Senile seminal vesicle amyloid is derived from semenogelin I

Linke, Reinhold P.; Joswig, R.; Murphy, Charles L.; Wang, Shuching; Zhou, Hui; Groß, Ulrich; Röcken, Christoph; Westermark, Per; Weiss, Deborah; Solomon, Alan

doi:10.1016/j.lab.2005.02.002

Cited by 52 publications

(30 citation statements)

References 31 publications

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“…SEM1(86-107) was, in fact, previously detected in SF by MS (8) but was not further analyzed because, at the time, the focus was on longer SEM peptides that overlapped with a region of SEM1 previously reported to be amyloidogenic in seminal vesicles (17). The inability of the present MS experiments to detect these longer SEM1 fragments in the SF stock is likely because of efficient PSA cleavage at internal sites within these peptides (4).…”

Section: Resultsmentioning

confidence: 82%

“…Importantly, whereas semen from healthy individuals markedly enhances HIV infection in vitro (8)(9)(10)(11)(12)(13)(14)(15)(16), semen samples naturally lacking SEMs due to ejaculatory duct obstruction (EDO) fail to enhance HIV infectivity (8). As amyloids derived from the SEMs have also been detected within the seminal vesicles of men, these fibrils may form even before semen emission (17).…”

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confidence: 99%

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Liquefaction of Semen Generates and Later Degrades a Conserved Semenogelin Peptide That Enhances HIV Infection

Roan

Liu

Usmani

et al. 2014

J Virol

106

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Semen enhances HIV infection in vitro, but how long it retains this activity has not been carefully examined. Immediately postejaculation, semen exists as a semisolid coagulum, which then converts to a more liquid form in a process termed liquefaction. We demonstrate that early during liquefaction, semen exhibits maximal HIV-enhancing activity that gradually declines upon further incubation. The decline in HIV-enhancing activity parallels the degradation of peptide fragments derived from the semenogelins (SEMs), the major components of the coagulum that are cleaved in a site-specific and progressive manner upon initiation of liquefaction. Because amyloid fibrils generated from SEM fragments were recently demonstrated to enhance HIV infection, we set out to determine whether any of the liquefaction-generated SEM fragments associate with the presence of HIVenhancing activity. We identify SEM1 from amino acids 86 to 107 [SEM1(86-107)] to be a short, cationic, amyloidogenic SEM peptide that is generated early in the process of liquefaction but that, conversely, is lost during prolonged liquefaction due to the activity of serine proteases. Synthetic SEM1(86-107) amyloids directly bind HIV-1 virions and are sufficient to enhance HIV infection of permissive cells. Furthermore, endogenous seminal levels of SEM1(86-107) correlate with donor-dependent variations in viral enhancement activity, and antibodies generated against SEM1(86-107) recognize endogenous amyloids in human semen. The amyloidogenic potential of SEM1(86-107) and its virus-enhancing properties are conserved among great apes, suggesting an evolutionarily conserved function. These studies identify SEM1(86-107) to be a key, HIV-enhancing amyloid species in human semen and underscore the dynamic nature of semen's HIV-enhancing activity. IMPORTANCESemen, the most common vehicle for HIV transmission, enhances HIV infection in vitro, but how long it retains this activity has not been investigated. Semen naturally undergoes physiological changes over time, whereby it converts from a gel-like consistency to a more liquid form. This process, termed liquefaction, is characterized at the molecular level by site-specific and progressive cleavage of SEMs, the major components of the coagulum, by seminal proteases. We demonstrate that the HIV-enhancing activity of semen gradually decreases over the course of extended liquefaction and identify a naturally occurring semenogelin-derived fragment, SEM1(86-107), whose levels correlate with virus-enhancing activity over the course of liquefaction. SEM1(86-107) amyloids are naturally present in semen, and synthetic SEM1(86-107) fibrils bind virions and are sufficient to enhance HIV infection. Therefore, by characterizing dynamic changes in the HIV-enhancing activity of semen during extended liquefaction, we identified SEM1(86-107) to be a key virus-enhancing component of human semen. Human semen is a complex biological fluid that begins as a gelatinous structure and, over time, undergoes regulated changes in consistenc...

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Section: Resultsmentioning

confidence: 82%

mentioning

confidence: 99%

Liquefaction of Semen Generates and Later Degrades a Conserved Semenogelin Peptide That Enhances HIV Infection

Roan

Liu

Usmani

et al. 2014

J Virol

106

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“…[58][59][60] Very few studies with IHC characterization have been performed, and results have been conflicting. [60][61][62] A single study on a few cases (n ¼ 5) has shown that the predominant subtype in this location, upon characterization with mass spectrometry, is semenogelin type 1; however, this number largely underestimates the total number of cases of SVA in the literature and easily in existence because SVA is not consistently reported on surgical pathology reports. 62 Only about 200 cases of primary bladder amyloidosis have been reported worldwide.…”

Section: Amyloidosis Of the Genitourinary Tractmentioning

confidence: 94%

“…[60][61][62] A single study on a few cases (n ¼ 5) has shown that the predominant subtype in this location, upon characterization with mass spectrometry, is semenogelin type 1; however, this number largely underestimates the total number of cases of SVA in the literature and easily in existence because SVA is not consistently reported on surgical pathology reports. 62 Only about 200 cases of primary bladder amyloidosis have been reported worldwide. 63 Primary (or secondary) amyloidosis of the urinary tract commonly masquerades as malignancy, indicating the clinical importance of the location.…”

Section: Amyloidosis Of the Genitourinary Tractmentioning

confidence: 94%

Biomarker, Molecular, and Technologic Advances in Urologic Pathology, Oncology, and Imaging

Ellis

Harik

Cohen

et al. 2017

Archives of Pathology &Amp; Laboratory Medicine

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Urologic pathology is evolving rapidly. Emerging trends include the expanded diagnostic utility of biomarkers and molecular testing, as well as adapting to the plethora of technical advances occurring in genitourinary oncology, surgical practice, and imaging. We illustrate those trends by highlighting our approach to the diagnostic workup of a few selected disease entities that pathologists may encounter, including newly recognized subtypes of renal cell carcinoma, pheochromocytoma, and prostate cancer, some of which harbor a distinctive chromosomal translocation, gene loss, or mutation. We illustrate applications of immunohistochemistry for differential diagnosis of needle core renal biopsies, intraductal carcinoma of the prostate, and amyloidosis and cite encouraging results from early studies using targeted gene expression panels to predict recurrence after prostate cancer surgery. At our institution, pathologists are working closely with urologic surgeons and interventional radiologists to explore the use of intraoperative frozen sections for margins and nerve sparing during robotic prostatectomy, to pioneer minimally invasive videoscopic inguinal lymphadenectomy, and to refine image-guided needle core biopsies and cryotherapy of prostate cancer as well as blue-light/fluorescence cystoscopy. This collaborative, multidisciplinary approach enhances clinical management and research, and optimizes the care of patients with urologic disorders. (Arch Pathol Lab Med. 2017;141:499-516; doi: 10.5858.arpa.2016-0263-SA) I n this review, we summarize the effect of a number of biomarker, molecular, and technologic advances in urologic pathology, oncology, and imaging on routine, day-to-day practice and research at our institution. The objective of this review is not to cover the entire gamut of all advances that we have and use at our institution but, rather, to highlight a few pertinent concepts in our field. Topics that will be covered include biomarkers, molecular testing of selected malignancies (eg, transcription factor E3 [TFE3]/ Xp11.2 translocation-associated renal cell carcinoma; p63, high-molecular-weight cytokeratin and racemase cocktail [PIN4]/phosphatase and tensin homolog [PTEN] for some cases of intraductal carcinoma of the prostate; and succinate dehydrogenase subunit B in renal cell carcinoma and pheochromocytoma), amyloidosis of the genitourinary tract, and workup of neoplastic needle core kidney biopsies. In addition, we will report the effect of pathologic, oncologic, and radiologic technologic advances (ie, global transcriptome analysis and RNA biomarkers of prostate cancer; robotic-assisted radical prostatectomy; minimally invasive videoscopic inguinal lymphadenectomy; targeted magnetic resonance imaging [MRI]-guided prostate needle core biopsies; anti-1-amino-3-fluorine 18-fluorocyclobutane-1-carboxylic acid in prostate cancer; cryotherapy for prostate cancer; and blue-light/white-light cystoscopy for bladder lesions) performed at our institution.

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“…Quelle est leur fonction physiologique ? Des fragments de SEM étant détectés dans les vési-cules séminales [14], il est possible que les fibrilles de SEM commencent à se former avant l'émission du sperme. Bien que les fibrilles de SEVI et SEM soient dérivées de protéines complètement SEVI et les fibrilles amyloïdes de SEM partagent de multiples propriétés.…”

Section: Les Fibrilles Amyloïdes Du Spermeunclassified