The Syntenic Relationship of the Genes for Human Lysosomal Acid Phosphatase, Isozyme C, and LDH-A

1974 ◽  
Vol 13 (1-2) ◽  
pp. 69-72 ◽  
Author(s):  
G. Bruns ◽  
P.S. Gerald
Keyword(s):  
Acid Phosphatase ◽  
Syntenic Relationship ◽  
Lysosomal Acid ◽  
Relationship Of

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.

High Degree of Homology Between Primary Structure of Human Lysosomal Acid Phosphatase and Human Prostatic Acid Phosphatase

1989 ◽  
Vol 370 (1) ◽  
pp. 177-182 ◽  
Author(s):  
Christoph PETERS ◽  
Carola GEIER ◽  
Regina POHLMANN ◽  
Abdul WAHEED ◽  
Kurt VON FIGURA ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Primary Structure ◽  
Prostatic Acid Phosphatase ◽  
Lysosomal Acid ◽  
High Degree

scholarly journals Sequential processing of lysosomal acid phosphatase by a cytoplasmic thiol proteinase and a lysosomal aspartyl proteinase.

1989 ◽  
Vol 8 (11) ◽  
pp. 3215-3219 ◽  
Author(s):  
S. Gottschalk ◽  
A. Waheed ◽  
B. Schmidt ◽  
P. Laidler ◽  
K. von Figura
Keyword(s):  
Acid Phosphatase ◽  
Lysosomal Acid ◽  
Sequential Processing ◽  
Thiol Proteinase

scholarly journals Purkinje Cell Compartmentation in the Cerebellum of the Lysosomal Acid Phosphatase 2 Mutant Mouse (Nax - Naked-Ataxia Mutant Mouse)

PLoS ONE ◽  
2014 ◽  
Vol 9 (4) ◽  
pp. e94327 ◽  
Author(s):  
Karen Bailey ◽  
Maryam Rahimi Balaei ◽  
Ashraf Mannan ◽  
Marc R. Del Bigio ◽  
Hassan Marzban
Keyword(s):  
Acid Phosphatase ◽  
Purkinje Cell ◽  
Mutant Mouse ◽  
Lysosomal Acid

scholarly journals Localization of lysosomal acid phosphatase mRNA in mouse tissues.

1992 ◽  
Vol 40 (9) ◽  
pp. 1275-1282 ◽  
Author(s):  
C Geier ◽  
J Kreysing ◽  
H Boettcher ◽  
R Pohlmann ◽  
K von Figura
Keyword(s):  
Acid Phosphatase ◽  
Mrna Level ◽  
Pyramidal Cells ◽  
Housekeeping Gene ◽  
Lysosomal Acid ◽  
Tissue Sections ◽  
Adult Mice ◽  
Mouse Tissues ◽  
Major Species

We studied the expression of lysosomal acid phosphatase (LAP) in mouse by hybridizing Northern blots and tissue sections with the mouse LAP cDNA. Three mRNA species of 2.3, 3.2 and 5.2 KB were identified, which differ in the length of their 3' untranslated region (UTR). The 3.2 KB mRNA is expressed in equal amounts in all tissues and represents the major species in most tissues, whereas the amounts of the 2.3 and 5.2 KB species differ. In situ hybridization of different tissues of adult mice showed a uniform expression of LAP, as expected for a housekeeping gene, except in testis and brain. In testis we found an increase in the LAP mRNA level in spermatocytes. By Northern blot analysis of young mouse testis, this increase could be attributed to late pachytene primary spermatocytes or secondary spermatocytes. In brain tissue the neurons were predominantly labeled, especially the Purkinje and pyramidal cells, whereas glial cells expressed only low amounts of LAP mRNA. Very high LAP expression was also found in the epithelial cells of the choroid plexus. Analysis of LAP expression during mouse embryonic development between Days 9.5 and 17.5 revealed a prominent expression relative to other tissues in the neural tube from Day 9.5 to Day 13.5.

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