Skip to main content
SpringerLink
Log in

Structure, Expression and Function of Mouse Laminin

  • Conference paper
Book cover Mesenchymal-Epithelial Interactions in Neural Development

Part of the book series: NATO ASI Series ((ASIH,volume 5))

Abstract

Basement membranes are thin extracellular matrices that separate epithelial and endothelial cells from underlaying stroma (Kefalides, 1973; Timpl and Martin, 1982). At the ultrastructural level, different zones are observed in the basement membrane including an electron dense zone, the lamina densa, and adjacent to it less electron dense zones, the lamina lucida. Basement membranes have diverse functions including forming barriers to the passage of proteins as well as of cells (Kefalides, 1979). They also play important roles in embryogenesis by delineating the developing tissues and by mediating the adhesion, growth, and differentiation of muscle, and peripheral nerve as well as of a variety of epithelial cells and organs.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Barlow, D.P., N.M. Green, M. Kurkinen, and B.L.M. Hogan (1984) Sequencing of laminin B chain cDNAs reveals C-terminal regions of coiled-coil alpha-helix. EMBO J. 3: 2355–2362.

    PubMed  CAS  Google Scholar 

  • Baron van Evercooren, A., H.K. Kleinman, S. Ohno, P. Marangos, J.P. Schwartz, and M.E. Dubois-Dalcq (1982) Nerve growth factor, laminin, and fibronectin promote neurite growth in human fetal sensory ganglia cultures. J. Neurosci. Res. 8: 179–193.

    Article  Google Scholar 

  • Bassel-Duby, R., A. Jayasuriya, D. Chatterjee, N. Sonenberg, J.V. Maizel, and B.N. Fields (1985) Sequence of reovirus haemagglutinin predicts a coiled-coil structure. Nature 315: 421–423.

    Article  PubMed  CAS  Google Scholar 

  • Bumol, T.F., and R.A. Reisfeld (1982) Unique glycoprotein-proteoglycan complex defined by monoclonal antibody on human melanoma cells. Proc. Natl. Acad. Sci. (USA) 79: 1245–1249.

    Article  CAS  Google Scholar 

  • Carpenter, G., and S. Cohen (1979) Epidermal growth factor. Annu. Rev. Biochem. 48: 193–216.

    Article  PubMed  CAS  Google Scholar 

  • Chung, A.E., R. Jaffe, I.L. Freeman, J.P. Vergnes, J. Braginski, and B. Carlin (1979) Properties of a basement membrane-related glycoprotein synthesized by a mouse embryonal carcinoma derived cell line. Cell 16: 277–287.

    Article  PubMed  CAS  Google Scholar 

  • Cooper, A.R., and H.A. MacQueen (1983) Subunits of laminin are differentially synthesized in mouse eggs and early embryos. Dev. Biol. 96: 467–471.

    Article  PubMed  CAS  Google Scholar 

  • Cornbrooks, C.J., D.J. Carey, J.A. McDonald, R. Timpl, and R.P. Bunge (1983) In vivo and in vitro observations on laminin production by Schwann cells. Proc. Natl. Acad. Sci. (USA) 80: 3850–3854.

    Article  CAS  Google Scholar 

  • Del Rosso, M., R. Cappelletti, M. Viti, S. Vannucchi, and V. Chiarugi (1981) Binding of the basement-membrane glycoprotein laminin to glycosaminoglycans. An affinity- chromatography study. Biochem. J. 199: 699–704.

    PubMed  Google Scholar 

  • Derynck, R., J.A. Jarrett, E.Y. Chen, D.H. Eaton, J.R. Bell, R.K. Assoian, A.B. Roberts, M.B. Sporn, and D.V. Goeddel (1984) Human transforming growth factor-beta complementary DNA sequence and expression in normal and transformed cells. Nature 316: 701–705.

    Article  Google Scholar 

  • Doege, K., J.R. Hassell, B. Caterson, and Y. Yamada (1986) Link protein cDNA sequence reveals a tandemly repeated protein structure. Proc. Natl. Acad. Sci. (USA), in press.

    Google Scholar 

  • Doolittle, R.F. (1985) The genealogy of some recently evolved vertebrate proteins. Trends Biochem. Sci. 10: 233–237.

    Article  CAS  Google Scholar 

  • Dynan, W.S., and R. Tjian (1983a) Isolation of transcription factors that discriminate between different promoters recognized by RNA polymerase II. Cell 32: 669–680.

    Article  PubMed  CAS  Google Scholar 

  • Dynan, W.S. and R. Tjian (1983b) The promoter-specific transcription factor Spl binds to upstream sequences in the SV40 early promoter. Cell 35: 79–87.

    Article  PubMed  CAS  Google Scholar 

  • Dziadek, M., and R. Timpl (1985) Expression of nidogen and laminin in basement membranes during mouse embryogenesis and in teratocarcinoma cells. Dev. Biol. 111: 372–382.

    Article  PubMed  CAS  Google Scholar 

  • Edgar, D., R. Timpl, and H. Thoenen (1984) The heparin-binding domain of laminin is responsible for its effects on neurite outgrowth and neuronal survival. EMBO J. 3: 1463–1468.

    PubMed  CAS  Google Scholar 

  • Engel, J., E. Odermatt, A. Engel, J.A. Madri, H. Furthmayr, H. Rohde, and R. Timpl (1981) Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix. J. Mol. Biol. 150: 97–120.

    Article  PubMed  CAS  Google Scholar 

  • Gray, A., T.J. Dull, and A. Ullrich (1983) Nucleotide sequence of epidermal growth factor cDNA predicts a 128,000-molecular weight protein precursor. Nature 303: 722–725.

    Article  PubMed  CAS  Google Scholar 

  • Greig, R.G., T.P. Koestler, D.L. Trainer, S.P. Corwin, L. Miles, T. Kline, R. Sweet, S. Yokoyama, and G. Poste (1985) Tumorigenic and metastatic properties of “normal” and ras-transfected NIH/3T3 cells. Proc. Natl. Acad. Sci. (USA) 82: 3698 - 3701.

    Article  CAS  Google Scholar 

  • Hassell, J.R., W.C. Leyson, S.R. Ledbetter, B. Tyree, S. Suzuki, M. Kato, K. Kimata, and H.K. Kleinman (1985) Isolation of two forms of basement membrane proteoglycans. J. Biol. Chem. 260: 8098–8105.

    PubMed  CAS  Google Scholar 

  • Hay, E.D. (1982) Interaction of embryonic surface and cytoskeleton with extracellular matrix. Am. J. Anat. 165: 1–12.

    Article  PubMed  CAS  Google Scholar 

  • Kefalides, N.A. (1973) Structure and biosynthesis of basement membrane. Int. Rev. Connect. Tissue Res. 6: 63–104.

    PubMed  CAS  Google Scholar 

  • Kefalides, N.A. (1979) Biochemistry and metabolism of basement membranes. Int. Rev. Cytol. 61: 167–228.

    Article  PubMed  CAS  Google Scholar 

  • Kennedy, D.W., D.H. Rohrbach, G.R. Martin, T. Momoi, and K.M. Yamada (1983) The adhesive glycoprotein laminin is an agglutinin. J. Cell Physiol. 3: 257–262.

    Article  Google Scholar 

  • Klebe, R.J. (1974) Isolation of a collagen-dependent cell attachment factor. Nature 250: 248–251.

    Article  PubMed  CAS  Google Scholar 

  • Kleinman, H.K., R.J. Klebe, and G.R. Martin (1984) Role of collagenous matrices in the adhesion and growth of cells. J. Cell Biol. 88: 473–485.

    Article  Google Scholar 

  • Kleinman, H.K., F.B. Cannon, G.W. Laurie, J.R. Hassell, M. Aumailley, V.P. Terranova, G.R. Martin, and M. DuBois-Dalcq (1985) Biological activities of laminin. In The Role of Extracellular Matrix in Development, R.L. Trelstad, ed., pp. 123–143. Alan R. Liss, New York.

    Google Scholar 

  • Kohno, K., M. Sullivan, and Y. Yamada (1985) Structure of the promoter of the rat type II procollagen gene. J. Biol. Chem. 260: 4441–4447.

    PubMed  CAS  Google Scholar 

  • Kurachi, K. and E.W. Davie (1982) Isolation and characterization of a cDNA coding for human factor IX. Proc. Natl. Acad. Sci. (USA) 79: 6461–6464.

    Article  CAS  Google Scholar 

  • Laurie, G.W., J.T. Bing, H.K. Kleinman, J.R. Hassell, M. Aumailley, G.R. Martin, and R.J. Feldmann (1986) Localization of binding sites for laminin, heparan sulfate proteoglycan, and fibronectin on basement membrane (Type IV) collagen. J. Mol. Biol., in press.

    Google Scholar 

  • Liau, G., Y. Yamada, and B. de Crombrugghe (1985) Coordinate regulation of the levels of type III and type I collagen mRNA in most but not all mouse fibroblasts. J. Biol. Chem. 260: 531–536.

    PubMed  CAS  Google Scholar 

  • Malinoff, A.L., and M.S. Wicha (1983) Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells. J. Cell Biol. 96: 1475–1479.

    Article  PubMed  CAS  Google Scholar 

  • McKnight, S.L., and R. Kingsbury (1982) Transcriptional control signals of a eukaryotic protein-coding gene. Science 217: 316–324.

    Article  PubMed  CAS  Google Scholar 

  • McLachlan, A.D., and J. Karn (1982) Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle. Nature 299: 226–231.

    Article  PubMed  CAS  Google Scholar 

  • McMullen, B.A., K. Fujikawa, W. Kisiel, T. Sasagawa, W.N. Howald, E.Y. Kwa, and B. Weinstein (1983) Complete amino acid sequence of the light chain of human blood coagulation factor X: Evidence for identification of residue 63 as beta-hydroxy- aspartic acid. Biochemistry 22: 2875–2884.

    Article  PubMed  CAS  Google Scholar 

  • Oberbaumer, I., M. Laurent, U. Schwarz, Y. Sakurai, Y. Yamada, G. Vogeli, T. Voss, B. Siebold, R.W. Glanville, and K. Kuhn (1985) Amino acid sequence of the non-col- lagenous globular domain (NCI) of the ad(IV) chain of basement membrane col-lagen as derived from complementary DNA. Eur. J. Biochem. 147: 217–224.

    Article  PubMed  CAS  Google Scholar 

  • Okayama, H., and P. Berg (1982) High-efficiency cloning of full-length cDNA. Mol. Cell. Biol. 2: 161–170.

    PubMed  CAS  Google Scholar 

  • Patthy, L. (1985) Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules. Cell 41: 657–663.

    Article  PubMed  CAS  Google Scholar 

  • Paulsson, M., R. Deutzmann, R. Timpl, D. Dalzoppo, E. Odermatt, and 3. Engel (1985) Evidence for coiled-coil alpha-helical regions in the long arm of laminin. EMBO. J. 4: 309–316.

    PubMed  CAS  Google Scholar 

  • Rao, C.N., I.M. Margulies, T.S. Tralka, V.P. Terranova, J.A. Madri, and L.A. Liotta (1982) Isolation of a subunit of laminin and its role in molecular structure and tumor cell attachment. J. Biol. Chem. 257: 9740–9744.

    PubMed  CAS  Google Scholar 

  • Rao, C.N., S.H. Barsky, V.P. Terranova, and L.A. Liotta (1983) Isolation of a tumor cell laminin receptor. Biochem. Biophys. Res. Commun. 111: 804–808.

    Article  PubMed  CAS  Google Scholar 

  • Rennard, S.I., R. Berg, G.R. Martin, J.M. Foidart, and P. Gehron-Robey (1980) Enzyme linked immunoassay (ELISA) for connective tissue components. Analyt. Biochem. 104: 205–214.

    Article  PubMed  CAS  Google Scholar 

  • Reynolds, G., S.K. Basu, T.F. Osborne, D.J. Chin, G. Gil, M.S. Brown, J.L. Goldstein, and K.L. Luskey (1984) HMG CoA reductase: A negatively regulated gene with unusual promoter and 5’ untranslated regions. Cell 38: 275–285.

    Article  PubMed  CAS  Google Scholar 

  • Roberts, D.D., C.N. Rao, J.L. Magnani, S.L. Spitalnick, L.A. Liotta, and V. Ginsburg (1985) Laminin binds specifically to sulfate glycolipids. Proc. Natl. Acad Sci. (USA) 82: 1306 - 1310.

    Article  CAS  Google Scholar 

  • Rogers, S.L., J.B. McCarthy, S.L. Palm, L.T. Furcht, and P.C. Letourneau (1985) Neuron- specific interactions with two neurite-promoting fragments of fibronectin. J. Neurosci. 2: 369–378.

    Google Scholar 

  • Schmidt, A., Y. Yamada, and B. de Crombrugghe (1984) DNA sequence comparison of the regulatory signals at the 5’ end of the mouse and chick alpha 2 type I collagen genes. J. Biol. Chem. 259: 7411–7415.

    PubMed  CAS  Google Scholar 

  • Strickland, S., K.K. Smith, and K.R. Marotti (1980) Hormonal induction of differentiation in teratocarcinoma stem cells: Generation of parietal endoderm by retinoic acid and dibutyryl camp. Cell 21: 347–355.

    Article  PubMed  CAS  Google Scholar 

  • Stroobant, P., A.P. Rice, W.J. Gullick, K.J. Cheng, I.M. Kerr, and M.D. Waterfield (1983) Purification and characterization of vaccinia virus growth factor. Cell 42: 383– 393.

    Article  Google Scholar 

  • Sudhof, T.C., J.L. Goldstein, M.S. Brown, and D.W. Russell (1985) The LDL receptor gene: A mosaic of exons shared with different proteins. Science 228: 815–822.

    Article  PubMed  CAS  Google Scholar 

  • Terranova, V.P., D. Rohrbach, and G.R. Martin (1982) Role of laminin in the attachment of PAM 212 (epithelial) cells to basement membrane collagen. Cell 22: 719–726.

    Article  Google Scholar 

  • Terranova, V.P., L.A. Liotta, R.G. Russo, and G.R. Martin (1982) Role of laminin in the attachment and metastasis of murine tumor cells. Cancer Res. 42: 2265–2269.

    PubMed  CAS  Google Scholar 

  • Terranova, V.P., C.N. Rao, T. Kalebic, I.M. Margulies, and L.A. Liotta (1983) Laminin receptor on human breast carcinoma cells. Proc. Natl. Acad. Sci. (USA) 80: 444– 448.

    Google Scholar 

  • Timpl, R., H. Rohde, P.G. Robey, S.I. Rennard, 3.M. Foidart, and G.R. Martin (1979) Laminin - a glycoprotein from basement membranes. J. Biol. Chem. 254: 9932– 9933.

    Google Scholar 

  • Timpl, R., and G.R. Martin (1982) Components of basement membrane. In Immuno- chemistry of Collagen, H. Furthmayr, ed., pp. 119–150, CRC Press, Cleveland, Ohio.

    Google Scholar 

  • Timpl, R., J. Engel, and G.R. Martin (1983) Laminin - a multifunctional protein of base-ment membranes. TIBS 8: 207–209.

    CAS  Google Scholar 

  • Towbin, H., T. Stachlin, and J. Gordon (1979) Electrophoretic transfer of proteins from polycrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. (USA) 76: 4350–4354.

    Article  CAS  Google Scholar 

  • Turpeenniemi-Hujanen, T., U.P. Thorgeirsson, C.N. Rao, and L.A. Liotta (1986) Laminin increases the release of type IV collagenase from malignant cells. J. Biol. Chem. 261: 1883–1889.

    PubMed  CAS  Google Scholar 

  • von der Mark, K., and U. Kuhl (1985) Laminin and its receptor. Biochem. Biophys. Acta 2: 147–160.

    Google Scholar 

  • Wang, S., G.J. LaRosa, and J. Gudus (1985) Molecular cloning of gene sequences tran-scriptionally regulated by retinoic acid and dibutyryl cyclic AMP in cultured mouse teratocarcinoma cells. Dev. Biol. 107: 75–86.

    Article  PubMed  CAS  Google Scholar 

  • Woodley, D.T., C.N. Rao, J.R. Hassell, L.A. Liotta, G.R. Martin, and H.K. Kleinman (1983) Interactions of basement membrane components. Biochem. Biophys. Acta. 761: 278–283.

    PubMed  CAS  Google Scholar 

  • Yamada, K.M. and S.K. Akiyama (1984) The interactions of cells with extracellular ma-trix components. In Cell Membranes, E. Elsan, W. Frazier, and L. Glaser, eds., pp. 77–148. Plenum, New York.

    Google Scholar 

  • Yamada, Y., M. Sasaki, K. Kohno, H.K. Kleinman, S. Kato, and G. Martin (1985) A novel structure for the protein and gene for the mouse laminin B1 chain u. In Basement Membrane, S. Shibata, ed., pp. 139–146. Elsevier Science, Amsterdam.

    Google Scholar 

  • Young, R.A., and R.W. Davis (1983) Efficient isolation of genes by using antibody probes. Proc. Natl. Acad. Sci. (USA) 80: 1194–1198.

    Article  CAS  Google Scholar 

Download references

Author information

Author notes

  1. S. Kato

    Present address: Sagami Chemical Research Center, Sagami, Kanagawa, Japan

  2. K. Kohno

    Present address: First Department of Internal Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan

  3. F. A. Robey

    Present address: Center for Drugs and Biologies, Food and Drug Administration, Bethesda, MD, USA

Authors and Affiliations

  1. Laboratory of Developmental Biology and Anomalies, National Institutes of Health, Bethesda, MD, USA

    Y. Yamada, A. Albini, I. Ebihara, J. Graf, S. Kato, P. Killen, H. K. Kleinman, K. Kohno, G. R. Martin, C. Rhodes, F. A. Robey & M. Sasaki

  2. National Institute of Dental Research, National Institutes of Health, Bethesda, MD, USA

    Y. Yamada, A. Albini, I. Ebihara, J. Graf, S. Kato, P. Killen, H. K. Kleinman, K. Kohno, G. R. Martin, C. Rhodes, F. A. Robey & M. Sasaki

Authors
  1. Y. Yamada
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. A. Albini
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. I. Ebihara
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. J. Graf
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. S. Kato
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. P. Killen
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. H. K. Kleinman
    View author publications

    You can also search for this author in PubMed Google Scholar

  8. K. Kohno
    View author publications

    You can also search for this author in PubMed Google Scholar

  9. G. R. Martin
    View author publications

    You can also search for this author in PubMed Google Scholar

  10. C. Rhodes
    View author publications

    You can also search for this author in PubMed Google Scholar

  11. F. A. Robey
    View author publications

    You can also search for this author in PubMed Google Scholar

  12. M. Sasaki
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. Berlin Institute for Advanced Study, Zentrum Anatomie, Kreuzbergring 36, 3400, Göttingen, Germany

    Joachim R. Wolff

  2. Universität Göttingen, Zentrum Anatomie, Kreuzbergring 36, 3400, Göttingen, Germany

    Joachim R. Wolff

  3. Anatomiches Institut, Universität Kiel, Olshausentr. 40-60, Haus N10, 2300, Kiel, Germany

    Jobst Sievers

  4. Department of Anatomy, Guy’s Hospital Medical School, London, SE1 9RT, England

    Martin Berry

Rights and permissions

Reprints and permissions

Copyright information

© 1987 Springer-Verlag Berlin Hedelberg

About this paper

Cite this paper

Yamada, Y. et al. (1987). Structure, Expression and Function of Mouse Laminin. In: Wolff, J.R., Sievers, J., Berry, M. (eds) Mesenchymal-Epithelial Interactions in Neural Development. NATO ASI Series, vol 5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71837-3_2

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-71837-3_2

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-71839-7

  • Online ISBN: 978-3-642-71837-3

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation