Conversion between renin and high-molecular-weight renin in the dog

Funakawa, Susumu; Funae, Yoshihiko; Yamamoto, Kenjiro

doi:10.1042/bj1760977

Cited by 48 publications

(20 citation statements)

References 14 publications

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“…21 These data have been supported by findings of other investigators. 22 However, Kawamura et al 23 more recently found a small amount of inactive renin in the dog kidney.…”

Section: Discussionsupporting

confidence: 82%

Urinary excretion of renin and its biochemical properties in dogs.

Yukimura¹,

Miura²,

Matsushima³

et al. 1984

Hypertension

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TOKIHITO YUKIMURA, KATSUYUKI MIURA, YOHKAZU MATSUSHIMA, FUMIHIKO IKEMOTO, AND KENJIRO YAMAMOTO SUMMARY The amount and biochemical properties of renin excreted by anesthetized dogs were investigated to elucidate the significance of urinary excretion in the metabolism of renin. Mean arterial blood pressure was 127 ± 4 mm Hg, renal blood flow was 170 ± 8 ml/min, glomerular filtration rate, 38.6 ± 2.3 ml/min, and urine flow rate, 0.37 ± 0.09 ml/min (n = 11). Urinary renin concentration (URC) was 9.2 ± 2.1 ng angiotensin I (ANG I)/ml-hr (n = 11), as determined by radioimmunoassay for ANG I generated by incubation with semipurified homologous renin substrate. The ANG I-producing activity was inhibited by more than 90% by a specific antibody to dog kidney renin. The renin secretion rate from the left kidney into the renal vein was 76.4 ± 13.3 ng ANG 1/ ml-hr per min (n = 11), and the simultaneous urinary excretion rate of renin was 2.3 ± 0.4 ng ANG 1/ ml-hr per min(n = 11). Molecular weight of the urinary renin was 40,000 daltons. The pH dependent curves of the angiotensin-forming capacity of renin showed an optimum between pH 5.5 to 6.0, and the estimated Michaelis constant was 0.42 /J,M. These biochemical parameters were similar to the findings in the case of renin in the plasma and the kidney. Moreover, neither acid nor trypsin treatment altered the renin activity in the urine. Thus, the active form of renin with a molecular weight 40,000 was excreted into the urine in dogs. Urinary excretion of renin was a small percentage of the renin secretion rate, thereby indicating the minor role of urinary excretion in the metabolism of renin. (Hypertension 6: 837-842, 1984) KEY WORDS • antirenin antibody • renin secretion rate high performance liquid chromatography

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“…21 These data have been supported by findings of other investigators. 22 However, Kawamura et al 23 more recently found a small amount of inactive renin in the dog kidney.…”

Section: Discussionsupporting

confidence: 82%

Urinary excretion of renin and its biochemical properties in dogs.

Yukimura¹,

Miura²,

Matsushima³

et al. 1984

Hypertension

Self Cite

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“…Sagnella et al [17] and our group [22] have indicated that renin stored in renin granules of rat kidney could not be activated by acidification. Funakawa et al [23] also reported similar findings using dog kidney extract. On the other hand.…”

Section: Discussionsupporting

confidence: 71%

Renin Granules Isolated from Rat Kidney Cortex by Continuous Colloidal Silica (Percoll) Density Gradient Centrifugation

Matsumura¹,

Takeshita²,

Miyawaki³

et al. 1986

Kidney Blood Press Res

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Renin granules were isolated from rat kidney cortex by a continuous polyvinyl-pyrrolidone-coated colloidal silica (Percoll) density gradient centrifugation. A major peak of renin activity was found at a density of 1.12–1.13 g/ml, and the specific activity of renin in the peak fraction was increased by approximately 70-fold, as compared with that in the kidney cortex homogenate. On the other hand, activities of other reference enzymes, such as succinate dehydrogenase, acid phosphatase and glucose-6-phosphatase, were not detectable in the peak fraction. When the extract of the peak fraction was applied to a pepstatin column, trypsin-activated renin could not be detected in the breakthrough fractions. These results indicate that renin granules of the rat kidney cortex contain only active renin.

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“…3). Renin from granular structures of the dog 27 also displayed a MW of about 40,000, indicating that in these species the storage form of renin is of the LMW type. In the present studies, the possibility of proteolytic conversion of renin by enzymes from other subcellular organelles was minimized by the rapid isolation of subcellular organelles and the subsequent osmotic lysis at 0°C before gel filtration on Sephadex G-100.…”

Section: Effect Of N-ethylmaleimlde On Gel Filtration Of Renin From Smentioning

confidence: 99%

Subcellular distribution and storage form of rat renal renin.

Sagnella¹,

Price²,

Peart³

1980

Hypertension

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SUMMARYThe subcellular distribution and nature of rat renal renin has been Investigated by means of analytical subcellular fractionation and gel filtration on Sephadex G-100. During differential centrifugation, renin activity was recovered mainly in soluble and heary mltochondrial fractions. On sucrose gradient centrifugation in either a conventional or in a B XIV zonal rotor, renin activity equilibrated at 1.54 M sucrose and was partially resolved from marker enzymes for mitochondria (succinate debydrogenase), lysosomes (acid phosphatase), plasma membranes (alkaline phosphatase), and peroxisomes (catalase). On gel filtration of the soluble or extracts of the renin-granular fractions on Sepbadex G-100, renin activity eluted as a single peak with an apparent molecular weight (MW) of 42,000; no change In activity was found when these fractions were acidified to pH 3.0. When kidney homogenates were prepared in the presence of the proteolytic inhibitor Nethylmaleimide (NEM, 10 mM), whereas the renin from the granular fractions displayed a MW of 44,000, that from the soluble fraction was apparently higher (69,000). Addition of NEM (10 mM) to the soluble fraction previously shown to contain only the low MW form of renin also resulted in an apparently high MW form of renin.These results indicate that rat renal renin is associated with a mechanically fragile, distinct type of subcellular organelle. Renin within this structure is of the low MW form and is not acid activatable. 3 "* have been contradictory as to the precise subcellular distribution of the enzyme. Also, limited information is available on the nature of the storage form of rat renin. It has been reported, however, that rat renin is stored as an inactive form that can be activated by acidification to pH 3.3,' yet others 7 '' have been unable to demonstrate acid activatable forms of rat renin.Recently, Inagami et al. 9 found that, in the presence of the proteolytic inhibitor N-ethylmaleimide, only a high molecular weight (HMW) form of renin (60,000) was extracted from the rat kidney; consequently they concluded that this form of renin represented a precursor of the low molecular weight (LMW) form of the enzyme. However, since these studies were carried out with crude soluble cortical extracts, the relationship between this HMW form of renin and the granular renin remained undetermined.Therefore, it was thought of importance to investigate further the subcellular distribution of renin and in particular to determine the effect of acidification and N-ethylmaleimide on the activity and molecular size of renin not only from soluble but also from granular fractions. 595 Materials and Methods Preparation of Cortical HomogenatesMale Wistar rats (180-200 g) that had free access to water and standard laboratory food were killed by cervical dislocation. The kidneys were removed, stripped of the capsule and bisected. The cortices were

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Conversion between renin and high-molecular-weight renin in the dog

Cited by 48 publications

References 14 publications

Urinary excretion of renin and its biochemical properties in dogs.

Urinary excretion of renin and its biochemical properties in dogs.

Renin Granules Isolated from Rat Kidney Cortex by Continuous Colloidal Silica (Percoll) Density Gradient Centrifugation

Subcellular distribution and storage form of rat renal renin.

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