S1) by in situ hybridization. Proc Natl Acad Sci U S A. 1983 Nov;80(22):6932–6936. doi: 10.1073/pnas.80.22.6932. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. von der Mark H., Dürr J., Sonnenberg A., von der Mark K., Deutzmann R., Goodman S. L. Skeletal myoblasts utilize a novel beta 1-series integrin and not alpha 6 beta 1 for binding to the E8 and T8 fragments of laminin. J Biol Chem. 1991 Dec 15;266(35):23593–23601. [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES