Hematopoietic stem cell cytokines and fibroblast growth factor-2 stimulate human endothelial cell-pericyte tube co-assembly in 3D fibrin matrices under serum-free defined conditions.
Authors: Smith A, Bowers S, Stratman A, Davis G
PLoS ONE, 2013;8(12):e85147.
Species: Human
Sample Type: Whole Cells
Application: ICC Fluorescence
Pericyte recruitment during vasculogenic tube assembly stimulates endothelial basement membrane matrix formation.
Authors: Stratman AN, Malotte KM, Mahan RD, Davis MJ, Davis GE
Blood, 2009;114(24):5091-101.
Species: Human
Sample Type: Cell Lysates
Application: WB

Nidogen-1 (also entactin) is a 150 kDa, secreted, monomeric glycoprotein that serves as a major linking component of basement membranes (1-4). It is synthesized as a 1247 amino acid (aa) precursor with a 28 aa signal sequence and a 1219 aa mature protein. The molecule is modular in structure with five distinct regions. There are three globular domains (G1-3) separated by a mucin region and an extended rod-shaped segment (5-7). The N-terminal globular domain (G1) is 200 aa in length and seemingly unrelated to any known motif (8). The mucin region is nearly 160 aa in length and presumably O-glycosylated (2, 8). G2 and G3 are both approximately 300 aa in length. G2 is described as a Nidogen ( beta -barrel) domain, while C-terminal G3 assumes a beta -propeller configuration (1). The 250 aa rod-shaped segment has multiple EGF-like motifs and two thyroglobulin type 1 domains. Functionally, G1 is reported to bind type IV collagen (2, 7). The mucin region contains a short peptide that ligates alpha ₃beta₁ integrins (9, 10). G2 interacts with perlecan, and an RGD motif in the rod-shaped segment serves as a binding site for alpha _vbeta₃ integrins (9, 10). Finally, G3 is associated with laminin binding (2, 7). As a full-length molecule, the multiple extracellular matrix-binding sites of Nidogen-1 are well positioned to serve as anchor sites for basement membrane molecules. Nidogen-1 also undergoes proteolytic processing by at least two MMPs, MMP-7 and MMP-19 (10, 11). While this destroys the integrity of Nidogen-associated matrices, it also generates peptide fragments that are capable of inducing neutrophil chemotaxis and phagocytosis (10). Nidogen-2 is related to Nidogen-1 (≈ 50% aa identity) and shares many of the same adhesive properties as Nidogen-1 (12). Both bind perlecan plus collagens I and IV. Nidogen‑2, however, does not bind fibulin-1 or 2, and shows only modest interaction with laminin. Thus, although coexpressed, Nidogen-2 serves as only a partial substitute for Nidogen-1 (2, 12). Human Nidogen-1 shares 85% aa sequence identity with both mouse and rat Nidogen-1, and 88% aa sequence identity with canine Nidogen-1.

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