Esterases of Testis and Other Tissues

Abstract

This paper is concerned with some physiologic relationships of non-specific esterases of tissues of the rat, dog, and man which were investigated by a colorimetric technique. Two patterns of hydrolysis were revealed that were characteristic of several tissues. I t was found also that the esterase of rat testis is produced in the interstitial cells, that its content is under control of the hypophysis, and that its concentration is related to the production of androgen by the testis.The colorimetric method employed chromogenic substrates, colorless compounds that liberate color on hydrolysis. The color value is read directly, the depth of color produced by enzymatic hydrolysis being directly related to activity of the enzyme. The chromogenic substrate techniques of enzymatic investigation combine accuracy, delicacy, and simplicity. All the chromogenic substrates, beginning with the first use of this technique by Ohmori (1), have been compounds of phenolic acid-base indicators esterified with phosphoric (1, 2), glucuronic (3), sulfuric (4), or fatty acids (5). In the present studies the substrates were the aeyl esters of p-nitrophenol previously synthesized in this laboratory.Three principal esterase activities in animal tissues can be differentiated according to their distribution, their efficiency against various substrates, and the effect of inhibitors (5, 24) upon them. An enzyme cannot be characterized with certainty until it has been isolated in a pure state and this has not been achieved with any of the esterases. However, from indirect evidence esterolysis seems to be brought about by three separate types of enzymes; in this paper the effects will be designated according to conventional usage as cholinesterase, non-specific esterase, and lipase. No doubt there is some overlapping of their activities and, as will be brought out, the chief differentiating characteristics are quantitative rather than qualitative.The choline esters are sufficiently soluble in water to serve as satisfactory substrates in vitro. Cholinesterase has an entirely different distribution than the other esterases.Maruay and Nachmansohn (6) found that the cerebral cortex and uterus of guinea pig hydrolyzed acetylcholine more effectively than extracts of kidney or liver did. In swine (7) aeetylcholine is hydrolyzed more rapidly by certain structures which, in descending order of magnitude, are the parotid, lachrymal and sublingual glands, Fallopian tube, jejunal and gastric mucosa, and the medulla oblongata. Mendel,

Autoradiographic study on the distribution of Bis-p-nitrophenylphosphate (BNPP), a specific inhibitor of carboxylesterases, in the rat

“…The second "phase" of the distribution pattern correlates well with histochemical and biochemical data about the occurance of esterases in the organs of the rat (8,10,11,12,20) and of other species (e.g. 16,22).…”

“…16,22). liver, kidneys, intestinal mucosa (17), testis (8,19) and within the kidney, as well, seems to correspond to histochemical results as to preferential representation of the cortex. The specificity of the binding characteristics of BNPP is further underlined by the fact that fetal liver in contrast to that of the adult is found unlabelled in spite of free diaplacental passage of the inhibitor.…”

“…The specificity of the binding characteristics of BNPP is further underlined by the fact that fetal liver in contrast to that of the adult is found unlabelled in spite of free diaplacental passage of the inhibitor. As we know from literature (8,11,20,23,41,42) liver carboxylesterase activity quantitatively does not develop before a few days after birth. In accordance with histochemical staining we also find autoradiographic representation of the mucosal epithelia of small intestine (Figure 3), of the epithelia of canaliculi epididymis (Figure 2b), of the tubuli contorti testis (Figure 2a) and of the seminal vesicle (Figure 2c).…”

The Proteins in Fluids From the Seminiferous Tubules and Rete Testis of the Rat

“…On the basis of the results of chemical and histochemical studies, testicular tissue is known to be rich in non-specific esterase activity (Huggins & Moulton, 1948) which is mainly distributed in the interstitial cells (Nachlas & Seligman, 1949). Esterase activity is also found in the seminiferous tubules and is located in the Sertoli cells (Niemi & Kormano, 1965a).…”

Intracellularly Degradable, Self‐Assembled Amphiphilic Block Copolycurcumin Nanoparticles for Efficient In Vivo Cancer Chemotherapy

“…Moreover, the hydrophobic core made of PCDA should lead to high drug loading and providing effective protection for Cur against hydrolysis. The Biotin-PEG-PCDA NP should be stable during the blood transport but can readily release its API (Cur) once enters the target cancer cells/tissues triggered by the high intracellular glutathione (GSH, 1-10 mM v.s.~10 M in blood) [11] and esterase [12] contents.The over-expressed biotin receptors found on cancer cells can be exploited for effective, active cancer targeting. [13] Importantly, the Biotin-PEG-PCDA NP can be loaded with a 4 second anticancer drug (e.g.…”