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Laminin-5 in Epithelial Tumour Invasion

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Abstract

Laminin-5 (LN-5), consisting of α3-, β3-, and γ2-chains, is a component of the cell adhesion complex containing hemidesmosomes and anchoring fibrils. This protein is a major constituent of the extracellular matrix and has recently proved to be an invasion marker for epithelial cells in many immunohistochemical surveys, indicating that it is frequently expressed in the invading edges of epithelial tumour cells. Additionally, intracellular accumulation of monomeric γ2-chains has been widely observed in the invasive carcinoma cells, but its mechanism was not entirely understood. Epithelial carcinoma cells prefer to adhere onto the LN-5-rich basement membranes using the specific integrins as receptors. Induction of cell migration is an important function of LN-5 and the enhanced activity is observed in its truncated form after proteolytic shedding of the N-terminal fragments of γ2-chains. This processing was demonstrated to be mediated mainly by several kinds of matrix metallo-proteinases. The degraded fragments of γ2-chains, released from invading carcinomas, can be immunodetected in biological fluids and potentially utilized in the clinical diagnosis of various epithelial cancers. Here, we summarize the previous clinical investigations of LN-5 in epithelial tumour progression, and also discuss what it can regulate in the cell physiological events.

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References

  • Akamatsu H, Ichihara-Tanaka K, Ozono K, Kamiike W, Matsuda H, Sekiguchi K (1996) Suppression of transformed phenotypes of human fibrosarcoma cells by overexpression of recombinant fibronectin. Cancer Res 56: 4541–4546.

    Google Scholar 

  • Akashi T, Ito E, Eishi Y, Koike M, Nakamura K, Burgeson RE (2001) Reduced expression of laminin α3 and α5 chains in non-small cell lung cancers. Jpn J Cancer Res 92: 293–301.

    Google Scholar 

  • Amano S, Scott IC, Takahara K, Koch M, Champliaud M-F, Gerecke DR, Keene DR, Hudson DL, Nishiyama T, Lee S, Greenspan DS, Burgeson RE (2000) Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 γ2 chain. J Biol Chem 275: 22728–22735.

    Google Scholar 

  • Anderson TD, Feldman M, Wever RS, Ziober AF, Ziober BL (2001) Tumor deposition of laminin-5 and the relationship with perineural invasion. Laryngoscope 111: 2140–2143.

    Google Scholar 

  • Aoki S, Nakanishi Y, Akimoto S, Moriya Y, Yoshimura K, Kitajima M, Sakamoto M, Hirohashi S (2002) Prognostic significance of laminin-5 γ2 chain expression in colorectal carcinoma. Dis Colon Rectum 45: 1520–1527.

    Google Scholar 

  • Aumailley M, Khal AE, Knöss N, Tunggal L (2003) Laminin 5 processing and its integration into the ECM. Matrix Biol 22: 49–54.

    Google Scholar 

  • Berndt A, Borsi L, Hyckel P, Kosmehl H (2001) Fibrillary co-deposition of laminin-5 and large unspliced tenascin-C in the invasive front of oral squamous cell carcinomas in vivo and in vitro. J Cancer Res Clin Oncol 127: 286–292.

    Google Scholar 

  • Burgeson RE, Chiquet M, Deutzmann R, Ekblom P, Engel J, Kleinman H, Martin GR, Meneguzzi G, Paulsson M, Sanes J, Timpl R, Tryggvason K, Yamada Y, Yurchenco PD (1994) A new nomenclature for the laminins. Matrix Biol 14: 209–211.

    Google Scholar 

  • Byers LJ, Osborne JL, Carson LF, Carter JR, Haney AF, Weinberg JB, Ramakrishnan S (1995) Increased levels of laminin in ascitic fluid of patients with ovarian cancer. Cancer Lett 88: 67–72.

    Google Scholar 

  • Carter WG, Ryan MC, Gahr PJ (1991) Epiligrin, a new cell adhesion ligand for integrin α3β1 in epithelial basement membranes. Cell 65: 599–610.

    Google Scholar 

  • Colognato H, Yurchenco PD (2000) Form and function: The laminin family of heterotrimers. Dev Dyn 218: 213–234.

    Google Scholar 

  • Dajee M, Lazarov M, Zhang JY, Green CL, Russell AJ, Marinkovich MP, Tao S, Lin Q, Kubo Y, Khavari PA (2003) NF-κ B blockade and oncogenic Ras trigger invasive human epidermal neoplasia. Nature 421: 639–643.

    Google Scholar 

  • Egeblad M, Werb Z (2002) New functions for the matrix metallo-proteinases in cancer progression. Nat Rev Cancer 2: 161–174.

    Google Scholar 

  • Fukushima N, Sakamoto M, Hirohashi S (2001) Expression of laminin-5-γ-2 chain in intraductal papillary-mucinous and invasive ductal tumors of the pancreas. Mod Pathol 14: 404–409.

    Google Scholar 

  • Fukushima Y, Ohnishi T, Arita N, Hayakawa T, Sekiguchi K (1998) Integrin α3β1-mediated interaction with laminin-5 stimulates adhesion, migration and invasion of malignant glioma cells. Int J Cancer 76: 63–72.

    Google Scholar 

  • Geuijen CAW, Sonnenberg A (2002) Dynamics of the α6β4 integrin in keratinocytes. Mol Biol Cell 13: 3845–3858.

    Google Scholar 

  • Giannelli G, Falk-Marzillier J, Schiraldi O, Stetler-Stevenson WG, Quaranta V (1997) Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5. Science 277: 225–228.

    Google Scholar 

  • Giannelli G, Bergamini C, Fransvea E, Marinosci F, Quaranta V, Antonaci S (2001) Human hepatocellular carcinoma (HCC) cells require both α3β1 integrin and matrix metalloproteinases activity for migration and invasion. Lab Invest 81: 613–627.

    Google Scholar 

  • Gilles C, Polette M, Coraux C, Tournier J-M, Meneguzzi G, Munaut C, Volders L, Rousselle P, Birembaut P, Foidart J-M (2001) Contribution of MT1-MMPand human laminin-5 γ 2 chain degradation to mammary epithelial cell migration. J Cell Sci 114: 2967–2976.

    Google Scholar 

  • Goldfinger LE, Stack MS, Jones JCR (1998) Processing of laminin-5 and its functional consequences: Role of plasmin and tissue-type plasminogen activator. J Cell Biol 141: 255–265.

    Google Scholar 

  • Haas KM, Berndt A, Stiller KJ, Hyckel P, Kosmehl H (2001) A comparative quantitative analysis of laminin-5 in the basement membrane of normal, hyperplastic, and malignant oral mucosa by confocal immunofluorescence imaging. J Histochem Cytochem 49: 1261–1268.

    Google Scholar 

  • Habermann J, Lenander C, Roblick UJ, Kr¨ uger S, Ludwig D, Alaiya A, Freitag S, D¨umbgen L, Bruch H-P, Stange E, Salo S, Tryggvason K, Auer G, Schimmelpenning H (2001) Ulcerative colitis and colorectal carcinoma: DNA-profile, laminin-5 γ 2 chain and cyclin A expression as early markers for risk assessment. Scand J Gastroenterol 7: 751–758.

    Google Scholar 

  • Hagedorn HG, Sauer U, Schleicher ED, Nerlich AG (2001) Divergence in distribution and prognostic significance of major basement components in laryngeal carcinomas. Int J Oncol 18: 1045–1051.

    Google Scholar 

  • Hao J, Yang Y, McDaniel KM, Dalkin BL, Cress AE, Nagle RB (1996) Differential expression of laminin 5 (α3β3γ2) by human malignant and normal prostate. Am J Pathol 149: 1341–1349.

    Google Scholar 

  • Hao J, Jackson L, Calaluce R, McDaniel K, Dalkin BL, Nagle RB (2001) Investigation into the mechanism of the loss of laminin 5 (α3β3γ2) expression in prostate cancer. Am J Pathol 158: 1129–1135.

    Google Scholar 

  • Hellman K, Hellström A-C, Silfverswärd C, Salo S, Aspenblad U, Nilsson B, Frankendal B, Tryggvasson K, Auer G(2000) Cancer of the vagina: Laminin-5 γ 2 chain expression and prognosis. Int J Gynecol Cancer 10: 391–396.

    Google Scholar 

  • Henning K, Berndt A, Katenkamp D, Kosmehl H (1999) Loss of laminin-5 in the epithelium–stroma interface: An immunohisto-chemical marker of malignancy in epithelial lesions of the breast. Histopathology 34: 305–309.

    Google Scholar 

  • Hindermann W, Berndt A, Haas KM, Wunderlich H, Katenkamp D, Kosmehl H (2003) Immunohistochemical demonstration of the γ 2 chain of laminin-5 in urinary bladder urothelial carcinoma: Impact for diagnosis and prognosis. Cancer Detect Prevent 27: 109–115.

    Google Scholar 

  • Hintermann E, Bilban M, Sharabi A, Quaranta V (2001) Inhibitory role of α6β-associated erbB-2 and phosphoinositide 3-kinase in keratinocyte haptotactic migration dependent on α3β1 integrin. J Cell Biol 153: 465–478.

    Google Scholar 

  • Hlubek F, Jung A, Kotzor N, Kirchner T, Brabletz T (2001) Expression of the invasion factor laminin γ 2 in colorectal carcinomas is regulated by α-catenin. Cancer Res 61: 8089–8093.

    Google Scholar 

  • Ishii N, Wadsworth WG, Stern BD, Culotti JG, Hedgecock EM (1992) UNC-6, a laminin-related protein, guides cell and pioneer axon migrations in C. elegans. Neuron 9: 873–881.

    Google Scholar 

  • Ishizaka A, Hashimoto S, Matsuda T, Koh H, Tasaka S, Hasegawa N, Yamaguchi K, Katayama M, Sanzen N, Sekiguchi K (2002) Plasma soluble laminin-5 is increased in ARDS with poor prognosis. Am J Respir Crit Care Med Proceedings of American Thoracic Society International Conference 2002.

  • Kainulainen T, Autio-Harmainen H, Oikarinen A, Salo S, Tryggvason K, Salo T (1997) Altered distribution and synthesis of laminin-5 (kalinin) in oral lichen planus, epithelial dysplasias and squamous cell carcinomas. Br J Dermatol 136: 331–336.

    Google Scholar 

  • Kagesato Y, Mizushima H, Koshikawa N, Kitamura H, Hayashi H, Ogawa N, Tsukuda M, Miyazaki K (2001) Sole expression of laminin γ 2 chain in invading tumor cells and its association with stromal fibrosis in lung adenocarcinomas. Jpn J Cancer Res 92: 184–192.

    Google Scholar 

  • Katayama M, Kamihagi K, Hirai S, Kurome T, Murakami K, Hino F, Kato I (1992) Urinary laminin fragments as a tumour marker potentially reflecting basement membrane destruction. Br J Cancer 65: 509–514.

    Google Scholar 

  • Katayama M, Sanzen N, Funakoshi A, Sekiguchi K (2003) Laminin γ 2-chain fragment in the circulation: A prognostic indicator of epithelial tumor invasion. Cancer Res 63: 222–229.

    Google Scholar 

  • Katoh K, Nakanishi Y, Akimoto S, Yoshimura K, Takagi M, Sakamoto M, Hirohashi S (2002) Correlation between laminin-5 γ 2 chain expression and epidermal growth factor receptor expression and its clinico-pathological significance in squamous cell carcinoma of the tongue. Oncology 62: 318–326.

    Google Scholar 

  • Kennel SJ, Foote LJ, Falcioni R, Sonnenberg A, Stringer CD, Crouse C, Hemler ME (1989) Analysis of the tumor-associated antigen TSP-180. Identity with the α6β4 in the integrin superfamily. J Biol Chem 264: 15515–15521.

    Google Scholar 

  • Kikkawa Y, Sanzen N, Sekiguchi K (1998) Isolation and characterization of laminin-10/11 secreted by human lung carcinoma cells. J Biol Chem 273: 15854–15859.

    Google Scholar 

  • Kim WH, Nomizu M, Song S-Y, Tanaka K, Kuratomi Y, Kleinman HK, Yamada Y (1998) Laminin-á 1-chain sequence Leu–Gln–Val– Gln–Leu–Ser–Ile–Arg (LQVQLSIR) enhances murine melanoma cell metastasis. Int J Cancer 77: 632–639.

    Google Scholar 

  • Koch M, Olson PF, Albus A, Jin W, Hunter DD, Brunken WJ, Burgeson RE, Champliaud M-F (1999) Characterization and expres-sion of the laminin γ3 chain: A novel, non-basement membrane-associated, laminin chain. J Cell Biol 145: 605–617.

    Google Scholar 

  • Koch M, Murrell JR, Hunter DD, Olson PF, Jin W, Keene DR, Brunken WJ, Burgeson RE (2000) Anovel member of the netrin family, α-netrin, shares homology with the α chain of laminin: Identification, expression, and functional characterization. J Cell Biol 151: 221–234.

    Google Scholar 

  • Kohlberger P, Muller-Klingspor V, Heinzl H, Obermair A, Breitenecker G, Leodolter S (2002) Prognostic value of laminin-5 in serous adenocarcinomas of the ovary. Anticancer Res 22: 3541–3544.

    Google Scholar 

  • Koshikawa N, Moriyama K, Takamura H, Mizushima H, Ngashima Y, Yanoma S, Miyazaki K (1999) Overexpression of laminin γ 2 chain monomer in invading gastric carcinoma cells. Cancer Res 59: 5596–5601.

    Google Scholar 

  • Koshikawa N, Giannelli G, Cirulli V, Miyazaki K, Quaranta V (2000) Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5.J Cell Biol 148: 615–624.

    Google Scholar 

  • Kosmehl H, Berndt A, Strassburger S, Borsi L, Rousselle P, Mandel U, Hyckel P, Zardi L, Katenkamp D (1999) Distribution of laminin and fibronectin isoforms in oral mucosa and oral squamous cell carcinoma. Br J Cancer 81: 1071–1079.

    Google Scholar 

  • Kuratomi Y, Nomizu M, Nielsen PK, Tanaka K, Song S-Y, Kleinman HK, Yamada Y (1999) Identification of metastasis-promoting sequences in the mouse laminin γ1 chain. Exp Cell Res 249: 386–395.

    Google Scholar 

  • Kuratomi Y, Nomizu M, Tanaka K, Ponce ML, Komiyama S, Kleinman HK, Yamada Y (2002) Laminin γ 1 chain peptide, C-16 (KAFDITYVRLKF), promotes migration, MMP-9 secretion, and pulmonary metastasis of B16-F10 mouse melanoma cells. Br J Cancer 86: 1169–1173.

    Google Scholar 

  • Lenander C, Habermann JK, öst Å, Nilsson B, Schimmelpenning H, Tryggvason K, Auer G (2001) Laminin-5 γ2 chain expression correlates with unfavorable prognosis in colon carcinomas. Anal Cell Pathol 22: 201–209.

    Google Scholar 

  • Lohi J, Tani T, Leivo I, Linnala A, Kangas L, Burgeson RE, Lehto V-P, Virtanen I (1996) Expression of laminin in renal-cell carcinomas, renal-cell carcinoma cell lines and xenografts in nude mice. Int J Cancer 68: 364–371.

    Google Scholar 

  • Lohi J, Leivo I, Owaribe K, Burgeson RE, Franssila K, Virtanen I (1998) Neoexpression of the epithelial adhesion complex antigens in thyroid tumours is associated with proliferation and squamous differentiation markers. J Pathol 184: 191–196.

    Google Scholar 

  • Lohi J, Oivula J, Kivilaakso E, Kiviluoto T, Fröjdman K, Yamada Y, Burgeson RE, Leivo I, Virtanen I (2000) Basement membrane laminin-5 is deposited in colorectal adenomas and carcinomas and serves as a ligand for α3β1 integrin. APMIS 108: 161–172.

    Google Scholar 

  • Määttä M, Soini Y, Pääkkö P, Salo S, Tryggvason K, Autio-Harmainen H (1999) Expression of the laminin γ 2 chain in different histological types of lung carcinoma. A study by immunohistochemistry and in situ hybridization. J Pathol 188: 361–368.

    Google Scholar 

  • Mainiero F, Pepe A, Yeon M, Ren Y, Giancotti FG (1996) The intra-cellular functions of α6β4 integrin are regulated by EGF. J Cell Biol 134: 241–253.

    Google Scholar 

  • Martin KJ, Kwan C-P, Nagasaki K, Zhang X, O'Hare MJ, Kaelin CM, Burgeson RE, Pardee AB, Sager R (1998) Down-regulation of laminin-5 in breast carcinoma cells. Mol Med 4: 602–613.

    Google Scholar 

  • Masaki T, Matsuoka H, Sugiyama M, Abe N, Izumisato Y, Sakamoto A, Atomi Y (2003) Laminin-5 γ 2 chain expression as a possible determinant of tumor aggressiveness in T1 colorectal carcinomas. Dig Dis Sci 48: 272–278.

    Google Scholar 

  • Matsui C, Nelson CF, Hernandez GT, Herron GS, Bauer EA, Hoeffler WK (1995) γ 2 chain of laminin-5 is recognized by monoclonal antibody GB3. J Invest Dematol 105: 648–652.

    Google Scholar 

  • Mercurio AM, Rabinovitz I, Shaw LM (2001) The α6β4 integrin and epithelial cell migration. Curr Opin Cell Biol 13: 541–545.

    Google Scholar 

  • Mercurio AM(2003) Invasive skin carcinoma-ras and α6β4 integrin lead the way. Cancer Cell 3: 201–202.

    Google Scholar 

  • Meyerhardt JA, Caca K, Eckstrands BC, Hu G, Lengauer C, Banavali S, Look AT, Fearon ER (1999) Netrin-1: Interaction with deleted in colorectal cancer (DCC) and alterations in brain tumors and neuro-blastomas. Cell Growth Differ 10: 35–42.

    Google Scholar 

  • Miyazaki K, Kikkawa Y, Nakamura A, Yasumitsu H, Umeda M (1993) A large cell-adhesive scatter factor secreted by human gastric carcinoma cells. Proc Natl Acad Sci USA 90: 11767–11771.

    Google Scholar 

  • Mizushima H, Hirosaki T, Miyata S, Takamura H, Miyagi Y, Miyazaki K (2002) Expression of laminin-5 enhances tumorigenicity of human fibrosarcoma cells in nude mice. Jpn J Cancer Res 93: 652–659.

    Google Scholar 

  • Moriya Y, Niki T, Yamada T, Matsuno Y, Kondo H, Hirohashi S (2001) Increased expression of laminin-5 and its prognostic significance in lung adenocarcinomas of small size. Cancer 91: 1129–1141.

    Google Scholar 

  • Nguyen BP, Gil SG, Carter WG (2000) Deposition of laminin-5 by keratinocytes regulates integrin adhesion and signaling. J Biol Chem 275: 31896–31907.

    Google Scholar 

  • Nordström B, Einhorn N, Silfverswärd C, Sjövall K, Tryggvason K, Auer G(2002) Laminin-5 γ 2 chain as an invasivity marker for uni-and multifocal lesions in the lower anogenital tract. Int J Gynecol Cancer 12: 105–109.

    Google Scholar 

  • Niessen CM, Hogervorst F, Jaspars LH, de Melker AA, Delwel GO, Hulsman EHM, Kuikman I, Sonnenberg A (1994) The α6β4 integrin is a receptor for both laminin and kalinin. Exp Cell Res 211: 360–367.

    Google Scholar 

  • O'Connor KL, Shaw LM, Mercurio AM (1998) Release of cAMP gating by the α6β4 integrin stimulates lamellae formation and the chemotactic migration of invasive carcinoma cells. J Cell Biol 143: 1749–1760.

    Google Scholar 

  • Olsen J, Lefebvre O, Fritsch C, Troelsen JT, Orian-Rousseau V, Kedinger M, Simon-Assmann P (2000) Involvement of activator protein 1 complexes in the epithelium-specific activation of the laminin γ 2-chain gene promoter by hepatocyte growth factor (scatter factor). Biochem J 347: 407–417.

    Google Scholar 

  • Ono Y, Nakanishi Y, Ino Y, Niki T, Yamada T, Yoshimura K, Saikawa M, Nakajima T, Hirohashi S (1999) Clinicopathologic significance of laminin-5 γ 2 chain expression in squamous cell carcinoma of the tongue. Cancer 85: 2315–2321.

    Google Scholar 

  • Panayotou G, End P, Aumailley M, Timple R, Engel J (1989) Domains of laminin with growth-factor activity. Cell 56: 93–101.

    Google Scholar 

  • Patarroyo M, Tryggvason K, Virtanen I (2002) Laminin isoforms in tumor invasion, angiogenesis and metastasis. Semin Cancer Biol 12: 197–207.

    Google Scholar 

  • Pirilä E, Sharabi A, Salo T, Quaranta V, Tu H, Heljasvaara R, Koshikawa N, Sorsa T, Maisi P (2003) Matrix metalloproteinases process the laminin-5 γ 2-chain and regulate epithelial cell migration. Biochem Biophys Res Comm 303: 1012–1017.

    Google Scholar 

  • Pyke C, Rømer J, Kallunki P, Lund LR, Ralfkiær E, Danø K, Tryggvason K (1994) The γ 2 chain of kalinin/laminin 5 is prefer-entially expressed in invading malignant cells in human cancers. Am J Pathol 145: 782–791.

    Google Scholar 

  • Pyke C, Salo S, Ralfkiær E, Rømer J, Danø K, Tryggvason K (1995) Laminin-5 is a marker of invading cancer cells in some human carcinomas and is coexpressed with the receptor for urokinase plasminogen activator in budding cancer cells in colon adenocarcinomas. Cancer Res 55: 4132–4139.

    Google Scholar 

  • Rabinovitz I, Gipson IK, Mercurio AM (2001) Traction forces mediated by α6β4 integrin: Implications for basement membrane organization and tumor invasion. Mol Biol Cell 12: 4030–4043.

    Google Scholar 

  • Rousselle P, Lunstrum GP, Keene DR, Burgeson RE (1991) Kalinin: An epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments. J Cell Biol 114: 567–576.

    Google Scholar 

  • Rousselle P, Aumailley M(1994) Kalinin is more efficient than laminin in promoting adhesion of primary keratinocytes and some other epithelial cells and has a different requirement for integrin receptors. J Cell Biol 125: 205–214.

    Google Scholar 

  • Russell AJ, Fincher EF, Millman L, Smith R, Vela V, Waterman EA, Dey CN, Guide S, Weaver VM, Marinkovich MP (2003) α6β4 integrin regulates keratinocyte chemotaxis through differential GTPase activation and antagonism of α3β1 integrin. J Cell Sci 116: 3543–3556.

    Google Scholar 

  • Schenk S, Hintermann E, Bilban M, Koshikawa N, Hojilla C, Khokha R, Quaranta V (2003) Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution. J Cell Biol 161: 197–209.

    Google Scholar 

  • Schofield O, Kist D, Lucas A, Wayner E, Carter W, Zachary C (1998) Abnormal expression of epiligrin and α6β4 integrin in basal cell carcinoma. Dermatol Surg 24: 555–559.

    Google Scholar 

  • Shapiro SD (1998) Matrix metalloproteinase degradation of extracellular matrix: Biological consequences. Curr Opin Cell Biol 10: 602–608.

    Google Scholar 

  • Skyldberg B, Salo S, Eriksson E, Aspenblad U, Moberger B, Tryggvason K, Auer G (1999) Laminin-5 as a marker of invasiveness in cervical lesions. JNCI 91: 1882–1887.

    Google Scholar 

  • Soini Y, Määttä M, Salo S, Tryggvason K, Autio-Harmainen H (1996) Expression of the laminin γ 2 chain in pancreatic adenocarcinoma. J Pathol 180: 290–294.

    Google Scholar 

  • Sonnenberg A, Calafat J, Janssen H, Daams H, van der Raaij-Helmer LMH, Falcioni R, Kennel SJ, Aplin JD, Baker J, Loizidou M, Garrod D (1991) Integrin α6β4 complex is located in hemidesmosomes, suggesting a major role in epidermal cell-basement membrane adhesion. J Cell Biol 113: 907–917.

    Google Scholar 

  • Sordat I, Bosman FT, Dorta G, Rousselle P, Aberdam D, Blum AL, Sordat B (1998) Differential expression of laminin-5 subunits and integrin receptors in human colorectal neoplasia. J Pathol 185: 44–52.

    Google Scholar 

  • Sordat I, Rousselle P, Chaubert P, Petermann O, Aberdam D, Bosman FT, Sordat B (2000) Tumor cell budding and laminin-5 expression in colorectal carcinoma can be modulated by the tissue micro-environment. Int J Cancer 88: 708–717.

    Google Scholar 

  • Streuli C (1999) Extracellular matrix remodelling and cellular differentiation. Curr Opin Cell Biol 11: 634–640.

    Google Scholar 

  • Takahashi S, Hasebe T, Oda T, Sasaki S, Kinoshita T, Konishi M, Ochiai T, Ochiai A(2002) Cytoplasmic expression of laminin γ 2 chain correlates with postoperative hepatic metastasis and poor prognosis in patients with pancreatic ductal adenocarcinoma. Cancer 94: 1894–1901.

    Google Scholar 

  • Tani T, Karttunen T, Kiviluoto T, Kivilaakso E, Burgeson RE, Sipponen P, Virtanen I (1996) α6β4 integrin and newly deposited laminin-1 and laminin-5 form the adhesion mechanism of gastric carcinoma. Am J Pathol 149: 781–793.

    Google Scholar 

  • Tani T, Lumme A, Linnala A, Kivilaakso E, Kiviluoto T, Burgeson RE, Kangas L, Leivo I, Virtanen I (1997) Pancreatic carcinomas deposit laminin-5, preferably adhere to laminin-5, and migrate on the newly deposited basement membrane. Am J Pathol 151: 1289–1302.

    Google Scholar 

  • Thorup AK, Reibel J, Schiødt M, Stenersen TC, Therkildsen MH, Carter WG, Dabelsteen E (1998) Can alterations in integrin and laminin-5 expression be used as markers of malignancy? APMIS 106: 1170–1180.

    Google Scholar 

  • Timpl R, Brown JC (1994) The laminins. Matrix Biol 14: 275–281.

    Google Scholar 

  • Tunggal L, Ravaux J, Pesch M, Smola H, Krieg T, Gaill F, Sasaki T, Timple R, Mauch C, Aumailley M (2002) Defective laminin 5 processing in cylindroma cells. Am J Pathol 160: 459–468.

    Google Scholar 

  • Van Waes C, Kozarsky KF, Warren AB, Kidd L, Paugh D, Liebert M, Carey TE (1991) The A9 antigen associated with aggressive human squamous carcinoma is structurally and functionally similar to the newly defined integrin α6β4. Cancer Res 51: 2395–2402.

    Google Scholar 

  • Veitch DP, Nokelainen P, McGowan KA, Nguyen T-T, Nguyen NE, Stephenson R, Pappano WN, Keene DR, Spong SM, Greenspan DS, Findell PR, Marinkovich MP (2003) Mammalian tolloid metallo-proteinase, and not matrix metalloprotease 2 or membrane type 1 metalloprotease, processes laminin-5 in keratinocytes and skin. J Biol Chem 278: 15661–15668.

    Google Scholar 

  • Vejda S, Psovszky C, Zelzer S, Peter B, Bayer E, Gelbmann D, Schulte-Hermann R, Gerner C (2002) Plasma from cancer patients featuring a characteristic protein composition mediates protection against apoptosis. Mol Cell Proteomics 1: 387–393.

    Google Scholar 

  • Virtanen I, Gullberg D, Rissanen J, Kivilaakso E, Kiviluoto T, Laitinen LA, Lehto V-P, Ekblom P (2000) Laminin α 1-chain shows a restricted distribution in epithelial basement membranes of fetal and adult human tissues. Exp Cell Res 257: 298–309.

    Google Scholar 

  • Wang W, Wyckoff JB, Frohlich VC, Oleynikov Y, H¨ uttelmaier S, Zavadil J, Cermak L, Bottinger EP, Singer RH, White JG, Segall JE, Condeelis JS (2002) Single cell behavior in metastatic primary mammary tumors correlated with gene expression patterns revealed by molecular profiling. Cancer Res 62: 6278–6288.

    Google Scholar 

  • Yamamoto H, Itoh F, Iku S, Hosokawa M, Imai K (2001) Expression of the γ 2 chain of laminin-5 at the invasive front is associated with recurrence and poor prognosis in human esophageal squamous cell carcinoma. Clin Cancer Res 7: 896–900.

    Google Scholar 

  • Yurchenco PD, Schittny JC (1990) Molecular architecture of basement membranes. FASEB J 4: 1577–1590.

    Google Scholar 

  • Zhang K, Kramer RH(1996) Laminin 5 deposition promotes keratinocyte motility. Exp Cell Res 227: 309–322.

    Google Scholar 

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  1. Diagnostic Department, Tsukuba Research Laboratories, Eisai Co., Ltd, Tsukuba, Ibaraki, 300-2635, Japan

    Masahiko Katayama

  2. Institute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan

    Kiyotoshi Sekiguchi

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  1. Masahiko Katayama
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Katayama, M., Sekiguchi, K. Laminin-5 in Epithelial Tumour Invasion. Histochem J 35, 277–286 (2004). https://doi.org/10.1023/B:HIJO.0000032359.35698.fe

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