Publications by authors named "Anjali Sharma-Bhandari"

Article Synopsis
  • Lysyl oxidase-variant 2 (LOX-v2) is a new variant of the enzyme LOX, involved in creating collagen and elastin in the extracellular matrix but lacks the N-terminal prepropeptide region.
  • * Research shows LOX-v2 primarily localizes in the nucleus of HEK293 cells, where it interacts with promyelocytic leukemia nuclear bodies (PML-NBs), which play roles in DNA repair and cell regulation.
  • * The overexpression of LOX-v2 increases SUMOylation levels in the nucleus, suggesting it has unique functions different from those of traditional LOX, particularly in relation to cellular processes occurring in PML-NBs.
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Lysyl oxidase (LOX) is an extracellular amine oxidase that mediates the formation of collagen fibers. Thus far, five LOX family genes [LOX, lysyl oxidase-like (LOXL)1, LOXL2, LOXL3 and LOXL4] have been identified in humans, each encoding the characteristic C-terminal domains that are required for amine oxidase activity. During osteoblastogenesis, collagen fibers function as a three-dimensional scaffold for organizing mineral deposition.

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