scholarly journals Dual concentration-dependent effect of Ascorbic acid on PAP(248-286) amyloid formation and SEVI-mediated HIV infection

2021 ◽  
Author(s):  
Daniel Segal ◽  
Jan Munch ◽  
Ashim Paul ◽  
elad arad ◽  
Raz Jelinek ◽  
...  
Keyword(s):  
Ascorbic Acid ◽  
Acid Phosphatase ◽  
Hiv Infection ◽  
Prostatic Acid Phosphatase ◽  
Amyloid Formation ◽  
Human Semen ◽  
Dependent Effect ◽  
Amyloidogenic Peptides ◽  
Hiv 1

Human semen contains various amyloidogenic peptides derived from Prostatic Acid Phosphatase (PAP) and Semenogelin proteins that are capable of enhancing HIV-1 infection when assembled into fibrils. The best characterized among...

scholarly journals Seminal Plasma Accelerates Semen-derived Enhancer of Viral Infection (SEVI) Fibril Formation by the Prostatic Acid Phosphatase (PAP248–286) Peptide

2012 ◽  
Vol 287 (15) ◽  
pp. 11842-11849 ◽  
Author(s):  
Joanna S. Olsen ◽  
John T. M. DiMaio ◽  
Todd M. Doran ◽  
Caitlin Brown ◽  
Bradley L. Nilsson ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Viral Infection ◽  
Seminal Plasma ◽  
Amyloid Fibrils ◽  
Divalent Cations ◽  
Prostatic Acid Phosphatase ◽  
Fibril Formation ◽  
Amyloid Formation ◽  
Precursor Peptide

Amyloid fibrils contained in semen, known as SEVI, or semen-derived enhancer of viral infection, have been shown to increase the infectivity of HIV dramatically. However, previous work with these fibrils has suggested that extensive time and nonphysiologic levels of agitation are necessary to induce amyloid formation from the precursor peptide (a proteolytic cleavage product of prostatic acid phosphatase, PAP248–286). Here, we show that fibril formation by PAP248–286is accelerated dramatically in the presence of seminal plasma (SP) and that agitation is not required for fibrillization in this setting. Analysis of the effects of specific SP components on fibril formation by PAP248–286revealed that this effect is primarily due to the anionic buffer components of SP (notably inorganic phosphate and sodium bicarbonate). Divalent cations present in SP had little effect on the kinetics of fibril formation, but physiologic levels of Zn2+strongly protected SEVI fibrils from degradation by seminal proteases. Taken together, these data suggest that in thein vivoenvironment, PAP248–286is likely to form fibrils efficiently, thus providing an explanation for the presence of SEVI in human semen.

scholarly journals HIV-1 Enhancing Effect of Prostatic Acid Phosphatase Peptides Is Reduced in Human Seminal Plasma

PLoS ONE ◽  
2011 ◽  
Vol 6 (1) ◽  
pp. e16285 ◽  
Author(s):  
Julie A. Martellini ◽  
Amy L. Cole ◽  
Pavel Svoboda ◽  
Olga Stuchlik ◽  
Li-Mei Chen ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Seminal Plasma ◽  
Prostatic Acid Phosphatase ◽  
Human Seminal Plasma ◽  
Enhancing Effect ◽  
Hiv 1

scholarly journals Naturally Occurring Fragments from Two Distinct Regions of the Prostatic Acid Phosphatase Form Amyloidogenic Enhancers of HIV Infection

2011 ◽  
Vol 86 (2) ◽  
pp. 1244-1249 ◽  
Author(s):  
F. Arnold ◽  
J. Schnell ◽  
O. Zirafi ◽  
C. Sturzel ◽  
C. Meier ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Hiv Infection ◽  
Prostatic Acid Phosphatase ◽  
Naturally Occurring

The Demonstration of Human Prostatic Acid Phosphatase (Pap) With Phosphorylcholine

1976 ◽  
Vol 34 ◽  
pp. 88-89
Author(s):  
José A. Serrano ◽  
Hannah L. Wasserkrug ◽  
Anna A. Serrano ◽  
Arnold M. Seligman
Keyword(s):  
Acid Phosphatase ◽  
Prostate Gland ◽  
Prostatic Acid Phosphatase ◽  
Human Prostate ◽  
Rat Tissues ◽  
Specific Substrate ◽  
Acid Phosphatases ◽  
Lysosomal Acid ◽  
Cacodylate Buffer

As previously reported (1, 2) phosphorylcholine (PC) is a specific substrate for prostatatic acid phosphatase (PAP) as opposed to other acid phosphatases, e.g., lysosomal acid phosphatase. The specificity of PC for PAP is due to the pentavalent nitrogen in PC, a feature that renders PC resistant to hydrolysis by all other acid phosphatases. Detailed comparative cytochemical results in rat tissues are in press. This report deals with ultracytochemical results applying the method to normal and pathological human prostate gland.Fresh human prostate was obtained from 7 patients having transurethral resections or radical prostatectomies. The tissue was fixed in 3% glutaraldehyde- 0.1 M cacodylate buffer (pH 7.4) for 15 min, sectioned at 50 μm on a Sorvall TC-2 tissue sectioner, refixed for a total of 2 hr, and rinsed overnight in 0.1 M cacodylate buffer (pH 7.4)-7.5% sucrose.

Prostatic Acid Phosphatase (PAP) Differentiated Ultracytochemically from Lysosomal Acid Phosphate in the Rat with a PAP/Specific Substrate, Phosphorylcholine

1975 ◽  
Vol 33 ◽  
pp. 450-451
Author(s):  
W. Allen Shannon ◽  
José A. Serrano ◽  
Hannah L. Wasserkrug ◽  
Anna A. Serrano ◽  
Arnold M. Seligman
Keyword(s):  
Acid Phosphatase ◽  
Phosphate Buffer ◽  
Prostatic Carcinoma ◽  
Prostatic Acid Phosphatase ◽  
Chemotherapeutic Agents ◽  
Specific Substrate ◽  
Acid Phosphate ◽  
Lysosomal Acid ◽  
Design And Synthesis ◽  
New Chemotherapeutic Agents

During the design and synthesis of new chemotherapeutic agents for prostatic carcinoma based on phosphorylated agents which might be enzyme-activated to cytotoxicity, phosphorylcholine, [(CH3)3+NCH2CH2OPO3Ca]Cl-, has been indicated to be a very specific substrate for prostatic acid phosphatase (PAP). This phenomenon has led to the development of specific histochemical and ultracytochemical methods for PAP using modifications of the Gomori lead method for acid phosphatase. Comparative histochemical results in prostate and kidney of the rat have been published earlier with phosphorylcholine (PC) and β-glycerophosphate (βGP). We now report the ultracytochemical results.Minced tissues were fixed in 3% glutaraldehyde-0.1 M phosphate buffered (pH 7.4) for 1.5 hr and rinsed overnight in several changes of 0.05 M phosphate buffer (pH 7.0) containing 7.5% sucrose. Tissues were incubated 30 min to 2 hr in Gomori acid phosphatase medium (2) containing 0.1 M substrate, either PC or βGP.

Use of monoclonal and polyclonal antibodies to detect prostatic acid phosphatase by immunoblotting.

1986 ◽  
Vol 32 (10) ◽  
pp. 1832-1835 ◽  
Author(s):  
P C Patel ◽  
L Aubin ◽  
J Côte
Keyword(s):  
Monoclonal Antibodies ◽  
Acid Phosphatase ◽  
Western Blot ◽  
Polyclonal Antibodies ◽  
Prostatic Acid Phosphatase ◽  
The Other ◽  
Dot Blot ◽  
Western Blots ◽  
Dot Blot Assay ◽  
Polyclonal Antisera

Abstract We investigated two techniques of immunoblotting--the Western blot and the dot blot--for use in detecting prostatic acid phosphatase (PAP, EC 3.1.3.2). We used polyclonal antisera to human PAP, produced in rabbits by hyperimmunization with purified PAP, and PAP-specific monoclonal antibodies in the immunoenzymatic protocols. We conclude that PAP can be readily detected by Western blots with use of polyclonal antisera, but not with monoclonal antibodies. On the other hand, using a dot blot assay, we could easily detect PAP with both polyclonal and monoclonal antibodies.

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