StayCurrentMD · Interplay between collagenase and undescended testes in Adamts16 knockout rats
Article1 min read·Published Feb 2020Older

Interplay between collagenase and undescended testes in Adamts16 knockout rats

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Article · Feb 2020 · 1 min read

In brief

In brief

Adamts16 knockout rats develop cryptorchidism due to impaired gubernacular migration during postnatal testicular descent. Histological analysis reveals excessive collagen accumulation in the inguinoscrotal fat pad when Adamts16 proteinase is absent, demonstrating that this enzyme is essential for ECM remodeling during normal testicular descent.

Written by the GCMD Library team from the article.

Abstract

Background

The inguinoscrotal stage of testicular descent is characterized by an increase in cell density and collagen fibers as the gubernaculum undergoes cell division and increases Extracellular Matrix (ECM) activity. Rats that lack the enzyme Adamts16, a known ECM proteinase, develop cryptorchidism postnatally and are infertile. Therefore, this study aims to investigate the link between the Adamts16 enzyme and congenital undescended testes (UDT) in Adamts16 knockout (KO) rats during postnatal development.

Methods

Formalin-fixed specimens of Wild-Type, Adamts16 heterozygous and Adamts16 homozygous KO rats post birth were sectioned and used for standard H&E histology and Masson's trichrome staining. A quantitative analysis on image J was performed to determine the intensity of collagen fibers within the inguinoscrotal fat pad (IFP) (n = 3 age/genotype).

Results

The migration of the gubernaculum within the Adamts16 heterozygous and Adamts16 KO rat was considerably disrupted. Furthermore, the Masson's trichrome staining demonstrated a significant increase in collagen fibers around the gubernaculum of rats that lacked Adamts16 enzyme at day 8.

Conclusion

This study reports a failure of gubernacular migration leading to UDT in Adamts16 KO rats during development, suggesting that the expression of Adamts16 gene is critical for normal gubernacular migration through the breakdown of collagen fibers within the IFP.

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