Possible Role for Two Calcium-Binding Proteins of the S-100 Family, Co-Expressed in Granulocytes and Certain Epithelia
Calgranulins A and B - originally designated cystic fibrosis antigen (CFAG) - were first recognized as components of an anonymous serum protein found at elevated level in cystic fibrosis (CF) homozygotes and heterozygotes (van Heyningen et al., 1985; Hayward et al., 1987). Polyclonal and monoclonal antibodies recognizing this protein were used in tissue localization, chromosomal mapping, and purification of the heteropolymeric protein (van Heyningen et al., 1985; Dorin et al., 1987). Partial N-terminal aminoacid analysis revealed one polypeptide. Multiple redundant synthetic oligonucleotides corresponding to part of this sequence were used to isolate a clone encoding this gene from a chronic myeloid leukemia (CML) cDNA library (Dorin et al., 1987). The deduced aminoacid sequence of the gene product showed homology to: S-100 a and b, intestinal calcium-binding protein, calcyclin, and to the 11K calpactin light chain (Dorin et al.,1987) as well as to p9Ka which has been associated with breast cancer (Barraclough et al., 1987; Murphy et al., 1988). Clones encoding part of a second polypeptide with a blocked N-terminus (Michal Novak personal communication; Odink et al., 1987) were isolated subsequently from the same CML cDNA library, using the published sequence information of Odink et al. (1987). This second subunit, calgranulin B, also shows homology to the S-100 family, with approximately the same degree of similarity to calgranulin A as to other members of the S-100 family.
KeywordsCystic Fibrosis Chronic Myeloid Leukemia Chloride Channel Cystic Fibrosis Airway Exocrine Pancreatic Insufficiency
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