Logo image
Back
Identification and characterization of arginine vasopressin-like substances in the rat testis
Journal article   Open access   Peer reviewed

Identification and characterization of arginine vasopressin-like substances in the rat testis

B. G Kasson, R Meidan and A. J. W Hsueh
The Journal of biological chemistry, Vol.260(9), pp.5302-5306
1985
DOI: 10.1016/S0021-9258(18)89022-6
PMID: 3988755
url
https://doi.org/10.1016/S0021-9258(18)89022-6View
Published (Version of record) Open Access

Abstract

We have previously demonstrated the suppression of Leydig cell steroidogenesis by arginine vasopressin (AVP) in vitro. Since the circulating level of AVP is too low to mediate a testicular action of this peptide, we have conducted studies to identify testicular AVP-like substances. The supernatant of homogenized, acid-extracted rat testes was found to contain AVP immunoreactivity which showed parallelism with synthetic AVP in a specific radioimmunoassay for AVP. Chromatography of this extract on a Sephadex G-25 column produced three peaks of AVP immunoreactivity. The largest peak eluted close to the column void volume, a second smaller peak eluted at the total column volume, while a third peak co-eluted with synthetic AVP. Following acetone precipitation, ether extraction, and octadecylsilica (C18) adsorption chromatography of the acid extract, the third peak of AVP immunoreactivity (about 600 pg/testis) was fully retained by C18 chromatography and showed parallelism with synthetic AVP in both radioimmuno- and radioreceptor assays. This substance also co-migrated with synthetic AVP on both Sephadex G-25 and reverse-phase thin layer chromatography (RPTLC). The second peak was only partially retained by C18 adsorption chromatography, dilution curves were not parallel with synthetic AVP in radioimmuno- or radioreceptor assay, and this material failed to co-migrate with synthetic AVP on Sephadex G-25 and RPTLC. The first peak of apparent AVP immunoreactivity was associated with an enzyme(s) that degraded labeled AVP. This enzymatic activity, as well as the immunoreactivity, could be eliminated by heating the extract to 90 degrees C. These results demonstrate, by a number of independent criteria, that rat testes contain a substance which behaves like authentic AVP. Due to its high concentration, the AVP-like peptide may be synthesized or concentrated by testis cells. In addition, testis tissue contains enzymatic activity which degrades AVP and could represent a site of regulation of AVP action. Coupled with the previously demonstrated testis action of AVP, these results suggest a paracrine or autocrine role of the neurohypophysial hormone at the testis level.
 Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Biological and medical sciences Fundamental and applied biological sciences. Psychology Proteins

Details

Metrics

10 Record Views
77 Times Cited - Web of Science
Logo image