Still more complexity in mammalian basement membranes.

Research output: Contribution to journal › Journal article › Research › peer-review

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Still more complexity in mammalian basement membranes. / Erickson, A C; Couchman, J R.

In: Journal of Histochemistry and Cytochemistry, Vol. 48, No. 10, 2000, p. 1291-306.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Erickson, AC & Couchman, JR 2000, 'Still more complexity in mammalian basement membranes.', Journal of Histochemistry and Cytochemistry, vol. 48, no. 10, pp. 1291-306.

APA

Erickson, A. C., & Couchman, J. R. (2000). Still more complexity in mammalian basement membranes. Journal of Histochemistry and Cytochemistry, 48(10), 1291-306.

Vancouver

Erickson AC, Couchman JR. Still more complexity in mammalian basement membranes. Journal of Histochemistry and Cytochemistry. 2000;48(10):1291-306.

Author

Erickson, A C ; Couchman, J R. / Still more complexity in mammalian basement membranes. In: Journal of Histochemistry and Cytochemistry. 2000 ; Vol. 48, No. 10. pp. 1291-306.

Bibtex

@article{5a3561c0597011dd8d9f000ea68e967b,
title = "Still more complexity in mammalian basement membranes.",
abstract = "At the epithelial/mesenchymal interface of most tissues lies the basement membrane (BM). These thin sheets of highly specialized extracellular matrix vary in composition in a tissue-specific manner, and during development and repair. For about two decades it has been apparent that all BMs contain laminins, entactin-1/nidogen-1, Type IV collagen, and proteoglycans. However, within the past few years this complexity has increased as new components are described. The entactin/nidogen (E/N) family has expanded with the recent description of a new isoform, E/N-2/osteonidogen. Agrin and Type XVIII collagen have been reclassified as heparan sulfate proteoglycans (HSPGs), expanding the repertoire of HSPGs in the BM. The laminin family has become more diverse as new alpha-chains have been characterized, increasing the number of laminin isoforms. Interactions between BM components are now appreciated to be regulated through multiple, mostly domain-specific mechanisms. Understanding the functions of individual BM components and their assembly into macromolecular complexes is a considerable challenge that may increase as further BM and cell surface ligands are discovered for these proteins.",
author = "Erickson, {A C} and Couchman, {J R}",
note = "Keywords: Agrin; Animals; Basement Membrane; Carrier Proteins; Cell Adhesion Molecules; Collagen; Humans; Laminin; Membrane Glycoproteins; Proteoglycans",
year = "2000",
language = "English",
volume = "48",
pages = "1291--306",
journal = "Journal of Histochemistry and Cytochemistry",
issn = "0022-1554",
publisher = "SAGE Publications",
number = "10",

}

RIS

TY - JOUR

T1 - Still more complexity in mammalian basement membranes.

AU - Erickson, A C

AU - Couchman, J R

N1 - Keywords: Agrin; Animals; Basement Membrane; Carrier Proteins; Cell Adhesion Molecules; Collagen; Humans; Laminin; Membrane Glycoproteins; Proteoglycans

PY - 2000

Y1 - 2000

N2 - At the epithelial/mesenchymal interface of most tissues lies the basement membrane (BM). These thin sheets of highly specialized extracellular matrix vary in composition in a tissue-specific manner, and during development and repair. For about two decades it has been apparent that all BMs contain laminins, entactin-1/nidogen-1, Type IV collagen, and proteoglycans. However, within the past few years this complexity has increased as new components are described. The entactin/nidogen (E/N) family has expanded with the recent description of a new isoform, E/N-2/osteonidogen. Agrin and Type XVIII collagen have been reclassified as heparan sulfate proteoglycans (HSPGs), expanding the repertoire of HSPGs in the BM. The laminin family has become more diverse as new alpha-chains have been characterized, increasing the number of laminin isoforms. Interactions between BM components are now appreciated to be regulated through multiple, mostly domain-specific mechanisms. Understanding the functions of individual BM components and their assembly into macromolecular complexes is a considerable challenge that may increase as further BM and cell surface ligands are discovered for these proteins.

AB - At the epithelial/mesenchymal interface of most tissues lies the basement membrane (BM). These thin sheets of highly specialized extracellular matrix vary in composition in a tissue-specific manner, and during development and repair. For about two decades it has been apparent that all BMs contain laminins, entactin-1/nidogen-1, Type IV collagen, and proteoglycans. However, within the past few years this complexity has increased as new components are described. The entactin/nidogen (E/N) family has expanded with the recent description of a new isoform, E/N-2/osteonidogen. Agrin and Type XVIII collagen have been reclassified as heparan sulfate proteoglycans (HSPGs), expanding the repertoire of HSPGs in the BM. The laminin family has become more diverse as new alpha-chains have been characterized, increasing the number of laminin isoforms. Interactions between BM components are now appreciated to be regulated through multiple, mostly domain-specific mechanisms. Understanding the functions of individual BM components and their assembly into macromolecular complexes is a considerable challenge that may increase as further BM and cell surface ligands are discovered for these proteins.

M3 - Journal article

C2 - 10990484

VL - 48

SP - 1291

EP - 1306

JO - Journal of Histochemistry and Cytochemistry

JF - Journal of Histochemistry and Cytochemistry

SN - 0022-1554

IS - 10

ER -

ID: 5163313