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Endocrinology Vol. 141, No. 12 4413-4418
Copyright © 2000 by The Endocrine Society

ARTICLES

Molecular Cloning and Expression of a Functionally Different Alternative Splice Variant of Prointerleukin-1{alpha} from the Rat Testis1

Taranum Sultana, Konstantin Svechnikov, Günther Weber and Olle Söder

Department of Woman and Child Health, Pediatric Endocrinology Unit, and Department of Molecular Medicine, Clinical Genetics Unit, Karolinska Institute and Hospital, S-17176 Stockholm, Sweden; and Endocrinological Genetics Unit, Institute of Cytology and Genetics, 630090 Novosibirsk, Russia

Address all correspondence and requests for reprints to: Olle Söder, M.D., Ph.D., Department of Woman and Child Health, Pediatric Endocrinology Unit, Astrid Lindgren Children’s Hospital, S-17176 Stockholm, Sweden. E-mail: olle.soder{at}kbh.ki.se

We report here the characterization of an alternative splice variant of prointerleukin-1{alpha} (proIL-1{alpha}), constitutively expressed by the normal adult rat testis. In addition to the classical 32K proIL-1{alpha} (32proIL-1{alpha}) messenger RNA, the testis produced a shorter variant encoding a putative protein of 24K (24proIL-1{alpha}). In situ hybridization demonstrated constitutive expression of the splice transcript in the seminiferous tubules. This alternative complementary DNA lacked the fifth exon, harboring the calpain cleavage site essential for generation of mature 17K IL-1{alpha}. This was verified by calpain treatment, producing the expected cleavage products of recombinant 32proIL-1{alpha}, but not of 24proIL-1{alpha}. Similarly, expression in COS-7 cells demonstrated processing of 32proIL-1{alpha} to the mature 17K form and secretion, whereas 24proIL-1{alpha} remained unprocessed. Both 32proIL-1{alpha} and 24proIL-1{alpha} showed a dose-dependent stimulatory effect in a thymocyte proliferation assay, although at lower potency than mature 17K IL-1{alpha}. In contrast, when tested on hCG-stimulated Leydig cells in vitro, a dose-dependent inhibition of testosterone production was obtained with mature 17K IL-1{alpha} and at a lower potency with 32proIL-1{alpha}, whereas 24proIL-1{alpha} was inactive. In conclusion, the three IL-1 bioactive proteins described here contribute to IL-1 protein heterogeneity and may serve as constitutive paracrine mediators in the testis.




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