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* Division of Matrix Biology, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts 02215; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02215; and Harvard-MIT Division of Health Sciences and Technology, Boston, Massachusetts 02139
To whom requests for reprints should be addressed at 1 Harvard Medical School, Division of Matrix Biology, Beth Israel Deaconess Medical Center, 330 Brookline Avenue (DANA 514), Boston, MA 02215. E-mail: rKalluri{at}BIDMC.Harvard.edu
Basement membranes (BMs) are present in every tissue of the human body. All epithelium and endothelium is in direct association with BMs. BMs are a composite of several large glycoproteins and form an organized scaffold to provide structural support to the tissue and also offer functional input to modulate cellular function. While collagen I is the most abundant protein in the human body, type IV collagen is the most abundant protein in BMs. Matrigel is commonly used as surrogate for BMs in many experiments, but this is a tumor-derived BM–like material and does not contain all of the components that natural BMs possess. The structure of BMs and their functional role in tissues are unique and unlike any other class of proteins in the human body. Increasing evidence suggests that BMs are unique signal input devices that likely fine tune cellular function. Additionally, the resulting endothelial and epithelial heterogeneity in human body is a direct contribution of cell-matrix interaction facilitated by the diverse compositions of BMs.
Key Words: basement membrane • assembly • type IV collagen • laminin • nidogen/entactin, perlecan • extracellular matrix • vascular • collagen
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