Amyloidosis of seminal vesicles and ejaculatory ducts: a histologic analysis of 21 cases among 447 prostatectomy specimens

Kee, Keun Hong; Lee, Mi Ja; Shen, Steven S.; Suh, Jae Hee; Lee, Ok Jun; Cho, Hyun Y.; Ayala, Alberto G.; Ro, Jae Y.

doi:10.1016/j.anndiagpath.2007.12.004

Cited by 26 publications

(18 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Amyloid fibril generation is also important for AMP activities, mediating disruption of microbial cell membranes (Sood et al, 2008), neutralization of bacterial endotoxins (Wang et al, 2014), and pathogen agglutination and entrapment (Chu et al, 2012; Torrent et al, 2012). However, dysregulated AMP oligomerization can also lead to serious pathologies, including inflammation, tissue degeneration (Paulsen et al, 2002; Pereira et al, 1996; Reinholz et al, 2012; Scarpa et al, 2012), and deposition as amyloid in at least three human amyloidopathies (Araki-Sasaki et al, 2005; Ciornei et al, 2006; Kee et al, 2008; Linke et al, 2005; Millucci et al, 2011; Pálffy et al, 2009; Reinholz et al, 2012; Scarpa et al, 2012; Yamaguchi et al, 2007; Zhao et al, 2008). Thus, AMP oligomerization carries a potential for protective/damaging duality in human health.…”

Section: Introductionmentioning

confidence: 99%

Alzheimer’s Disease-Associated β-Amyloid Is Rapidly Seeded by Herpesviridae to Protect against Brain Infection

Eimer

Kumar

Shanmugam

et al. 2018

Neuron

499

371

View full text Add to dashboard Cite

SUMMARY Amyloid-β peptide (Aβ) fibrilization and deposition as β-amyloid are hallmarks of Alzheimer’s disease (AD) pathology. We recently reported Aβ is an innate immune protein that protects against fungal and bacterial infections. Fibrilization pathways mediate Aβ antimicrobial activities. Thus, infection can seed and dramatically accelerate β-amyloid deposition. Here, we show Aβ oligomers bind herpesvirus surface glycoproteins, accelerating β-amyloid deposition and leading to protective viral entrapment activity in 5XFAD mouse and 3D human neural cell culture infection models against neurotropic herpes simplex virus 1 (HSV1) and human herpesvirus 6A and B. Herpesviridae are linked to AD, but it has been unclear how viruses may induce β-amyloidosis in brain. These data support the notion that Aβ might play a protective role in CNS innate immunity, and suggest an AD etiological mechanism in which herpesviridae infection may directly promote Aβ amyloidosis.

show abstract

Section: Introductionmentioning

confidence: 99%

Alzheimer’s Disease-Associated β-Amyloid Is Rapidly Seeded by Herpesviridae to Protect against Brain Infection

Eimer

Kumar

Shanmugam

et al. 2018

Neuron

499

371

View full text Add to dashboard Cite

show abstract

“…60,61 Furthermore, an amyloid pathology of the seminal vesicles of elderly men is also derived from an amyloid peptide, semenogelin. 62,63 The authors hypothesized that stimulation of the innate immune system could lead to the generation of Aβ and subsequent amyloid deposition. Alternatively, they considered that a CNS infection could lead to a self-perpetuating innate immune response.…”

Section: Antimicrobial Effects: β-Amyloid Peptidementioning

confidence: 99%

Antimicrobial Properties of Amyloid Peptides

et al. 2011

View full text Add to dashboard Cite

More than two dozen clinical syndromes known as amyloid diseases are characterized by the buildup of extended insoluble fibrillar deposits in tissues. These amorphous Congo red staining deposits known as amyloids exhibit a characteristic green birefringence and cross-β structure. Substantial evidence implicates oligomeric intermediates of amyloids as toxic species in the pathogenesis of these chronic disease states. A growing body of data has suggested that these toxic species form ion channels in cellular membranes causing disruption of calcium homeostasis, membrane depolarization, energy drainage, and in some cases apoptosis. Amyloid peptide channels exhibit a number of common biological properties including the universal U-shape β-strand-turn-β-strand structure, irreversible and spontaneous insertion into membranes, production of large heterogeneous single-channel conductances, relatively poor ion selectivity, inhibition by Congo red, and channel blockade by zinc. Recent evidence has suggested that increased amounts of amyloids are not only toxic to its host target cells but also possess antimicrobial activity. Furthermore, at least one human antimicrobial peptide, protegrin-1, which kills microbes by a channel-forming mechanism, has been shown to possess the ability to form extended amyloid fibrils very similar to those of classic disease-forming amyloids. In this paper, we will review the reported antimicrobial properties of amyloids and the implications of these discoveries for our understanding of amyloid structure and function.

show abstract

“…We observed these same findings as in previous studies and they guided us in the VSA diagnosis. (7). Although the incidence is similar in the two studies, having multicenter studies with a larger number of cases when we take the between-institution incidence variability into account would enable reaching a more balanced decision,…”

Section: Discussionmentioning

confidence: 94%

“…Linke et al have demonstrated that Semenogelin I consists of polypeptide fragments and these fragments are identical to the N-terminal region of the main secretion produced by the seminal vesicle (16). It is suggested that localized amyloidosis histogenesis is via the accumulation of the exocrine secretory product of the lining epithelium of the ejaculatory ductus system in the subepithelial seminal vesicle, vas deference and ejaculatory ducti by local diffusion (7,16).…”

Section: Discussionmentioning

confidence: 97%

See 1 more Smart Citation

Amyloidosis of seminal vesicles; incidence and pathologic characteristics

Argon¹,

Şimşir²,

Sarsık³

et al. 2012

TJPATH

View full text Add to dashboard Cite

Localized amyloidosis of seminal vesicles is not an unusual finding. amyloidosis of seminal vesicles incidence in Turkish patients included in this study and histopathologic characteristics of these patients are not different from the other studies. Systemic AA amyloidosis is the most common form of amyloidosis in our country. To be aware of amyloidosis of seminal vesicles is of importance in discrimination from the other forms of amyloidosis.

show abstract

Amyloidosis of seminal vesicles and ejaculatory ducts: a histologic analysis of 21 cases among 447 prostatectomy specimens

Cited by 26 publications

References 13 publications

Alzheimer’s Disease-Associated β-Amyloid Is Rapidly Seeded by Herpesviridae to Protect against Brain Infection

Alzheimer’s Disease-Associated β-Amyloid Is Rapidly Seeded by Herpesviridae to Protect against Brain Infection

Antimicrobial Properties of Amyloid Peptides

Amyloidosis of seminal vesicles; incidence and pathologic characteristics

Contact Info

Product

Resources

About