Abstract
.Collagen remodeling occurs in many prostate pathologies; however, the underlying structural architecture in both normal and diseased prostatic tissues is largely unexplored. Here, we use second-harmonic generation (SHG) microscopy to specifically probe the role of the proteoglycan decorin (Dcn) on collagen assembly in a wild type (wt) and Dcn null mouse (). Dcn is required for proper organization of collagen fibrils as it regulates size by forming an arch-like structure at the end of the fibril. We have utilized SHG metrics based on emission directionality (forward–backward ratio) and relative conversion efficiency, which are both related to the SHG coherence length, and found more disordered fibril organization in the . We have also used image analysis readouts based on entropy, multifractal dimension, and wavelet transforms to compare the collagen fibril/fiber architecture in the two models, where all these showed that the prostate comprised smaller and more disorganized collagen structures. All these SHG metrics are consistent with decreased SHG phase matching in the and are further consistent with ultrastructural analysis of collagen in this model in other tissues, which show a more random distribution of fibril sizes and their packing into fibers. As Dcn is a known tumor suppressor, this work forms the basis for future studies of collagen remodeling in both malignant and benign prostate disease.
Highlights
Proper collagen organization is critical for normal function and the architecture becomes abnormally assembled in many diseases, including connective tissue disorders, cancers, and fibroses
We examine the effect of loss of the structural protein decorin on collagen assembly in the prostate, where we quantify differences by using several secondharmonic generation (SHG) metrics developed in our laboratory.[9]
We have previously shown how second-harmonic generation (SHG) microscopy is a powerful tool for analyzing changes in collagen organization in many diseased states, including ovarian cancer, colon cancer, pulmonary fibrosis, and connective tissue disorders.[27,28,29,30]
Summary
Proper collagen organization is critical for normal function and the architecture becomes abnormally assembled in many diseases, including connective tissue disorders, cancers, and fibroses. In the connective tissue disorder osteogenesis imperfecta, the collagen is misfolded and results in incorrect fibril size and spacing, smaller fibers, and weaker mechanical structures.[1,2,3] Relatedly, the loss of Col V, which is essential for correct Col I fibril formation, results in numerous structural defects.[4,5] an increase in Col V and III have been associated with cancers and fibroses in several tissues.[6,7,8]
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
