Rabbit Polymorphonuclear Neutrophils Form35S-LabeledS-Sulfo-calgranulin C When Incubated with Inorganic [35S]Sulfate Academic Article uri icon

abstract

  • Rabbit peritoneal polymorphonuclear neutrophils reduced inorganic [35S]sulfate to [35S]sulfite in vitro, concomitant with incorporation of 35S into a 10.68-kDa cytosolic protein as a S-[35S]sulfo-derivative. Amino-terminal sequencing of the purified protein identified calgranulin C, a member of the S100 protein family. cDNA clones of calgranulins B and C were isolated using oligonucleotide primers based on the established amino acid sequences of other mammalian calgranulins. The complete amino acid sequence of rabbit calgranulin C was deduced from the nucleotide sequence of the corresponding cDNA. It comprises 91 amino acid residues, has a calculated molecular mass of 10.52 kDa, has 74% identity with porcine calgranulin C, and shows high homology with other S100 calcium-binding proteins. Rabbit calgranulin C has a single cysteine residue at position 30, which we believe to be modified to S-[35S]sulfo-cysteine as a consequence of sulfate reduction by neutrophils. The formation of S-[35S]sulfo-calgranulin C appears to be a reaction specific to neutrophils. The specific radioactivity of calgranulin C from the neutrophil culture medium was 50-fold greater than that of the calgranulin C within the cells, suggesting that S-sulfation of calgranulin C might be associated with its secretion.

authors

  • Yang, Zheng
  • deVeer, Michael J
  • Gardiner, Elizabeth E
  • Devenish, Rodney J
  • Handley, Christopher J
  • Underwood, John R
  • Robinson, H Clem

publication date

  • August 16, 1996

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