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J. Biol. Chem., Vol. 277, Issue 1, 233-242, January 4, 2002

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Characterization and Cloning of Two Isoforms of Heteroglobin, a Novel Heterodimeric Glycoprotein of the Secretoglobin-Uteroglobin Family Showing Tissue-specific and Sex Differential Expression^*

Javier Alvarez, Jorge Viñas^§, José M. Martín Alonso, Juan Pablo Albar^¶, Keith Ashman, and Pedro Domínguez^**

From the  Departamento de Bioquímica y Biología Molecular, Edificio Santiago Gascón, Universidad de Oviedo, 33006 Oviedo, Spain, ^¶ Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Campus de Cantoblanco, Universidad Autónoma, 28049 Madrid, Spain, and  Samuel Lunenfeld Institute, Toronto MSG 1X5, Canada

Heteroglobin (HGB) is a 39-kDa heterodimeric protein detected under non-reducing conditions in harderian, parotid, and submaxillary glands and saliva of the Syrian hamster with antiserum raised against the carboxyl end deduced from the female harderian gland cDNA FHG22 (Domínguez, P. (1995) FEBS Lett. 376, 257-261). After reduction, only one 5.6-kDa polypeptide, named HGB.A, was immunodetected and identified by sequencing as the mature FHG22 product. Tissue-specific expression of HGB.A and HGB mimics that of FHG22 mRNA, with sex differences in submaxillary and harderian glands. Purification of HGB revealed it consists of HGB.A disulfide bonded to HGB.B, a 33.5-kDa N-glycosylated subunit that yields a 9-kDa core polypeptide after deglycosylation. Two highly homologous (96.2%) cDNA clones (HGB.B1 and HGB.B2) encoding 94 amino acid-long isoforms were identified by screening a female harderian gland library with an HGB.B probe. The corresponding mature polypeptides are 78 amino acids long with 12 differences, but 3 putative N-glycosylation sites are maintained. The expression of HGB.B mRNAs is parallel to that of HGB and HGB.A, but no HGB.B2 mRNA was detected in submaxillary glands. Homology studies indicate that HGB.A and HGB.B1/HGB.B2 belong to different subfamilies of the secretoglobin-uteroglobin family and form heterodimers as previously described.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AJ252138 and AJ252139.

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