Galectin-3 is dispensable for thoracic aortic aneurysmal formation and rupture in mice.

Thoracic aortic aneurysm (TAA) development involves disruption of extracellular matrix structural proteins such as collagen and elastin. An increased level of Galectin-3 (Gal-3), a β-galactoside-binding lectin, was reported in ascending aortic aneurysmal patients. To examine the role of Gal-3 on TAA formation in mice, two models were used: administration of lysyl oxidase inhibitor, β-aminopropionitrile (BAPN 0.5%, 0.3%, and 0.1% wt/vol) to 3- to 4 -week-old male and female Gal-3 wild-type (WT) or deficient knockout (KO) mice for 4 weeks in drinking water; and 8- to 10-week-old Gal-3 WT or KO mice were infused with either saline or angiotensin II (AngII) via osmotic mini-pumps for 28 days. High or low doses of BAPN administration promoted TAA rupture-induced death equivalently in both WT and KO male (WT = 64%; KO = 73%) and female (WT = 41%; KO = 54%) mice compared with controls. Similarly, AngII infusion caused a significantly increased, but equivalent, dilation of thoracic aortas in both male and female Gal-3 and Gal-3 KO mice compared with controls. Histological analysis revealed increased elastin fragmentation and collagen accumulation in both BAPN- and AngII-infused male and female WT and KO mice compared with controls. These findings suggest that Gal-3 deficiency did not influence either BAPN- or AngII-induced TAA formation or rupture in mice.