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Presentation
Absence of Col11a1 Downregulates BMP-2 Induced Phosphorylation of Smad1/5/8
Idaho Conference on Undergraduate Research
  • Amanda Stauffer
  • Neda Shefa, Boise State University
  • Julia Oxford, (Mentor), Boise State University
Abstract
Collagen XI (Col11a1) is a heterotrimeric, extracellular matrix protein involved in fibrillogenesis and cell signaling during osteoblast maturation. Alternative splicing of the Col11a1 gene results in up to eight different isoforms. Mutations in Col11a1 can result in Marshall syndrome, Type II Stickler syndrome, and Fibrochondrogenesis. In the absence of Col11a1 protein, abnormally thick collagen fibrils form, disrupting the structural stability of the extracellular matrix. To better understand the role of Col11a1 in bone formation, we hypothesize that BMP-2 signaling is altered in the absence of Col11a1. We treated C2C12 cells with Col11a1 siRNA and performed western blots to assess BMP-2 induced smad1/5/8 phosphorylation. Our results suggest a downregulation of phospho-smad1/5/8 in the absence of Col11a1. Our findings indicate that Col11a1 may be an important regulator of BMP signaling during bone formation.
Citation Information
Amanda Stauffer, Neda Shefa and Julia Oxford. "Absence of Col11a1 Downregulates BMP-2 Induced Phosphorylation of Smad1/5/8"
Available at: http://works.bepress.com/julia_oxford/52/