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PubMed1984

Tissue culture of human kidney epithelial cells of proximal tubule origin.

The in vitro culture of human kidney epithelial cells of defined nephronal origin would prove valuable in a variety of studies defining the factors and mechanisms responsible for diseases and disorders of the kidney. In this study we have tested the hypothesis that employing a serum-free growth medium allows the selective cultivation of human kidney epithelial cells. It is demonstrated that human kidney cortex, explanted into serum-free hormonally defined growth medium gives rise to a primary culture of kidney epithelial cells of homogeneous morphology capable of hemicyst formation. While these cells were able to proliferate to confluency as an explant culture, they were unable to undergo stable subculture. Subsequent manipulation of the culture vessel surface (an initial coat of bovine type I collagen followed by the absorption of macromolecules from fetal calf serum) yielded cultures able to be subcultured with growth to at least 30 cell generations. These cells were identified to be of proximal tubule origin by employment of enzyme histochemistry, immunohistochemistry, and ultrastructural examination.

Cells, Cultured↗
PubMed2003

Analysis of angiotensin II mediated COX-2 downregulation in angiotensin II- or aldosterone-infused hypertensive rat.

The renin-angiotensin cascade plays an important role in blood pressure control and sodium homeostasis. This study investigated whether cyclooxygenase-2 expression is regulated in the kidney, in an angiotensin II- and aldosterone-induced hypertension model. For this purpose, we treated male Sprague-Dawley rats (n=8 per group) with angiotensin II (9 mg/h, subcutaneously) for 14 d and aldosterone (0.75 mg/h, subcutaneously) for 42 d. Systolic blood pressure was significantly increased by angiotensin II (p<0.001) and by aldosterone (p<0.001). We found that angiotensin II downregulated cyclooxygenase-2 protein in the kidney cortex, whereas aldosterone showed no effect. These results indicate that angiotensin II may act directly to inhibit kidney cortex cyclooxygenase-2 protein expression, rather than acting via stimulation of aldosterone.

Aldosterone↗
PubMed2006

Effect of estrogen on neprilysin expression in uterus and kidney of Sprague-Dawley normotensive and heterozygous (mRen2)27-transgenic hypertensive rats.

The present study was designed to determine whether estrogen modulates the angiotensin processing enzymes in membrane homogenates obtained from uterus and kidney cortex and medulla of Sprague-Dawley (SD) and heterozygous (mRen2)27-transgenic hypertensive (Tg(+)) female rats treated with or without 17beta-estradiol (E2). We evaluated estrogen's influence on neprilysin (NEP), an endopeptidase that forms angiotensin-(1-7) [Ang-(1-7)] and on aminopeptidase (AMP), which degrades Ang-(1-7). Renal tissue from normotensive and hypertensive male rats was also evaluated. E2 up-regulated NEP mRNA in the uterus of both SD and Tg(+) and this was associated with increased NEP activity in the uterus of SD (0.31+/-0.03 nmol/min/mg versus 0.18+/-0.04 nmol/min/mg of protein, p<0.05) and Tg(+) (0.26+/-0.04 nmol/min/mg versus 0.13+/-0.02 nmol/min/mg of protein, p<0.05) female). E2 had no significant effect on NEP activity in cortex and medulla of hypertensive and normotensive female. In female animals, cortical NEP activity is two-fold higher than medullary; in males there is a four-fold higher cortical NEP activity as compared to medulla. In male animals, medullary NEP was significantly lower than females with or without E2 treatment; no gender specific effect was found in cortex. E2 treatment also caused a two-fold increase in AMP activity in the uterus and 1.6-fold decrease in kidney cortex of SD and Tg(+) female (p<0.05). Our studies indicate that NEP may be a primary candidate for increased Ang-(1-7) processing in the uterus with estrogen treatment; kidney NEP, on the other hand, showed no modulation by estrogen, suggesting that down regulation of other processing enzymes, like AMP and ACE, may come into play in the kidney with estrogen replacement. In addition, these studies showed that there is tissue-specific regulation of NEP with estrogen treatment that is strain independent.

Aminopeptidases↗
PubMed1970

Effects of ischaemia on content of metabolites in rat liver and kidney in vivo.

1. The time-course of changes in content of intermediates of glycolysis in rat liver and kidney cortex after severance of blood supply was investigated. 2. The decline in content of ATP was more rapid in kidney (1.7-0.5mumol/g in 30s) than in liver (2.7-1.6mumol/g in 60s). In both tissues AMP and P(i) accumulated. 3. Net formation of lactate was 1.7mumol/g during the second minute of ischaemia in liver from well-fed rats, 1.1mumol/g in liver from 48h-starved rats, and about 1.0mumol/g during the first 30s of ischaemia in kidney. Net formation of alpha-glycerophosphate was rapid, especially in liver. 4. In kidney the concentration of beta-hydroxybutyrate rose, but that of alpha-oxoglutarate and acetoacetate decreased. 5. In both organs the concentrations of fructose diphosphate and triose phosphates increased during ischaemia and those of other phosphorylated C(3) intermediates decreased. 6. The concentration of the hexose 6-phosphates rose rapidly during the first minute of ischaemia in liver, but decreased during renal ischaemia. 7. In kidney the content of glutamine fell after 2min of ischaemia, and that of ammonia and glutamate rose. 8. The redox states of the cytoplasmic and mitochondrial NAD couple in kidney cortex were similar to those in liver. 9. The regulatory role of glycogen phosphorylase, pyruvate kinase and phosphofructokinase is discussed in relation to the observed changes in the concentrations of the glycolytic intermediates.

Acetoacetates↗
PubMed2005

Loss of nitric oxide and endothelial-derived hyperpolarizing factor-mediated responses in aging.

BACKGROUND: Aging has considerable structural and functional effects on the vascular system of the kidney. One such effect is an alteration in vascular tone which potentially will initiate renal damage. Vascular tone is determined by the balance between vasoconstrictors and vasodilators. Therefore, we hypothesized that aging attenuates vasodilatory responses in the kidney. These changes may be mediated by a loss of nitric oxide and endothelial-derived hyperpolarizing factor (EDHF). METHODS: The systemic and renal responses of nitric oxide and EDHF were investigated in aging (18 months old) and young (3 months old) Sprague-Dawley rats. RESULTS: We demonstrated a general loss of vasodilatory responses in the aging kidney. In addition, nitric oxide levels were reduced in the serum and kidney cortex of aging versus young animals, although this was not accompanied with a loss of endothelial nitric oxide synthase (eNOS) protein in the kidney cortex. Aging animals also exhibited a loss in EDHF-mediated vasodilation following stimulation with either acetylcholine or bradykinin in the isolated perfused kidney. CONCLUSION: These findings indicate that not only a defect in the nitric oxide pathway, but also a loss of EDHF-mediated responses may be responsible for impaired vasodilation in the aging kidney. This may result in enhanced vasoconstrictive responses in aging which potentially will cause renal damage and ultimately a loss in glomerular filtration rate (GFR).

Acetylcholine↗
PubMed2004

Rat mesangial alpha-endosulfine.

BACKGROUND: Sulfonylurea agents exert their physiologic effects via binding to specific sulfonylurea receptors (SUR) in adenosine triphosphate-sensitive potassium (K(ATP)) channels. Mesangial cells express K(ATP) and respond to sulfonylureas by altering glucose metabolism, elevating intracellular calcium and contracting. A putative endogenous sulfonylurea, alpha-endosulfine, has been demonstrated in diverse tissues and is a member of the cyclic adenosine monophosphate (cAMP)-regulated family of phosphoproteins. This study investigates mesangial cell expression of ENSA, the gene encoding alpha-endosulfine, and its regulation by glucose. METHODS: Expression of rat glomerular and mesangial ENSA was examined by reverse transcription-polymerase chain reaction (RT-PCR) and Northern analysis. In situ hybridization studies were carried out to investigate the presence and distribution of ENSA in kidney cortex. Expression of mesangial cell alpha-endosulfine was studied by immunoblotting, immunofluorescence, and confocal microscopy. RESULTS: RT-PCR with gene-specific primers and Northern blotting disclosed abundant expression of two major ENSA transcripts at 2.4 kb and 1.2 kb in whole rat kidney, kidney cortex, and mesangial cells. In situ hybridization of rat kidney demonstrated renal ENSA expression, particularly within glomeruli. Confocal microscopy revealed a diffusely granular, cytosolic distribution of alpha-endosulfine. High glucose concentrations increased ENSA expression by 24 hours, an effect that persisted for at least 10 days. Protein expression paralleled gene expression. CONCLUSION: ENSA and alpha-endosulfine are expressed in rat glomeruli and mesangial cell and gene and protein expression are up-regulated by a high glucose environment. alpha-Endosulfine has potential roles as a regulator of metabolism and contractility via mesangial cell K(ATP).

Amino Acid Sequence↗
PubMed1993

Localization of NaPi-1, a Na/Pi cotransporter, in rabbit kidney proximal tubules. II. Localization by immunohistochemistry.

Polyclonal antibodies have been raised against a C-terminal peptide of NaPi-1, a recently cloned Na-Pi cotransport system of rabbit kidney cortex with a predicted (unglycosylated) molecular mass of 52 kDa. By Western blot analysis using brush-border membranes isolated from rabbit kidney cortex, two proteins with apparent molecular masses of 64 kDa and 35 kDa were specifically recognized (peptide protectable) by the antiserum obtained. The 64-kDa protein was found to migrate in parallel with the luminal membrane during separation by free-flow electrophoresis of brush-border and basolateral membranes. In immunofluorescence studies using cryostat sections of rabbit kidney, specific binding of antibodies was observed in proximal tubules (including S1, S2 and S3 segments) of superficial and deep nephrons. Anti-(NaPi-1)-antibody-mediated fluorescence was restricted to the brush border of proximal tubular cells. No specific immunoreaction was observed in other tubular segments. The results suggest that the native NaPi-1-related protein (Na-Pi cotransport system) has an apparent molecular mass of 64 kDa and is uniformly expressed in the apical membrane of proximal tubules of all nephron generations in the rabbit kidney. Immunohistochemical localization of the Na-Pi cotransport system NaPi-1 confirms the segmental localization within the nephron of NaPi-1-related mRNA as revealed by the reverse transcriptase/polymerase chain reaction (see preceding paper).

Amino Acid Sequence↗
PubMed1975

Catabolism of an isolated, purified intermediate of prostaglandin biosynthesis by regions of the adult rat kidney.

1. A heat labile, cold-stable, stannous chloride-reducible intermediate of prostaglandin biosynthesis was formed in good yield (greater than 60%) from 3H-labeled arachidonic acid during brief incubations (30--90 s, 37 degrees C) with sheep seminal vesicle microsomes in the presence of p-hydroxymercuribenzoate (4 mM). This intermediate appears to have properties similar to one of the endoperoxides (15-hydroxyprostaglandin-9,11-endoperoxide) recently isolated by Hamberg and Samuelsson (Proc. Natl. Acad. Sci. U.S. (1973) 70, 889-903) AND Nugteren and Hazelhof (Biochem. Biophys. Acta. (1973) 326, 448-461). 2. Treatment of the purified intermediate with homogenates of rat kidney cortex, medulla and papilla resulted within 2 min (37 degrees C) in complete conversion into several compounds including prostaglandins E2 and F2alpha. The main product (40-50% yield formed by papilla homogenates was prostaglandin E2. The conversion into prostaglandin E2 was largely abolished by previous bo9ling of the homogenate whereas the conversion into prostaglandin F2alpha was not. The intermediate was stable in buffer for the same period of incubation. 3. The ratio of tritiated prostaglandins E2: F2alpha obtained were: papilla, 1.90; medulla, 0.76; cortex, 0.48. 4. These observations indicate that both types of prostaglandins can be formed by all three regions of the rat kidney and that regional differences exist in the proportion of E2 : F2alpha that is formed. Whereas prostaglandin E2 is mostly formed by an enzymatic process, prostaglandin F2alpha is not.

Animals↗
PubMed2000

Structural and functional characteristics and tissue distribution pattern of rat OCTN1, an organic cation transporter, cloned from placenta.

This report describes the structure, function, and tissue distribution pattern of rat OCTN1 (novel organic cation transporter 1). The rat OCTN1 cDNA was isolated from a rat placental cDNA library. The cDNA is 2258 bp long and codes for a protein of 553 amino acids. Its amino acid sequence bears high homology to human OCTN1 (85% identity) and rat OCTN2 (74% identity). When expressed heterologously in mammalian cells, rat OCTN1 mediates Na(+)-independent and pH-dependent transport of the prototypical organic cation tetraethylammonium. The transporter interacts with a variety of structurally diverse organic cations such as desipramine, dimethylamiloride, cimetidine, procainamide, and verapamil. Carnitine, a zwitterion, interacts with rat OCTN1 with a very low affinity. However, the transport of carnitine via rat OCTN1 is not evident in the presence or absence of Na(+). We conclude that rat OCTN1 is a multispecific organic cation transporter. OCTN1-specific mRNA transcripts are present in a wide variety of tissues in the rat, principally in the liver, intestine, kidney, brain, heart and placenta. In situ hybridization shows the distribution pattern of the transcripts in the brain (cerebellum, hippocampus and cortex), kidney (cortex and medulla with relatively more abundance in the cortical-medullary junction), heart (myocardium and valves) and placenta (labyrinthine zone).

Amino Acid Sequence↗
PubMed1999

Existence of acyl-CoA hydrolase-mediated pathway supplying arachidonic acid for prostaglandin synthesis in microsomes from rabbit kidney medulla.

We have previously shown that acyl-coenzyme A (CoA) hydrolase that hydrolyzes arachidonoyl-CoA (AA-CoA) to arachidonic acid (AA) and CoA is present in the cytosol of rabbit kidney medulla and that this enzyme can supply AA for prostaglandin (PG) synthesis in this region. In the present study, the existence of the acyl-CoA hydrolase-mediated pathway that supplies AA available for PG synthesis in microsomes from the kidney medulla was examined. AA-CoA (20 microM) was preincubated with the 105,000 g pellet (microsomes, 0.5 mg of protein) from the medulla for 5 min at 37 degrees C followed by incubation with the medulla microsomes (0.5 mg of protein) (the source of PG synthesizing enzymes) in the presence of hydroquinone and reduced glutathione for 5 min at 37 degrees C. The PGs formed were measured by high-pressure liquid chromatography using 9-anthryldiazomethane for derivatization. The addition of the microsomal fraction from the medulla in the preincubation mixture increased total PG formation from 3.86 to 8.70 nmol, and this stimulatory effect was somewhat weaker than that of the cytosolic fraction. On the other hand, the microsomal fraction in the kidney cortex has an extremely lower capacity to supply AA for PG synthesis than do medulla microsomes. These results suggest that, in kidney medulla, the microsomes as well as the cytosol have the potential route that supplies AA from AA-CoA for PG synthesis and that this pathway is mediated by acyl-CoA hydrolase.

Acyl Coenzyme A↗
PubMed1991

[The effect of aldosterone on the second messenger systems in the rat kidney].

The effect of aldosterone on the cAMP level, the state of inositol-phosphate pool and the intracellular free Ca2+ activity in the rat kidney, were studied. The cAMP level in the kidney cortex homogenate was not changed after i.p. injection of aldosterone. Reliable changes in the content of inositol-phosphates in the kidney cell suspension was not revealed after aldosterone treatment. A short-term enhancement of the intracellular Ca2+ activity in the isolated distal convoluted and cortical collecting tubules under the influence of aldosterone, was revealed. The participation of the second messenger systems in the realisation of aldosterone effects in kidney and the role of Ca2+ in the mechanism of aldosterone action, are discussed.

Aldosterone↗
PubMed2006

Public health evaluation of cadmium concentrations in liver and kidney of moose (Alces alces) from four areas of Alaska.

Liver and/or kidney samples were collected from 139 hunter-killed moose from four areas of Alaska during 1986. The concentration of cadmium in organ tissue was determined by direct-current plasma atomic emission spectrometry. All results are reported as mug/g wet weight. Concentrations of cadmium in liver ranged from 0.06 microg/g to 9.0 microg/g; in the kidney cortex they ranged from 0.10 microg/g to 65.7 microg/g. Cadmium levels were significantly associated with location and age. The highest geometric mean liver (2.11 microg/g) and kidney cortex (20.2 microg/g) cadmium concentrations were detected in moose harvested near Galena, Alaska. Limited dietary information from Alaska and Canada indicates that the intake of moose liver or kidney does not exceed, in most individuals, the World Health Organization recommendations for weekly cadmium consumption of 400 microg to 500 microg. Additionally, human biomonitoring data from Canada and Alaska indicate exposure to cadmium is low except for individuals who smoke cigarettes. Given the nutritional and cultural value of subsistence foods, the Alaska Division of Public Health continues to support the consumption of moose liver and kidney as part of a well-balanced diet. Human biomonitoring studies are needed in Alaska to determine actual cadmium exposure in populations with a lifelong history of moose liver and kidney consumption.

Alaska↗
PubMed1981

Demonstration of high levels of erythropoietin in rat kidneys following hypoxic hypoxia.

Controversial hypotheses exist as to whether hypoxic kidneys produce biologically active erythropoietin (Ep) or an inactive erythropoietic factor that generates Ep from plasma protein in the blood. To clarify the role of the kidney in Ep production we attempted to extract Ep from kidneys of normal and of hypoxia exposed (6 h at 0.42 atm) Sprague-Dawley rats. Ep was measured in the microsomal fraction of kidney homogenates, using the exhypoxic polycythemic mouse assay for Ep. The Ep content was also determined in kidneys that were flushed free of blood with isotonic phosphate-buffer prior to extirpation. We found 0.04 U Ep/g in blood-depleted kidneys of normal rats. Upon exposure of the animals to hypoxia the Ep level increased to 0.92 U/g kidney. Ep levels were significantly higher in the kidney cortex than in the medulla. The erythropoietic activity in renal extracts was not enhanced after incubation of samples with homologous serum. Ep extracted from hypoxic kidneys behaved identically with plasma-Ep in the following biochemical tests: heat stability, affinity chromatography, with wheat germ lectin, ion exchange chromatography, molecular sieve chromatography, and neuraminidase inactivation. These studies support the hypothesis that kidney cortex cells are capable of producing biologically active Ep.

Animals↗
PubMed1987

Acidic amino acid transport in animal cells and tissues.

1. The occurrence and characterization of acidic amino acid transport in the plasma membrane of a variety of cells and tissues of a number of organisms is reviewed. 2. Several cell types, especially in brain, possess both high- and low-affinity transport systems for acidic amino acids. 3. High-affinity systems in brain may function to remove neurotransmitter amino acid from the extracellular environment. 4. Many cell systems for acidic amino acid transport are energized by an inwardly directed Na+ gradient. Moreover, certain cell types, such as rat brain neurons, human placental trophoblast and rabbit and rat kidney cortex epithelium, respond to an outwardly directed K+ gradient as an additional source of energization. This simultaneous action may account for the high accumulation ratios seen with acidic amino acids. 5. Rabbit kidney has been found to have a glutamate-H+ co-transport system which is subject to stimulation by protons in the medium. 6. Acidic amino acid transport in rat brain neurons occurs with a stoichiometric coupling of 1 mol of amino acid to 2 mol of Na+. For rabbit intestine, one Na+ is predicted to migrate for each mol of amino acid. 7. Uptake in rat kidney cortex and in high-K+ dog erythrocytes is electrogenic. However, uptake in rabbit and newt kidney and in rat and rabbit intestine is electroneutral. 8. Na+-independent acidic amino acid transport systems have been described in the mouse lymphocyte, the human fibroblast, the mouse Ehrlich cell and in rat hepatoma cells. 9. In a number of cell systems, D-acidic amino acids have substantial affinity for transport; D-glutamate, in a number of systems, however, appears to have little reactivity. 10. Acidic amino acid transport in some cell systems appears to occur via the "classical" routes (Christensen, Adv. Enzymol. Relat. Areas Mol. Biol. 49, 41-101, 1979). For example, uptake in the Ehrlich cell is partitioned between the Na+-dependent A system (which transports a wide spectrum of neutral amino acids), the Na+-dependent ASC system (which transports alanine, serine, threonine, homoserine, etc.), and the Na+-independent L system (which shows reactivity centering around neutral amino acids such as leucine and phenylalanine). Also, a minor component of uptake in mouse lymphocytes occurs by a route resembling the A system. 11. Human fibroblasts possess a Na+-independent adaptive transport system for cystine and glutamate that is enhanced in activity by cystine starvation.(ABSTRACT TRUNCATED AT 400 WORDS)

Amino Acids↗
PubMed1983

Formation of 6-keto prostaglandin E1 in mammalian kidneys.

1 The metabolism of prostacyclin (PGI2) and 6-keto prostaglandin F1 alpha (6-keto PGF1 alpha) was studied in cell-free homogenates of rat, rabbit and guinea-pig kidney. 2 Rabbit kidney converted both PGI2 and 6-keto PGF1 alpha to a stable metabolite with chromatographic and biological activity identical to that of authentic 6-keto PGE1. Activity was found in the kidney cortex but not medulla, was inhibited by NAD+ or NADP+ (5 mM) and showed an optimum temperature requirement of 37 degrees C. 3 Guinea-pig kidney converted PGI2 but not 6-keto PGF1 alpha to a labile, biologically active metabolite which was not 6-keto pge1. 4 No conversion of prostacyclin or 6-keto PGF1 alpha to biologically active metabolites occurred in cell-free homogenates of rat kidney, liver and colon or guinea-pig liver and colon. 5 6-keto PGE1 rapidly lost spasmogenic activity on the rat stomach strip following incubation with rabbit or guinea-pig kidney supernatant in the absence of added cofactors. No loss of activity occurred on incubation with rat kidney. 6 Rutin (50 microM) potently inhibited synthesis of 6-keto PGE1 from added PGI2 by rabbit kidney cortex. This reaction was potentiated by a similar concentration of sulphasalazine, carbenoxolone, imidazole, papaverine or indomethacin. 7 The relevance of these findings for the possible physiological and pathological roles of 6-keto PGE1 in the kidney is discussed.

Alprostadil↗
PubMedDate not supplied

4-D micro-CT of the mouse heart.

PURPOSE: Demonstrate noninvasive imaging methods for in vivo characterization of cardiac structure and function in mice using a micro-CT system that provides high photon fluence rate and integrated motion control. MATERIALS AND METHODS: Simultaneous cardiac- and respiratory-gated micro-CT was performed in C57BL/6 mice during constant intravenous infusion of a conventional iodinated contrast agent (Isovue-370), and after a single intravenous injection of a blood pool contrast agent (Fenestra VC). Multiple phases of the cardiac cycle were reconstructed with contrast to noise and spatial resolution sufficient for quantitative assessment of cardiac function. RESULTS: Contrast enhancement with Isovue-370 increased over time with a maximum of approximately 500 HU (aorta) and 900 HU (kidney cortex). Fenestra VC provided more constant enhancement over 3 hr, with maximum enhancement of approximately 620 HU (aorta) and approximately 90 HU (kidney cortex). The maximum enhancement difference between blood and myocardium in the heart was approximately 250 HU for Isovue-370 and approximately 500 HU for Fenestra VC. In mice with Fenestra VC, volumetric measurements of the left ventricle were performed and cardiac function was estimated by ejection fraction, stroke volume, and cardiac output. CONCLUSION: Image quality with Fenestra VC was sufficient for morphological and functional studies required for a standardized method of cardiac phenotyping of the mouse.

Animals↗
PubMed1993

Zinc metabolism in fasted rats.

The effects of short-term starvation on serum and tissue levels of zinc, metallothionein (MT), and the activity of alkaline phosphatase (EC 3.1.3.1, ALP) were investigated with 6-month-old rats. The rats were fed a diet with adequate zinc (92mg/kg of Zn, 1.12% phytic acid) before they were starved for 0h (control), 12h, 24h, and 36h and then killed by decapitation. Fasting was accompanied by typical changes in serum parameters such as reduced glucose and protein concentrations, elevated ketogenesis, and a rapid breakdown of liver glycogen. Fasting did not alter serum zinc levels, but it did lead to a significant elevation in the percent of unsaturated serum-zinc binding capacity. Liver concentrations of zinc and MT, based both on fresh and dry weight, were increased throughout starvation. However, total liver zinc was reduced by up to 23% in response to fasting and total liver MT was slightly elevated. The increased concentrations of liver zinc and MT are, therefore, mainly a consequence of reduced liver weight. A part of the liver zinc, however, was bound to newly synthesized MT to prevent greater zinc loss. Starvation evoked no altered mucosa MT levels. Changes in kidney zinc and kidney medulla MT caused by starvation were small and not significant. In contrast to this observation some variation of kidney cortex MT was apparent. Starvation produced a permanent reduction of the serum and intestinal activity of ALP. In the liver and the medulla of the kidneys no significant differences of ALP activity could be observed. However, kidney cortex ALP was induced after 36h of fasting.(ABSTRACT TRUNCATED AT 250 WORDS)

Alkaline Phosphatase↗