Cyclic protein-2, a secretory product of rat sertoli cells, is the proenzyme form of cathepsin L

Moira Erickson-Lawrence, Sonya D. Zabludoff, William W Wright

Research output: Contribution to journalArticle

Abstract

Previous studies demonstrated that secretion of Cyclic Protein-2 (CP-2) by mature rat Sertoli cells increased 30-fold from stage II to stages VI-VII of the cycle of the seminiferous epithelium and suggested that this protein was concentrated around compacted spermatids. Analysis of other organs revealed that CP-2 was also detectable in the epithelium of the proximal kidney tubule and in neurons originating from the supraoptic and paraventricular nuclei of the hypothalamus. We now have isolated a partial 1.8-kilobase (kb) cDNA for CP-2 mRNA, and sequence analysis revealed that CP-2 was the proenzyme form of the cysteine protease cathepsin L; this was corroborated by immunoprecipitation of CP-2 by anticathepsin L immunoglobulin G and by enzymatic analysis of purified CP-2. Northern analysis of testis mRNA revealed major (1.7 kb) and minor (2.2 kb) transcripts which differed in the length of their 3′-untranslated sequences. Low levels of CP-2/cathepsin L transcripts were detected in many organs, while high levels were only detected in testis, kidney, and liver. In seminiferous tubules, CP-2/ cathepsin L mRNA was undetectable at stage II, increased to maximal levels at stages VI and VIIa,b, and was again undetectable at stage XII. At stages VI-VII, CP-2/cathepsin L mRNA was present in Sertoli but not germ cells. Taken together, these data suggest that CP-2/cathepsin L gene expression is regulated in a cell-specific manner and that in Sertoli cells this expression is influenced by germ cells at specific steps of development. We propose that at stages V-VII, secreted CP-2/cathepsin L degrades adhesion molecules which bind compacted spermatids to Sertoli cells, thereby facilitating movement of these spermatids toward the lumen of the tubule.

Original languageEnglish (US)
Pages (from-to)1789-1798
Number of pages10
JournalMolecular Endocrinology
Volume5
Issue number12
StatePublished - 1991

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Cathepsin L
Enzyme Precursors
Sertoli Cells
Proteins
Spermatids
Messenger RNA
Germ Cells
Testis
Seminiferous Epithelium
Supraoptic Nucleus
Proximal Kidney Tubule
Seminiferous Tubules
Cysteine Proteases
Paraventricular Hypothalamic Nucleus
Fourier Analysis
Immunoprecipitation
Sequence Analysis

ASJC Scopus subject areas

  • Molecular Biology
  • Endocrinology, Diabetes and Metabolism

Cite this

Cyclic protein-2, a secretory product of rat sertoli cells, is the proenzyme form of cathepsin L. / Erickson-Lawrence, Moira; Zabludoff, Sonya D.; Wright, William W.

In: Molecular Endocrinology, Vol. 5, No. 12, 1991, p. 1789-1798.

Research output: Contribution to journalArticle

Erickson-Lawrence, Moira ; Zabludoff, Sonya D. ; Wright, William W. / Cyclic protein-2, a secretory product of rat sertoli cells, is the proenzyme form of cathepsin L. In: Molecular Endocrinology. 1991 ; Vol. 5, No. 12. pp. 1789-1798.
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