Plasma acid phosphatase

Sebum and Plasma Acid Phosphatase Activity in Hematologic and Hematopoietic Disease... 

Reports on the alteration of serum and/or plasma acid phosphatase activity in thrombocytopenia have not always been consistent. Zucker and Woodard (Z2) described a series of 12 patients with thrombocyte-... 

In a group of six children with acute thrombocytopenia and bone marrow megakaryocytic hyperplasia, the blood plasma, prepared as previously described, showed, in each case, an acid phosphatase activity, as determined by Gutman s method, that was higher than the mean value for that age (p = 0.02). The p value for the comparison of the group as a whole with normals was between 0.01 and 0.02. In all six of these patients the plasma acid phosphatase values returned to normal or near normal levels as the thrombocytopenia was corrected. Oski et al. (02) also studied 15 cases of chronic idiopathic thrombocytopenic purpura in whom the bone marrow showed normal to increased numbers of megakaryocytes. Of these, 13 showed plasma acid phosphatase values that were elevated above the normal mean for their age, albeit some of these differences were small. However, these elevations were statistically significant with a p value less than 0.01. 

In essence, then, these investigators felt that the plasma acid phosphatase activity, unobscured by in vitro destruction of platelets, could reflect the contribution of acid phosphatase from in vivo platelet destruction in various types of thrombocytopenias. To summarize, in thrombocyto-... 

However, Cooley and Cohen (C9) studied nine cases of idiopathic thrombocytopenic purpura in. which they failed to find any consistent correlation between the plasma acid phosphatase activities and platelet counts. Cohen et al. (C6) had shown that this condition could be classi-fifed into two major types, destructive and nondestructive, comprising 80% and 20%, respectively, of the total. In sequential studies of their various patients, Cooley and Cohen (C9) did not find any increased plasma acid phosphatase activity in those showing the destructive type, although in two cases of nondestructive (hypoplastic) thrombocytopenias, the plasma acid phosphatase activities were usually normal or low. Cooley and Cohen (C9) also found that in a group of eight patients with secondary (nondestructive) thrombocytopenias with nearly normal platelet life-spans (mostly 5-7 days) the plasma acid phosphatase levels tended to be low and to be correlated with the platelet count. 

C9. Cooley, M. H., and Cohen, P., Plasma acid phosphatase in idiopathic and secondary thrombocytopenias. Arch. Intern. Med. 119, 345-354 (1967). 

Fig. 3. Intracellular transport route of the SFV spike glycoproteins from the endoplasmic reticulum (ER), over the Golgi apparatus, to the plasma membrane (PM). The cis cisternae do not react positively for add phosphatase or thiamin pyrophosphatase, and do not label with ridn in thin frozen sections. The medial cisternae do not react positively for thiamin pyrophosphatase or acid phosphatase, but label with ridn. The trans cisternae are positive for all of these markers.

Similarly, Chow et al. observed an increase in the lysozyme activity of a soluble lung fraction and of plasma after continuous exposure of rats to ozone at 0.8 ppm for 8 days. However, no difference in lung or plasma lysozyme activity from control values was present in rats continuously exposed to 0.2 or 0.5 ppm or intermittently exposed (0.2-0.8 ppm, 8 h/day for 7 days). Histochemical evidence of an increase in lung acid phosphatase, a lysosomal enzyme, has also been reported. ... 

Enzymes activities are particularly sensitive to the anticoagulant used in collecting the specimen. Heparin inhibits acid phosphatase (W16) and muramidase (Z5). Amylase activity is inhibited by oxalate or citrate (MIO), and lactic dehydrogenase and acid phosphatase lose activity in oxalate (C2). Alkaline phosphatase is stable in oxalate, oxalate-fluoride, or heparin, but 25 mAf citrate inhibits 50% of the activity, and as little as 50 mlf EDTA is completely inhibitory (B19). Leucine aminopeptidase is inhibited by EDTA, as is creatine phosphokinase (F3). Amylase activity has been reported to be only 83% of that in serum when oxalate or citrate-plasma is used (MIO). Heparin plasma appears to have no inhibitory effect. Despite the fact that clotting factor V is not stable in oxalate or EDTA, these are often used as anticoagulants to obtain plasma for prothrombin determinations (Z2, Z4). 

Brydon and Roberts- added hemolyzed blood to unhemolyzed plasma, analyzed the specimens for a variety of constituents and then compared the values with those in the unhemolyzed plasma (B28). The following procedures were considered unaffected by hemolysis (up to 1 g/100 ml hemoglobin) urea (diacetyl monoxime) carbon dioxide content (phe-nolphthalein complex) iron binding capacity cholesterol (ferric chloride) creatinine (alkaline picrate) uric acid (phosphotungstate reduction) alkaline phosphatase (4-nitrophenyl phosphate) 5 -nucleotidase (adenosine monophosphate-nickel) and tartrate-labile acid phosphatase (phenyl phosphate). In Table 2 are shown those assays where increases were observed. The hemolysis used in these studies was equivalent to that produced by the breakdown of about 15 X 10 erythrocytes. In the bromocresol green albumin method it has been reported that for every 100 mg of hemoglobin/100 ml serum, the apparent albumin concentration is increased by 100 mg/100 ml (D12). Hemolysis releases some amino acids, such as histidine, into the plasma (Alb). 

Lysis of formed blood elements other than erythrocytes may produce elevations in serum or plasma constituents. Platelet breakdown during blood collection can introduce enzymes into the plasma (Z3). Aldolase activity is very high in platelets (Dl), and elevations of acid phosphatase in myeloproliferative disease are probably the result of platelet lysis (B6). 

The involvement of testosterone in the testicular atrophy caused by di(2-ethyl-hexyl) phthalate was examined by co-administration of testosterone (1 mg/kg bw) subcutaneously with 2000 mg/kg bw di(2-ethylhexyl) phthalate [purity not specified] in groundnut oil to adult male Wistar rats for 15 days (Parmar et al., 1987). Administration of di(2-ethylhexyl) phthalate reduced the sperm count and also significantly increased the activity of y-GT, lactate dehydrogenase and P-glucuronidase and decreased the activity of sorbitol dehydrogenase and acid phosphatase. Co-adminis-tration of testosterone seemed to normalize the sperm count and the activity of testicular enz5mies. The role of testosterone in the testicular toxicity of di(2-ethylhexyl) phthalate has not been fully elucidated. Several reports refer to increased or decreased testosterone levels in plasma and testicular tissue. 

In 1924, Martland et al. (1) reported on phosphatase activity in red blood cells. Roche later differentiated between the phosphatase of the red cells with pH optimum 6.0-6.2 and the phosphatase from white cells with optimum 8.8-9.0. Roche also showed that a-glycerophosphate was split more rapidly than -glycerophosphate by red cell extracts while the reverse was true of acid phosphatase activity in plasma (2). While studying the source of acid phosphatase activity in male urine, Kutscher and Wolberg discovered the very high activity of acid phosphatase in human prostate (3). This tissue was shown by Woodard to have one-thousand times the activity of extracts from bone, liver, and kidney (3a). Igarashi and Hollander crystallized the acid phosphatase of rat liver and showed that under certain conditions allosteric control of the activity could be demonstrated (4). 

Effect of Metallic Ions on the Acid Phosphatases of Plasma, Prostate, and Red Cells0 1... 

Registration of adverse effects with Lorenzo s oil has been hampered by the absence of controlled trials. In 22 patients treated for at least 12 months, although Lorenzo s oil did not seem to be beneficial, there were possible adverse effects, such as mild increases in liver enzymes (55%), thrombocytopenia (55%), gastrointestinal complaints (14%), and gingivitis (14%). Furthermore, there were falls in hemoglobin concentration and leukocyte count, and an increase in the plasma alkaline phosphatase concentration the reduction in platelet count did not result in hemorrhage (1). Whether some of the adverse effects of Lorenzo s oil are due to low concentrations of essential fatty acids or caused by reduced dietary fat intake is not known. 

The active sites of these enzymes can have a nitrogen ligand, usually as histidine (acid phosphatases and some protein phosphatases), a nucleophilic serine residue (alkaline phosphatases), a cysteine residue in which the thiol group can form a covalent species with the phosphate ester (protein phosphatases), or an aspartate-linked phosphate (plasma membrane ion pumps). The inhibitory form of vanadium is usually anionic vanadate V(V), but cationic vanadyl V(IV) has also shown strong inhibition of some types of phosphorylase reactions. Above neutral pH, speciation of vanadyl ions produces anionic V(IV) species capable of inhibition of enzymes in the traditional transition-state analogue manner [5],... 

Because the intermediary metabolism of various organs is virtually the same, organ-specific enzymes are very rare. One example usually cited is the acid phosphatase of the prostate. However, the enzyme complement of the various organs may differ with respect to relative activities of the enzymes, the time dependence of their appearance in plasma, and the pattern of their isoenzymes (see below). Table 5.2 presents a list of enzymes commonly used for organ- and disease-specific diagnoses. 

CoA undergoes dephosphorylation, catalyzed by lysosomal acid phosphatase, to dephospho-CoA, followed by pyrophosphatase action to release 4 -phosphopantetheine and 5 -AMP - the reverse of the final stages of CoA synthesis shown in Figure 12.2. CoA is also a substrate for direct pyrophosphatase action, at about 10% of the rate of action on dephospho-CoA. The pyrophosphatase seems to be a general nucleotide pyrophosphatase of plasma membrane rather than an enzyme specific for the degradation of CoA. 

In man and in other mammalian species, the major mass of the prostate, usually consisting of the right and left lateral and the middle lobes, is composed of alveoli lined with columnar epithelium embedded in a thick fibromuscular stroma. These alveoli constantly secrete a fluid which is drained off by a system of branching ducts that empty into the floor and lateral surfaces of the posterior urethra. The normal secretion is dependent upon the degree of androgenic stimulation and amounts to about 0.5-2 ml per day. The prostatic secretion, which is characterized by very high acid phosphatase activity, is a milky fluid which contains citric acid, choline, cephalin, cholesterol, proteins, and electrolytes similar to those found in the plasma. 

As long ago as 1935, Kutscher and Wolbergs (K12) observed that semen and the prostate are among the richest sources of acid phosphatase in the human body. In a more recent survey (Bll) the acid phosphatase activities of seminal plasma in various species, determined as milligrams of nitrophenol liberated by 100 ml seminal plasma from 0.006 M p-nitrophenyl phosphate, in 60 minutes at 37°C and pH 4.9 were human, 274,000 cock, 15,000 turkey, 4000 bull, 570 rabbit 85. Human seminal plasma is made up by the secretory fluids produced in the epididymides, vasa deferentia, ampullae, seminal vesicles, the prostate and the bulbourethral (Cowper s) and urethral (Littre s) glands (M4). The semen contains many particulate bodies. Best known, of course, are the spermatozoa, which are formed in the seminiferous... 

Another procedure to increase the specificity of acid phosphatase determinations for prostatic disease has involved the use of n- (-I-) -tartrate to distinguish between the enzyme from the prostate and other tissues. In a series of papers from 1947 to 1949, Abul-Fadl and King (Al, A2, A3, A4) studied the properties of various acid phosphatases and reported that 0.01 Af L- (4-) -tartrate inhibited the hydrolysis of phenyl phosphate by human prostatic acid phosphatase dissolved in normal saline or in plasma to the extent of 95%, but had no effect on the hydrolysis by acid phosphatase from erythrocytes. The inhibitions of acid phosphatases from other human tissues were as follows liver, 70% kidney, 80% spleen, 70%. 

The remaining half of the sample collected in the silicone-treated glassware was transferred to ordinary glass and allowed to clot at room temperature for 30 minutes, as is usually done to obtain serum for acid phosphatase determinations. The mean values and their standard deviations for serums from platelet-poor plasma from various groups of subjects were as follows in Bodansky units 28 normal women, 0.094 0.009 23 normal men, 0.109 0.021. The corresponding values for ordinary serum acid phosphatase were 0.226 0.13 and 0.278 0.27. It appeared, therefore, that approximately 60% of the acid phosphatase in serum arises from the liberation of this enzyme from platelets as a result of clotting. 

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