Surgeons rats

A critical process that occurs during lens fiber differen-tiation is the coordinated migration of elongating fiber ends along the epithelium (anteriorly) and the capsule (posteriorly). Fiber migration is a highly coordinated and regulated progres-sion that involves adhesion, translocation, and detachment of fiber ends, and on the posterior aspect the entire process is mediated by the basal membrane complex (BMC). The BMC of avian lens fibers includes the basal domain of the fiber-cell membrane, the integral membrane proteins, and their associ-ated cytoskeletal elements [1]. The BMC is an important area that includes molecules such as integrins, cadherins, actin, myosin, and caldesmon. Several molecules of the BMC, such as actin, β-1 integrin, and N-cadherin, have been studied to show their role in cell attachment, migration, and prolifera-tion during fiber differentiation. Studies have definitively shown that β-1 integrins are the primary integrin receptor for the basal lamina proteins in the lens capsule [2]. The integrins act as bidirectional signaling receptors [3], mediating interactions between the cytoskeleton and extracellular matrix that affect prolifera-tion, adhesion, and fiber-cell polarity [4-6]. N-cadherin, a cell adhesion molecule, has also been implicated in lens fiber differentiation. Through its linkage to actin, N-cadherin regulates differentiation-dependent cytoskeletal reorganiza-tion [7]. N-cadherin is co-localized with actin both within the native BMC and in cell culture [1,7-9]. In addition, actin has also been found to play an important role in coordinatin