Characterization of lamprin, an unusual matrix protein from lamprey cartilage. Implications for evolution, structure, and assembly of elastin and other fibrillar proteins.

@article{Robson1993CharacterizationOL,
  title={Characterization of lamprin, an unusual matrix protein from lamprey cartilage. Implications for evolution, structure, and assembly of elastin and other fibrillar proteins.},
  author={Paul Robson and Glenda M. Wright and E E Sitarz and Arpita Maiti and Mamta Rawat and John H. Youson and Fred W. Keeley},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 2},
  pages={1440-7}
}
Lamprin, an insoluble non-collagen, non-elastin protein, is the major connective tissue component of the fibrillar extracellular matrix of lamprey annular cartilage. Here we demonstrate that the soluble monomer of lamprin is a family of highly hydrophobic, self-aggregating proteins with molecular masses of 12 and 10 kDa. Two mRNAs for soluble lamprin were identified (0.9 and 2 kilobases), differing principally in the length of their 3'-untranslated tails. Variants of soluble lamprin appear to… CONTINUE READING