Restoration of CD44H expression in colon carcinomas reduces tumorigenicity

Annals of Surgery

Volumn 222, Issue 4, 1995, Pages 493-503

  Tanabe, Kenneth K ^a   Stamenkovic, Ivan ^a   Cutler, Michael ^a   Takahashi, Kazuhisa ^a  

^a MASSACHUSETTS GENERAL HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN;

ALTERNATIVE RNA SPLICING; ANTIGEN EXPRESSION; CANCER GROWTH; CARCINOGENICITY; COLON CARCINOMA; CONFERENCE PAPER; GROWTH RATE; MALIGNANT TRANSFORMATION; METASTASIS; PRIORITY JOURNAL; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION;

EID: 0028862839     PISSN: 00034932     EISSN: None     Source Type: Journal    
DOI: 10.1097/00000658-199510000-00007     Document Type: Conference Paper

References (52)

1. Tanabe KK, Ellis LM, Saya H. Expression of the CD44R1 adhesion molecule is increased in human colon carcinomas and metastases. Lancet 1993; 341:725-726.
2. Nagasaka S, Tanabe KK, Bruner JM, et al. Alternative RNA splicing of the hyaluronic acid receptor, CD44, in normal human brain and brain tumors. J Neurosurg 1995; 82:858-863.
3. Cannistra SA, Kansas GS, Niloff J, et al. Binding of ovarian cancer cells to peritoneal mesothelium in vitro is partly mediated by CD44H. Cancer Res 1993; 53:3830-3838.
4. Fox SB, Fawcett J, Jackson DG, et al. Normal human tissues, in addition to some tumors, express multiple different CD44 isoforms. Cancer Res 1994; 54:4539-4546.
5. Li H, Hamou M-F, de Tribolet N, et al. Variant CD44 adhesion molecules are expressed in human brain metastases but not in glioblastomas. Cancer Res 1993; 53:5345-5349.
6. Wielenga VJM, Heider K-H, Offerhaus JA, et al. Expression of CD44 variant proteins in human colorectal cancer is related to tumor progression. Cancer Res 1993; 53:4754-4756.
7. Screaton GR, Bell MV, Jackson DG, et al. Genomic structure of DNA encoding the lymphocyte homing receptor CD44 reveals at least 12 alternatively spliced exons. Proc Natl Acad Sci USA 1992; 89:12160-12164.
8. Tolg C, Hofmann M, Herrlich P, Ponta H. Splicing choice from ten variant exons establishes CD44 variability. Nuc Acids Res 1993; 21:1225-1229.
9. Tanabe KK, Nishi T, Saya H. Novel variants of CD44 arising from alternative splicing: changes in the CD44 alternative splicing pattern of MCF-7 breast carcinoma cells treated with hyaluronidasc. Mol Carcinog 1993; 7:212-220.
10. Dougherty GJ, Landorp PM, Cooper DL, Humphries RK. Molecular cloning of CD44R1 and CD44R2, two novel isoforms of the human CD44 lymphocyte "homing" receptor expressed by hemopoietic cells. J Exp Med 1991; 174:1-5.
11. Gunthert U, Hofmann M, Rudy W, et al. A new variant of glycoprotein CD44 confers metastatic potential to rat carcinoma cells. Cell 1991; 65:13-24.
12. Jackson DG, Buckley J, Bell JI. Multiple variants of the human lymphocyte homing receptor CD44 generated by insertions at a single site in the extracellular domain. J Biol Chem 1992; 267: 4732-4739.
13. Stamenkovic I, Aruffo A, Amiot M, Seed B. The hematopoietic and epithelial forms of CD44 are distinct polypeptides with different adhesion potentials for hyaluronate-bearing cells. EMBO J 1991; 10:343-348.
14. Cooper DL, Dougherty G, Harn HJ, et al. The complex CD44 transcriptional unit: alternative splicing of three internal exons generates the epithelial form of CD44. Biochem Biophys Res Commun 1992; 182:569-578.
15. Brown TA, Bouchard T, St. John T. et al. Human keratinocytes express a new CD44 core protein (CD44E) as a heparan-sulfate intrinsic membrane proteoglycan with additional exons. J Cell Biol 1991; 113:207-221.
16. Smith CWJ, Patton JG, Nadal-Ginard B. Alternative splicing in the control of gene expression. Annu Rev Genet 1989; 23:527-577.
17. Aruffo A, Stamenkovic I, Melnick M, et al. CD44 is the principal cell surface receptor for hyaluronate. Cell 1990; 61:1303-1313.
18. Culty M, Miyake K, Kincade PW, et al. The hyaluronate receptor is a member of the CD44 (H-CAM) family of cell surface glycoproteins. J Cell Biol 1990; 111:2765-2774.
19. Miyake K, Underbill CB, Lesley J, Kincade PW. Hyaluronate can function as a cell adhesion molecule and CD44 participates in hyaluronate recognition. J Exp Med 1990; 172:69-75.
20. Stamenkovic I, Amiot M, Pesando JM, Seed B. A lymphocyte molecule implicated in lymph node homing is a member of the cartilage link protein family. Cell 1989; 56:1057-1062.
21. Lesley J, He Q, Miyake K, et al. Requirements for hyaluronic acid binding by CD44: a role for the cytoplasmic domain and activation by antibody. J Exp Med 1992; 175:257-266.
22. Dougherty GJ, Cooper DL, Memory JF, Chiu RK. Ligand binding specificity of alternatively spliced CD44 isoforms; recognition and binding of hyaluronan by CD44R1. J Biol Chem 1994; 269:9074-9078.
23. Thomas L, Byers R, Vink J, Stamenkovic I. CD44H regulates tumor cell migration on hyaluronate-coated substrate. J Cell Biol 1992; 113:971-977.
24. Birch M, Mitchell S, Hart IR. Isolation and characterization of human melanoma cell variants expressing high and low levels of CD44. Cancer Res 1991; 51:6660-6667.
25. Culty M, Nguyen HA, Underhill CB. The hyaluronan receptor (CD44) participates in the uptake and degradation of hyaluronan. J Cell Biol 1992; 116:1055-1062.
26. St. John T, Meyer J, Idzerda R, Gallatin WM. Expression of CD44 confers a new adhesive phenotype on transfected cells. Cell 1990; 60:45-52.
27. Jalkanen S, Steere AC, Fox RI, Butcher EC. A distinct endothelial cell recognition system that controls lymphocyte traffic into in-named synovium. Science 1986; 233:556-558.
28. Jalkanen ST, Bargatze RF, Herron LR, Butcher EC. A lymphoid cell surface glycoprotein involved in endothelial cell recognition and lymphocyte homing in man. Eur J Immunol 1986; 16:1195-1202.
29. Jalkanen S, Bargatze RF, Toyos J, Butcher EC. Lymphocyte recognition of high endothelium: antibodies to distinct epitopes of an 85-95-kD glycoprotein antigen differentially inhibit lymphocyte binding to lymph node, mucosal, or synovial endothelial cells. J Cell Biol 1987; 105:983-990.
30. Jalkanen S, Jalkanen M, Bargatze R, et al. Biochemical properties of glycoproteins involved in lymphocyte recognition of high endothelial venules in man. J Immunol 1988; 141:1615-1623.
31. Fidler IJ. Critical factors in the biology of human cancer metastasis: Twenty-eighth G.H.A. Clowes Memorial Award Lecture. Cancer Res 1990; 50:6130-6138.
32. Sy MS, Guo YJ, Stamenkovic I. Distinct effects of two CD44 isoforms on tumor growth in vivo. J Exp Med 1991; 174:859-866.
33. Bartolazzi A, Peach R, Aruffo A, Stamenkovic I. Interaction between CD44 and hyaluronate is directly implicated in the regulation of tumor development. J Exp Med 1994; 180:53-66.
34. Mulder J-WR, Kruyt PM, Sewnath M, et al. Colorectal cancer prognosis and expression of exon-v6-containing CD44 proteins. Lancet 1994; 344:1470-1472.
35. Matsumura Y, Tarin D. Significance of CD44 gene products for cancer diagnosis and disease evaluation. Lancet 1992; 340:1053-1058.
36. Joensuu H, Klemi PJ, Toikkanen S, Jalkanen S. Glycoprotein CD44 expression and its association with survival in breast cancer. Am J Pathol 1993; 143:867-874.
37. Pals ST, Horst E, Ossekoppele GJ, et al. Expression of lymphocyte homing receptor as a mechanism of dissemination in non-Hodgkin's lymphoma. Blood 1989; 73:885-888.
38. Jalkanen S, Joensuu H, Sod̈erstrom̈ K-O, Klemi P. Lymphocyte homing and clinical behavior of non-Hodgkin's lymphoma. J Clin Invest 1992; 87:1835-1840.
39. Horst E, Meijer CJLM, Radaszkiewicz T, et al. Adhesion molecules in the prognosis of diffuse large-cell lymphoma: Expression of a lymphocyte homing receptor (CD44), LFA-1 (CD11a/CD18), and ICAM-1 (CD54). Leukemia (Baltimore) 1990; 4:595-599.
40. Joensuu HRR, Klemi PJ, Jalkanen S. Lymphocyte homing receptor (CD44) expression is associated with poor prognosis in gastrointestinal lymphoma. Br J Cancer 1993; 68:428-432.
41. Guo Y-J, Liu G, Wang X, et al. Potential use of soluble CD44 in serum as indicator of tumor burden and metastasis in patients with gastric or colon cancer. Cancer Res 1994; 54:422-426.
42. Hofmann M, Rudy W, Zoller M. et al. CD44 splice variants confer metastatic behavior in rats: homologous sequences are expressed in human tumor cell lines. Cancer Res 1991; 51:5292-5297.
43. Folkman J, Moscona A. The role of cell shape in growth control. Nature 1978; 273:345-349.
44. Takeichi M. Cadherins: A molecular family important in selective cell-cell adhesion. Annu Rev Biochem 1990; 59:237-252.
45. Ruoslahti E, Pierschbacher MD. New perspectives in cell adhesion: RGD and integrins. Science 1987; 238:491-497.
46. Williams AF, Barclay AN. The immunoglobulin superfamily-domains for cell surface recognition. Annu Rev Immunol 1988; 6: 381-405.
47. Brown PJ, Juliano RL. Monoclonal antibodies to a cell surface glycoprotein selectively inhibit fibronectin mediated cell adhesion. Science 1985; 228:1448-1451.
48. Pytela R, Pierschbacher MD, Ruoslahti E. Identification and isolation of a 150 kd cell surface glycoprotein with properties expected of a fibronectin receptor. Cell 1985; 40:191-198.
49. Plantefaber LC, Hynes RO. Changes in integrin receptors on oncogenically transformed cells. Cell 1989; 56:281-290.
50. 1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells. Cell 1990; 60:849-859.
51. Schreiner C, Fisher M, Hussein S, Juliano RL. Increased tumorigenicity of fibronectin receptor deficient Chinese hamster ovary cell variants. Cancer Res 1991; 51:1738-1740.
52. Tsukita S, Oichi K, Sato N, et al. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J Cell Biol 1994; 126:391-401.