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Gene Review

Nid1  -  nidogen 1

Rattus norvegicus

Synonyms: Entactin, NID-1, Nid, Nidogen-1
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Disease relevance of Nid1


High impact information on Nid1

  • Protein A-gold immunocytochemistry was applied in combination with morphometrical approaches to reveal the alpha 1(IV), alpha 2(IV), and alpha 3(IV) chains of type IV collagen as well as entactin on renal basement membranes, particularly on the glomerular one, during maturation [6].
  • In the glomerulus at the capillary loop stage, both the epithelial and endothelial cell basement membranes were labeled for the alpha 1(IV) and alpha 2(IV) chains of type IV collagen and entactin [6].
  • The Arg-Gly-Asp cell recognition sequence is present in one of the EGF-type repeats, and a synthetic peptide from the putative cell-binding site of entactin was found to promote the attachment of mouse mammary tumor cells [7].
  • The complete amino acid sequence of mouse entactin has been derived from sequencing of cDNA clones [7].
  • The major constituents of this reconstituted matrix are collagen type IV, laminin, heparan sulfate proteoglycan, entactin, and nidogen [8].

Chemical compound and disease context of Nid1


Biological context of Nid1

  • The entactin gene is expressed early in mouse embryogenesis [1].
  • Two cDNA clones complementary to rat entactin mRNA were isolated by antibody screening of an oligo(dT)-primed cDNA library constructed in the lambda gt11 expression vector [1].
  • The cDNA insert, 1328 base pairs long, was sequenced and found to contain an open reading frame of 729 base pairs that coded for 243 amino acids at the carboxyl terminus of entactin [1].
  • Perturbation experiments using monoclonal antibodies directed against entactin-1 (nidogen-1) were performed with peritubular cells and Sertoli cells, respectively, and demonstrated loss of cell adhesion of the peritubular cells, while the Sertoli cells remained adherent [9].
  • Treatment with N-glycanase reduces the molecular mass of entactin and eliminates 9H6 binding, suggesting that the 9H6 epitope at synapses is dependent on glycosylation [10].

Anatomical context of Nid1


Associations of Nid1 with chemical compounds

  • We have purified the factor responsible for this effect from medium conditioned by bovine corneal endothelial cells, and have shown that it is composed of the glycoprotein laminin and two associated laminin-binding molecules: a sulfated protein known as entactin, and a large heparan sulfate proteoglycan [12].
  • The RGD (RGDS-NH2) sequence, found in the cell binding domain of the integrin family of cell adhesion molecules as well as in the A chain of laminin and in entactin, effectively inhibited Sertoli cell cord formation at a concentration of 1.0 mg/ml but was unable to prevent Sertoli cell attachment at concentrations as high as 2.0 mg/ml [13].
  • Laminin is a cross-shaped glycoprotein whose inner cross-region binds to the glycoprotein entactin (nidogen) forming a stable complex extractable from basement membrane matrices with chelating agents [14].
  • Meprin A also degraded purified nidogen into similar breakdown products [2].
  • Slot blot analysis of poly-A RNA demonstrated a significant (P < 0.01) increase in the level of entactin messenger RNA (mRNA) by 140% (P < 0.01) and a 50% reduction of type IV collagen alpha1 chain mRNA after thyroid hormone treatment [15].

Regulatory relationships of Nid1


Other interactions of Nid1


Analytical, diagnostic and therapeutic context of Nid1


  1. Carboxyl-terminal sequence of entactin deduced from a cDNA clone. Durkin, M.E., Carlin, B.E., Vergnes, J., Bartos, B., Merlie, J., Chung, A.E. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  2. Meprin A, the major matrix degrading enzyme in renal tubules, produces a novel nidogen fragment in vitro and in vivo. Walker, P.D., Kaushal, G.P., Shah, S.V. Kidney Int. (1998) [Pubmed]
  3. Entactin gene expression in normal and fibrotic rat liver and in rat liver cells. Schwoegler, S., Neubauer, K., Knittel, T., Chung, A.E., Ramadori, G. Lab. Invest. (1994) [Pubmed]
  4. Differential effects of diabetes and glomerulonephritis on glomerular basement membrane composition. Brees, D.K., Hutchison, F.N., Cole, G.J., Williams, J.C. Proc. Soc. Exp. Biol. Med. (1996) [Pubmed]
  5. Induction of rat yolk sac carcinomas with consistent pattern of laminin, entactin, and type IV collagen biosynthesis. Wewer, U. Acta pathologica, microbiologica, et immunologica Scandinavica. Section A, Pathology. (1984) [Pubmed]
  6. Ontogenesis of glomerular basement membrane: structural and functional properties. Desjardins, M., Bendayan, M. J. Cell Biol. (1991) [Pubmed]
  7. Amino acid sequence and domain structure of entactin. Homology with epidermal growth factor precursor and low density lipoprotein receptor. Durkin, M.E., Chakravarti, S., Bartos, B.B., Liu, S.H., Friedman, R.L., Chung, A.E. J. Cell Biol. (1988) [Pubmed]
  8. Schwann cell myelination: induction by exogenous basement membrane-like extracellular matrix. Carey, D.J., Todd, M.S., Rafferty, C.M. J. Cell Biol. (1986) [Pubmed]
  9. Mesenchymal entactin-1 (nidogen-1) is required for adhesion of peritubular cells of the rat testis in vitro. Konrad, L., Albrecht, M., Renneberg, H., Ulrix, W., Hoeben, E., Verhoeven, G., Aumüller, G. Eur. J. Cell Biol. (2000) [Pubmed]
  10. A novel epitope of entactin is present at the mammalian neuromuscular junction. Chiu, A.Y., Ko, J. J. Neurosci. (1994) [Pubmed]
  11. Expression of nidogens in rat uterus and embryo during decidualization and implantation. Oner, H., Oner, J., Demir, R. J. Morphol. (2006) [Pubmed]
  12. Purification of a factor that promotes neurite outgrowth: isolation of laminin and associated molecules. Lander, A.D., Fujii, D.K., Reichardt, L.F. J. Cell Biol. (1985) [Pubmed]
  13. Laminin promotes formation of cord-like structures by Sertoli cells in vitro. Hadley, M.A., Weeks, B.S., Kleinman, H.K., Dym, M. Dev. Biol. (1990) [Pubmed]
  14. Modulation of angiogenesis in vitro by laminin-entactin complex. Nicosia, R.F., Bonanno, E., Smith, M., Yurchenco, P. Dev. Biol. (1994) [Pubmed]
  15. Regulation by thyroid hormone of the expression of basement membrane components in rat prepubertal Sertoli cells. Ulisse, S., Rucci, N., Piersanti, D., Carosa, E., Graziano, F.M., Pavan, A., Ceddia, P., Arizzi, M., Muzi, P., Cironi, L., Gnessi, L., D'Armiento, M., Jannini, E.A. Endocrinology (1998) [Pubmed]
  16. Entactin expression by rat lung and rat alveolar epithelial cells. Senior, R.M., Griffin, G.L., Mudd, M.S., Moxley, M.A., Longmore, W.J., Pierce, R.A. Am. J. Respir. Cell Mol. Biol. (1996) [Pubmed]
  17. Extracellular matrix remodeling at the early stages of liver regeneration in the rat. Kim, T.H., Mars, W.M., Stolz, D.B., Petersen, B.E., Michalopoulos, G.K. Hepatology (1997) [Pubmed]
  18. Assembly of the exogenous extracellular matrix during basement membrane formation by alveolar epithelial cells in vitro. Furuyama, A., Mochitate, K. J. Cell. Sci. (2000) [Pubmed]
  19. Rat mesangial cells express two unique isoforms of laminin which modulate mesangial cell phenotype. Hansen, K.M., Berfield, A.K., Spicer, D., Abrass, C.K. Matrix Biol. (1998) [Pubmed]
  20. Modulation of extracellular matrix glycoproteins production by in vitro interacting conditions between rat colonic fibroblasts and tumoral cells. Perrin, P., Ringeard, S., Harb, J., Meflah, K., Menanteau, J. Cell Biol. Int. Rep. (1992) [Pubmed]
  21. Deposition of fibronectin and laminin in the basement membrane of the rat parietal yolk sac: immunohistochemical and biosynthetic studies. Amenta, P.S., Clark, C.C., Martinez-Hernandez, A. J. Cell Biol. (1983) [Pubmed]
  22. Cooperation of Ito cells and hepatocytes in the deposition of an extracellular matrix in vitro. Loréal, O., Levavasseur, F., Fromaget, C., Gros, D., Guillouzo, A., Clément, B. Am. J. Pathol. (1993) [Pubmed]
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