Increased Activity of Renal Glutaminases in Guinea Pig Following Prolonged Administration of Acid or Alkali.

Goldstein, Léon; Baerle, R. Richterich-Van; Dearborn, Earl H.

doi:10.3181/00379727-93-22733

Cited by 17 publications

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“…If a single mechanism is involved, this finding destroys the concept that ammonia secretion is merely an obli gatory consequence of the acidification of urine with protons trapping the diffusible NH 3 which remains in equilibrium with the low steady state con centration of NHs in tubular cells. The possibility that an entirely separate device is operative in the alkalotic guinea pig has not been excluded but seems unlikely in view of this group ' s finding (46) that the glutaminase I (phosphate-activated) and glutaminase II (pyruvate-activated) activity of guinea pig kidney homogenates increase 100 and 40 per cent respectively in acidosis, and 250 and 70 per cent in alkalosis. These were paralleled by 60 and 90 per cent increases in glutamine synthetase activity in these two states, respectively.…”

Section: Kamin and Handlermentioning

confidence: 91%

Amino Acid and Protein Metabolism

Kamin¹,

Handler²

1957

Annu. Rev. Biochem.

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AMMONIAThe central metabolic position of ammonia has received renewed atten tion in recent years. To the list of known ammonia-producing reactions in mammals, summarized by Bessman (1), has been added the following: formylation of THF A2 from formiminoglutamate (2, 3) and, in microbial sources, L-alanine dehydrogenase (4); formylation from formimino glycine (S to 11); reductive deamination from glycine (12); and the degradation of glucosamine-6-phosphate (13). Since the fate of the nitrogen of numerous compounds is at present unknown, this list may be expected to expand an nually. Crystalline glutamic dehydrogenase isolated from corn leaves by Bulen (14) is DPN -specific, sensitive to sulfide reagents, and in general resembles the enzyme obtained from mammalian sources. Since the amino nitrogen of L-amino acids can be directed toward glutamate by transamina tion, it appears that glutamic dehydrogenase is the enzyme responsible for the major production of ammonia in hepatic metabolism in the steady state; it is not equally certain, however, that glutamic dehydrogenase universally occupies so central a role. Of various strains of B. subtilis which have been isolated, only those which possess glutamic dehydrogenase can use NH 3 as the sole nitrogen source (15). However, a mutant (5-) which can use am monia lacks glutamic dehydrogenase yet is capable of oxidizing glutamate (4). Fractionation of lysozyme-treated cells yielded a DPN-specific L-alanine 1 The survey of the literature pertaining to this review included journals received through Novemb er, 1956.2 The following abbreviations are used in this chapter: AICAR for 4-amino 5-imidazole carboxamide ribotide; ADP for adenosinediphosphate; AMP for adeno sinemonophosphate; ATP for adenosinetriphosphate; CoA for coenzyme Aj CSA for cysteine sulfinic acid; CTP for cytidinetriphosphate; DAP for diaminopimelic acid; DNA for deoxyribonuc leic acid; DNP for 2,4-dinitrophenol; DOPA for 3,4-dihydroxy phenylalanine; DPN for diphosphopyridine nucleotide; DPNH for diphosphopyridine nucleotide (reduced form); EDT A for ethylenediamine tetraacetic acid ; FAD for flavin adenine dinucleotide; FI G for formimino glycine; FGAR for formyl glycinamide ribotide; FMN for riboflavin phosphate; GAR for glycinamide ribotide; GDP for guanosinediphosphate; GMP for guanosinemonophosphate; GTP for guanosinetri phosphate; IDP for inosine diphosphate; IGP for imidazole glycerol phosphate; IMP for inosinemonophosphate; INH for isonicotinylhydrazide; ITP for inosinetriphos phate; PCMB for p-chloromercuribenzoate; Pi for inorganic phosphate; PBi for in organic pyrophosphate; PRPP for 5-phosphoribosylpyrophosphate; RNA for ribo nucleic acid; THF A for tetrahydrofolic acid; TPN for triphosphopyridine nucleotide; TPNH fortriphosphopyridine nucleotide (reduced form); Tris for trishydroxymethyl aminomethane; and UTP for uridinetriphosphate. 419Annu. Rev. Biochem. 1957.26:419-490. Downloaded from www.annualreviews.org Access provided by Texas Christian University on 02/03/15. For personal use only.Quick l...

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Section: Kamin and Handlermentioning

confidence: 91%

Amino Acid and Protein Metabolism

Kamin¹,

Handler²

1957

Annu. Rev. Biochem.

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“…This was confirmed in rats when Davies and Yudkin (11) and others (7,12) found that the administration of HCl increased and the administration of NaHCO3 decreased the activity of rat kidney glutaminase. The observation of similar changes in acidotic guinea pigs and rabbits (13) has suggested that ammonia excretion in all mammals, including man, is regulated in part by adaptive changes in the activity of renal glutaminase.…”

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confidence: 91%

The Effect of the Administration of Sodium Bicarbonate and Ammonium Chloride on the Excretion and Production of Ammonia. The Absence of Alterations in the Activity of Renal Ammonia-Producing Enzymes in the Dog

Rector¹,

Orloff²

1959

J. Clin. Invest.

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The regulation of the excretion of ammonia by the kidney has been studied extensively. It is clear that urine pH is an important determinant of ammonia excretion, with greater amounts of ammonia diffusing into acid urines than into alkaline urines (1-8). However, it is also evident that the magnitude of the rise in ammonia excretion during the chronic administration of strong acids or acidifying salts cannot be accounted for solely on the basis of "trapping" of greater amounts of ammonia in increasingly acid urines. Thus Pitts (4) found that dogs given NH4C1 for two days excreted more ammonia at any given urine pH than did control animals, presumably due to increased production of ammonia by the renal tubule cells. Earlier, Van Slyke and co-workers (9) had found that the extraction of glutamine from renal arterial blood was greater in dogs receiving NH4C1 than in those receiving NaHCO3, and further that the extracted glutamine amide-N accounted for approximately 60 per cent of the ammonia produced by the kidney. Lotspeich and Pitts (10) postulated that the capacity of some renal mechanism, capable of extracting and hydrolyzing glutamine, increases during chronic metabolic acidosis to produce more ammonia. This was confirmed in rats when Davies and Yudkin (11) and others (7,12) found that the administration of HCl increased and the administration of NaHCO3 decreased the activity of rat kidney glutaminase. The observation of similar changes in acidotic guinea pigs and rabbits (13) has suggested that ammonia excretion in all mammals, including man, is regulated in part by adaptive changes in the activity of renal glutaminase.There is evidence, however, that the regulation of ammonia excretion differs in dogs and rats.Orloff and Berliner (6) observed that the relationship between urine pH and ammonia excretion in dogs was reproducible following the infusion of sodium bicarbonate and independent of acute alterations in acid-base balance. This is in contrast to the findings of Leonard and Orloff (7) in the rat. In this species a correlation between ammonia excretion and urine pH was not observed under all circumstances. Alterations in ammonia excretion occurred independently of urine pH changes in some circumstances. The converse was also observed: changes in urine pH without associated changes in ammonia excretion. In the rat variations in ammonia excretion in acute studies are conditioned not only by urine pH, the only determinant in the dog, but also by the state of acid-base balance. Dogs and rats also exhibit dissimilar urinary responses to the chronic inhibition of carbonic anhydrase. In rats treated chronically with acetazoleamide, ammonia excretion falls briefly, then rises to greater than normal levels. This elevated excretion of ammonia is associated with an increased activity of renal glutaminase (7,14

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“…In the rat [23,24] and in the guinea pig [5] a relationship has been demonstrated between ammonia excreted in the urine during NH4C1 induced acidosis and glutaminase activity in kidney tissue. In the dog, by contrast, glutaminase activity does not increase during or after 7 days loading with NH4C1 while ammonia excretion becomes greater [18,23], Thus, it is premature to draw any general conclusions at present as to the adaptive role of glutaminase in ammonia production by the kindey [13].…”

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confidence: 99%

Glutaminases

Mattenheimer¹,

DeBruin²

1964

Enzymol Biol Clin

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An ultramicro method for the determination of glutaminase activity is described. Glutaminases I (phosphate activated) and II (pyruvate activated) and non activated glutaminase has been determined in fresh homogenate from 10 mg of tissue. The optimum conditions for glutaminase assay have been investigated in the kidney of man, dog and rat. In human kidney taken at autopsy no glutaminase I activity was found ; whereas in fresh human kidney biopsy specimens the glutaminase activity was of the same order of magnitude as in the dog and rat kidney. The variation over three orders of magnitude of glutaminase activity reported in the literature for each species was interpreted as the result of the instability of the enzymes, differences in assay conditions and dependence of glutaminase activity on the age of the animal.

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Increased Activity of Renal Glutaminases in Guinea Pig Following Prolonged Administration of Acid or Alkali.

Cited by 17 publications

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Amino Acid and Protein Metabolism

Amino Acid and Protein Metabolism

The Effect of the Administration of Sodium Bicarbonate and Ammonium Chloride on the Excretion and Production of Ammonia. The Absence of Alterations in the Activity of Renal Ammonia-Producing Enzymes in the Dog

Glutaminases

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