Anti-Collagen Type I, II, III, IV, V (native) polyclonal antibody

Salen with two aza-crown ether pendants H2L1 and its analogues H2L2--H2L4 were successfully synthesized starting from benzo-10-aza-15-crown-5 (BN15C5) or morpholine. Their structures were characterized by IR, MS, H-1 NMR and elemental analysis, and were confirmed by X-ray diffraction analysis of H2L1. Moreover, the saturated oxygen uptake of their cobalt(II) complexes CoL1-CoL4 in diethyleneglycol dimethyl ether was determined at different temperature. The oxygenation contants ( K-O2) and thermodynamic parameters (DeltaHdegrees and DeltaSdegrees) were calculated. The modulation of O-2-binding capabilities by pendant substituents were investigated as compared with the parent Schiff base complex CoL5 (CoSalen). The results indicate that the dioxygen affinities of CoL have been much more enhanced by aza-crown pendants than that by morpholino pendants, and the O-2-binding capabilities of CoL1 and CoL2 with aza-crown pendants would also be enhanced by adding alkali metal cations.

The glomerular basement membrane (GBM) is a critical component of the kidney's blood filtration barrier. Alport syndrome, a hereditary disease leading to kidney failure, is caused by the loss or dysfunction of the GBM's major collagen type IV (COLA) isoform alpha(3),alpha(4),alpha(5). The constituent COL4 alpha-chains assemble into heterotrimers in the endoplasmic reticulum before secretion into the extracellular space. If any one of the alpha(3)-,alpha(4)- or alpha(5)-chains is lost due to mutation of one of the genes, then the entire heterotrimer is lost. Patients with Alport syndrome typically have mutations in the X-linked COL4A5 gene or uncommonly have the autosomal recessive form of the disease due to COL4A3 or COL4A4 mutations. Treatment for Alport syndrome is currently limited to angiotensin-converting enzyme inhibition or angiotensin receptor blockers. Experimental approaches in Alport mice have demonstrated that induced expression of COL4A3. either widely or specifically in podocytes of Col4a3(-/-) mice, can abrogate disease progression even after establishment of the abnormal GBM. While targeting podocytes in vivo for gene therapy is a significant challenge, the more accessible glomerular endothelium could be amenable for mutant gene repair. In the present study, we expressed COL4A3 in Col4a3(-/-) Alport mice using an endothelial cell-specific inducible transgenic system, but collagen-alpha(3)alpha(4)alpha(5) (IV) was not detected in the GBM or elsewhere, and the Alport phenotype was not rescued. Our results suggest that endothelial cells do not express the Col4a3/a4/a5 genes and should not be viewed as a target for gene therapy.