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Biochemical Characterization of Individual Nephron Segments

W. G. Guder, Francois Morel

10.1002/cphy.cp080246

Source: Supplement 25: Handbook of Physiology, Renal Physiology

Originally published: 1992

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Biochemical Basis of Active Tubular Transport
2 Biochemical Mechanisms of Hormone Action
2.1 Cyclic AMP as Intracellular Messenger of Hormones
2.2 Inositol Polyphosphates, Diacylglycerol, and Ca2+ as Hormone Messengers
2.3 Insulin and Growth Factors
2.4 Action of Steroid Hormones Including Vitamin D Hormone
2.5 Thyroid Hormones
3 Biochemical Functions of the Proximal Tubule
3.1 Coupling of Metabolism and Transport
3.2 Brush‐Border Enzymes
3.3 Renal Gluconeogenesis
3.4 Amino Acid and Peptide Metabolism
3.5 Biotransformation Reactions
4 Thin Limbs of Henle's Loop
5 Thick Ascending Limb of Henle's Loop
5.1 Tamm‐Horsfall Glycoprotein
6 The Distal Convoluted Tubule
7 The Collecting Tubule
7.1 Metabolism and Transport ATPases
8 Organic Osmolytes
Figure 1. Figure 1.

Model of sodium, potassium ATPase, and biochemical reactions involved in sodium‐driven conformational changes of the α‐subunit. Scheme of α‐subunit of Na+,K+‐ATPase (left) and α‐subunit changes during sodium‐potassium transport (right). 3 Na bind to E1‐ATP to form phosphorylated (E1‐P) which, after release of 3 Na at outer surface (above), undergoes conformational change to the E1 form, binding 2 K and is dephosphorylated during one turn to the inner surface, where it rebinds ATP and releases 2 K. The inner pathway (dotted lines) represents the reactions in the absence of extracellular K.

Derived from refs. 414 and 415
Figure 2. Figure 2.

Comparison between relative densities and activities of mitochondrial and basolateral functions. Relative mitochondrial and basolateral membrane densities were measured morphometrically 354, and activities of mitochondrial enzyme acetoacetyl‐CoA transferase 53 and basolateral Na+,K+‐ATPase 238 were measured with ultramicro‐procedures. Maximal densities and activities set at 100%.

From ref. 160
Figure 3. Figure 3.

Distribution pattern of segment‐specific metabolic functions along the nephron. Enzyme activities and luminal membrane area (F) represent segment‐specific metabolic functions, not correlating with basic morphological or biochemical equipment: (A) glycolysis (hexokinase) 461; (B) gluconeogenesis (phosphoenolpyruvate carboxykinase) 58,164; (C) bicarbonate transport (anion‐stimulated ATPase) 35; (D) choline metabolism (choline kinase) 476; (E) betaine formation 476; (F) brush border structure 354; (G) brush border function (alkaline phosphatase) 388; (H) glycerol metabolism (glycerokinase) 57,483; (I) lysosomal function (N‐acetyl, β‐D‐glucosaminidase) 160; (K) kallikrein secretion (kininogenase) 158,342; (L) K‐stimulated ATPase.

Adapted from refs. 35,99,158, and 160
Figure 4. Figure 4.

Role of guanine nucleotide binding proteins in adenylate cyclase activation and inhibition by hormones. Model for regulation of adenylate cyclase activity by stimulatory and inhibitory hormones. H, hormone; R, receptor; CT, cholera toxin; PT, pertussis toxin; C, cyclase; s, stimulatory; i, inhibitory; *, active conformation. Dissociation of Gs results in stimulation of C by its αs‐subunit. Dissociation of Gi results in inhibition of catalytic activity as a result of reduction of αs* following its interaction with β and/or as a result of indirect or direct effects of αi* on C. The β‐subunit represents the β‐γ‐complex found more recently 39,446.

Adapted from ref. 139
Figure 5. Figure 5.

Mechanism of action of hormones acting via intracellular calcium. Hormones (agonists) binding to specific receptors (R1, R2) activate plasma membrane phospholipase C, modulated by guanine nucleotide binding protein (GBP). Phospholipase splits specifically phosphatidylinositol phosphate (PIP) and phosphatidylinositolbisphosphate (PIP2) to release inositol 1,4‐biphosphate (IP2) and inositol 1,4,5‐triphosphate (IP3), plus diglycerides (DG). Inositol‐P3 stimulates calcium release from endoplasmic reticulum, which activates phospholipase A2 to release arachidonate from 1,2sn‐phosphoglycerides, the precursors of eicosanoids (prostaglandin, prostacyclins, leucotrienes). Diglyceride, on the other hand, activates proteinkinase C, which phosphorylates specific proteins involved in the metabolic effects of hormone. Inositol phosphates can re‐enter the cycle by being phosphorylated through the phosphatidic acid (PA), CDP‐diglyceride (CDP‐DG) pathway. Lithium (Li) inhibits IP phosphatase. Phorbol ester directly activates protein kinase C. For sake of simplicity additional isoforms of IP3 and enzymes involved have been omitted.

Adapted from refs. 38 and 205
Figure 6. Figure 6.

Coupling of active sodium transport to fluid acidification in proximal cells. Na+ ions enter the cell across the luminal cell border in exchange against H+ ions. On the peritubular cell border, Na+ ions are extruded by the Na+, +‐ATPase activity and by an electrogenic Na+‐ cotransport system 487. As indicated by the numbers in parentheses, one ATPase cycle would allow the secretion of 4.5 H+ ions and the net absorption of 4.5 sodium and bicarbonate ions.

Adapted from ref. 12
Figure 7. Figure 7.

Carbohydrate and fatty acid metabolism in the proximal tubule. Lactate, glutamine, ketone bodies, and fatty acids can be degraded to CO2. Gluconeogenic precursors are resynthetized to glucose and form the glycerol backbone of tryglycerides in presence of fatty acids.
Figure 8. Figure 8.

Pathways of renal gluconeogenesis. Metabolic steps involved in glucose formation from various precursors entering the proximal tubular cell from the luminal or contraluminal side. Besides basic metabolic steps like the citric acid cycle in mitochondria and the glycolytic pathway in cell cytosol, the following typical enzymes are involved: (1) pyruvate carboxylase; (2) mitochondrial phosphoenolpyruvate carboxykinase (not present in rat and mouse kidney); (3) cytosolic phosphoenolpyruvate carboxykinase (little present in avian kidney); (4) fructose‐1,6‐bisphosphatase; (5) glucose‐6‐phosphatase; (6) glycerokinase; (7) fructokinase; (8) phosphate‐dependent glutaminase; (9) proline oxidase.

From ref. 480
Figure 9. Figure 9.

Pathways of proximal tubular amido acid metabolism, summarizing the major metabolic steps involved in tubular glycine, serine, proline, glutamine, 4‐hydroxypyrroline, aspartate, and alanine metabolism. The enzymes involved are as follows: (1) phosphate‐dependent glutaminase; (2) glutamine synthetase; (3) proline oxidase; (4) pyrroline‐5‐carboxylate dehydrogenase; (5) 4‐hydroxyproline oxidase; (6) 3‐hydroxypyrroline‐5‐carboxylate dehydrogenase; (7) glutamate dehydrogenase; (8) serine hydroxymethyltransferase; (9) glycine pyruvate transaminase; (10) alanine aminotransferase; (11) aspartate aminotransferase; (12) aspartate aminotransferase; (13) hydroxyoxoglutarate aldolase.
Figure 10. Figure 10.

Cytochrome P‐450 redox cycle. A methyl‐substrate in the cycle is hydroxylated with the aid of molecular oxygen and electrons derived from NADPH catalyzed by ferri‐cytochrome P‐450.
Figure 11. Figure 11.

Glutathione‐related reactions in proximal tubular cell. Schematic proximal tubular cell with the luminal brush border (left) and the basolateral sides (right). Constituent amino acids can be reabsorbed by specific carriers from lumen and from basolateral side (not shown). The following enzymatic steps are shown: (1) γ‐glutamylcysteine synthase; (2) glutathione synthase; (3) glutathione peroxidase; (4) glutathione reductase; (5) glutathione S‐transferase; (6) brush border and basolateral γ‐glutamyl‐transferase; (7) brush border cysteinyl glycine dipeptidase; (8) cysteinyl conjugate N‐acetyltransferase; (9) β‐lyase; (10) superoxide dismutase.
Figure 12. Figure 12.

Coupling of sodium transport to NaCl reabsorption in thick ascending limb. Peritubular Na+,K+‐ATPase activity maintains low Na+ concentration in the cell, which, via luminal 1 Na/1 K/2 Cl electroneutral cotransport mechanism, allows accumulation of K+ and Cl− ions in the cell above their respective electrochemical equilibrium. Peritubular membranes conductive to chloride and apical membranes conductive to potassium allow passive reabsorption of chloride and passive recycling of potassium. The whole transcellular process is electrogenic. The resulting lumen‐positive transepithelial PD drives net fluxes of Na+ and Cl− ions along the intercellular pathway, which is highly conductive to cations. Numbers in parentheses indicate respective ion fluxes per ATP cycle. According to this scheme, one ATP would correspond to the net absorption of 5 NaCl.

Adapted from ref. 145
Figure 13. Figure 13.

Dependency of oxidative metabolism from extracellular chloride in cortical thick ascending limb. Co2 production from [U‐14C]lactate by single fragments of medullary thick ascending limb was measured in vitro for 40 min as function of the chloride concentration in incubation solution. Each point corresponds to mean value of 12‐18 measurements. Inset shows Hill plot of data (R = .99, N = 2.12, apparent Km=41 mM).

Adapted from ref. 212
Figure 14. Figure 14.

Carbohydrate and fatty acid metabolism in thick ascending limb of Henle's loop cells.
Figure 15. Figure 15.

Functional segmentation of rabbit distal convoluted tubule. A, deep cortex nephron, including an arcade; B, middle cortex nephron; C, very superficial nephron including a “light” DCT portion. Terminal CAL portion; “bright” distal tubule (true distal tubule); “granulous” distal tubule (connecting tubule, CNT); “light” distal tubule (initial collecting tubule, ICT). CAL, cortical portion of the thick ascending limb; MD, macula densa; CCT, cortical collecting tubule.

Redrawn from ref. 315
Figure 16. Figure 16.

Energy metabolism of collecting tubule.


Figure 1.

Model of sodium, potassium ATPase, and biochemical reactions involved in sodium‐driven conformational changes of the α‐subunit. Scheme of α‐subunit of Na+,K+‐ATPase (left) and α‐subunit changes during sodium‐potassium transport (right). 3 Na bind to E1‐ATP to form phosphorylated (E1‐P) which, after release of 3 Na at outer surface (above), undergoes conformational change to the E1 form, binding 2 K and is dephosphorylated during one turn to the inner surface, where it rebinds ATP and releases 2 K. The inner pathway (dotted lines) represents the reactions in the absence of extracellular K.

Derived from refs. 414 and 415


Figure 2.

Comparison between relative densities and activities of mitochondrial and basolateral functions. Relative mitochondrial and basolateral membrane densities were measured morphometrically 354, and activities of mitochondrial enzyme acetoacetyl‐CoA transferase 53 and basolateral Na+,K+‐ATPase 238 were measured with ultramicro‐procedures. Maximal densities and activities set at 100%.

From ref. 160


Figure 3.

Distribution pattern of segment‐specific metabolic functions along the nephron. Enzyme activities and luminal membrane area (F) represent segment‐specific metabolic functions, not correlating with basic morphological or biochemical equipment: (A) glycolysis (hexokinase) 461; (B) gluconeogenesis (phosphoenolpyruvate carboxykinase) 58,164; (C) bicarbonate transport (anion‐stimulated ATPase) 35; (D) choline metabolism (choline kinase) 476; (E) betaine formation 476; (F) brush border structure 354; (G) brush border function (alkaline phosphatase) 388; (H) glycerol metabolism (glycerokinase) 57,483; (I) lysosomal function (N‐acetyl, β‐D‐glucosaminidase) 160; (K) kallikrein secretion (kininogenase) 158,342; (L) K‐stimulated ATPase.

Adapted from refs. 35,99,158, and 160


Figure 4.

Role of guanine nucleotide binding proteins in adenylate cyclase activation and inhibition by hormones. Model for regulation of adenylate cyclase activity by stimulatory and inhibitory hormones. H, hormone; R, receptor; CT, cholera toxin; PT, pertussis toxin; C, cyclase; s, stimulatory; i, inhibitory; *, active conformation. Dissociation of Gs results in stimulation of C by its αs‐subunit. Dissociation of Gi results in inhibition of catalytic activity as a result of reduction of αs* following its interaction with β and/or as a result of indirect or direct effects of αi* on C. The β‐subunit represents the β‐γ‐complex found more recently 39,446.

Adapted from ref. 139


Figure 5.

Mechanism of action of hormones acting via intracellular calcium. Hormones (agonists) binding to specific receptors (R1, R2) activate plasma membrane phospholipase C, modulated by guanine nucleotide binding protein (GBP). Phospholipase splits specifically phosphatidylinositol phosphate (PIP) and phosphatidylinositolbisphosphate (PIP2) to release inositol 1,4‐biphosphate (IP2) and inositol 1,4,5‐triphosphate (IP3), plus diglycerides (DG). Inositol‐P3 stimulates calcium release from endoplasmic reticulum, which activates phospholipase A2 to release arachidonate from 1,2sn‐phosphoglycerides, the precursors of eicosanoids (prostaglandin, prostacyclins, leucotrienes). Diglyceride, on the other hand, activates proteinkinase C, which phosphorylates specific proteins involved in the metabolic effects of hormone. Inositol phosphates can re‐enter the cycle by being phosphorylated through the phosphatidic acid (PA), CDP‐diglyceride (CDP‐DG) pathway. Lithium (Li) inhibits IP phosphatase. Phorbol ester directly activates protein kinase C. For sake of simplicity additional isoforms of IP3 and enzymes involved have been omitted.

Adapted from refs. 38 and 205


Figure 6.

Coupling of active sodium transport to fluid acidification in proximal cells. Na+ ions enter the cell across the luminal cell border in exchange against H+ ions. On the peritubular cell border, Na+ ions are extruded by the Na+, +‐ATPase activity and by an electrogenic Na+‐ cotransport system 487. As indicated by the numbers in parentheses, one ATPase cycle would allow the secretion of 4.5 H+ ions and the net absorption of 4.5 sodium and bicarbonate ions.

Adapted from ref. 12


Figure 7.

Carbohydrate and fatty acid metabolism in the proximal tubule. Lactate, glutamine, ketone bodies, and fatty acids can be degraded to CO2. Gluconeogenic precursors are resynthetized to glucose and form the glycerol backbone of tryglycerides in presence of fatty acids.



Figure 8.

Pathways of renal gluconeogenesis. Metabolic steps involved in glucose formation from various precursors entering the proximal tubular cell from the luminal or contraluminal side. Besides basic metabolic steps like the citric acid cycle in mitochondria and the glycolytic pathway in cell cytosol, the following typical enzymes are involved: (1) pyruvate carboxylase; (2) mitochondrial phosphoenolpyruvate carboxykinase (not present in rat and mouse kidney); (3) cytosolic phosphoenolpyruvate carboxykinase (little present in avian kidney); (4) fructose‐1,6‐bisphosphatase; (5) glucose‐6‐phosphatase; (6) glycerokinase; (7) fructokinase; (8) phosphate‐dependent glutaminase; (9) proline oxidase.

From ref. 480


Figure 9.

Pathways of proximal tubular amido acid metabolism, summarizing the major metabolic steps involved in tubular glycine, serine, proline, glutamine, 4‐hydroxypyrroline, aspartate, and alanine metabolism. The enzymes involved are as follows: (1) phosphate‐dependent glutaminase; (2) glutamine synthetase; (3) proline oxidase; (4) pyrroline‐5‐carboxylate dehydrogenase; (5) 4‐hydroxyproline oxidase; (6) 3‐hydroxypyrroline‐5‐carboxylate dehydrogenase; (7) glutamate dehydrogenase; (8) serine hydroxymethyltransferase; (9) glycine pyruvate transaminase; (10) alanine aminotransferase; (11) aspartate aminotransferase; (12) aspartate aminotransferase; (13) hydroxyoxoglutarate aldolase.



Figure 10.

Cytochrome P‐450 redox cycle. A methyl‐substrate in the cycle is hydroxylated with the aid of molecular oxygen and electrons derived from NADPH catalyzed by ferri‐cytochrome P‐450.



Figure 11.

Glutathione‐related reactions in proximal tubular cell. Schematic proximal tubular cell with the luminal brush border (left) and the basolateral sides (right). Constituent amino acids can be reabsorbed by specific carriers from lumen and from basolateral side (not shown). The following enzymatic steps are shown: (1) γ‐glutamylcysteine synthase; (2) glutathione synthase; (3) glutathione peroxidase; (4) glutathione reductase; (5) glutathione S‐transferase; (6) brush border and basolateral γ‐glutamyl‐transferase; (7) brush border cysteinyl glycine dipeptidase; (8) cysteinyl conjugate N‐acetyltransferase; (9) β‐lyase; (10) superoxide dismutase.



Figure 12.

Coupling of sodium transport to NaCl reabsorption in thick ascending limb. Peritubular Na+,K+‐ATPase activity maintains low Na+ concentration in the cell, which, via luminal 1 Na/1 K/2 Cl electroneutral cotransport mechanism, allows accumulation of K+ and Cl− ions in the cell above their respective electrochemical equilibrium. Peritubular membranes conductive to chloride and apical membranes conductive to potassium allow passive reabsorption of chloride and passive recycling of potassium. The whole transcellular process is electrogenic. The resulting lumen‐positive transepithelial PD drives net fluxes of Na+ and Cl− ions along the intercellular pathway, which is highly conductive to cations. Numbers in parentheses indicate respective ion fluxes per ATP cycle. According to this scheme, one ATP would correspond to the net absorption of 5 NaCl.

Adapted from ref. 145


Figure 13.

Dependency of oxidative metabolism from extracellular chloride in cortical thick ascending limb. Co2 production from [U‐14C]lactate by single fragments of medullary thick ascending limb was measured in vitro for 40 min as function of the chloride concentration in incubation solution. Each point corresponds to mean value of 12‐18 measurements. Inset shows Hill plot of data (R = .99, N = 2.12, apparent Km=41 mM).

Adapted from ref. 212


Figure 14.

Carbohydrate and fatty acid metabolism in thick ascending limb of Henle's loop cells.



Figure 15.

Functional segmentation of rabbit distal convoluted tubule. A, deep cortex nephron, including an arcade; B, middle cortex nephron; C, very superficial nephron including a “light” DCT portion. Terminal CAL portion; “bright” distal tubule (true distal tubule); “granulous” distal tubule (connecting tubule, CNT); “light” distal tubule (initial collecting tubule, ICT). CAL, cortical portion of the thick ascending limb; MD, macula densa; CCT, cortical collecting tubule.

Redrawn from ref. 315


Figure 16.

Energy metabolism of collecting tubule.

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Article Title: Biochemical Characterization of Individual Nephron Segments
 

How to Cite

W. G. Guder, Francois Morel. Biochemical Characterization of Individual Nephron Segments. Compr Physiol 2011, Supplement 25: Handbook of Physiology, Renal Physiology: 2119-2164. First published in print 1992. doi: 10.1002/cphy.cp080246