Microassay for cathepsin D shows an unexpected effect of cycloheximide on limb-bone rudiments in organ culture

Hille, Merrill B.; Barrett, Annabella; Dingle, J. T.; Fell, Honor B.

doi:10.1016/0014-4827(70)90476-3

Cited by 75 publications

(12 citation statements)

References 9 publications

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“…This Awas then stirred with a glass-coated metal bar for 20-60 min in a glass universal on a magnetic stirring base (Gallenkamp, London) at Setting 2. The proteolytic activity in the collagenase preparation used was measured as described previously (Hille et al, 1970). A solution containing 0-2 mg/ ml of the collagenase preparation was found to contain the equivalent of 2 ,ug/ml of trypsin.…”

Section: Methodsmentioning

confidence: 99%

Radioiodination studies of tumour cell-surface proteins after different disaggregation procedures

Droogmans¹,

Latner²,

Turner³

1977

Br J Cancer

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Summary.-The surface of single cells isolated from solid tumours by either a mechanical or an enzymatic method have been compared, using lactoperoxidasecatalyzed radioiodination of the tyrosine-containing proteins. Qualitatively, the patterns of surface labelling were similar, and duplicate experiments indicated that each method of isolation gave reproducible results. Analysis of incorporated label into 4 defined sections of the electrophoretic pattern illustrated quantitative differences. When the cells were isolated mechanically, the incorporation into low-mol.-wt. components was considerably reduced, whereas that into the high-mol.-wt. components was unaffected. Treatment of enzymatically isolated cells with trypsin also reduced incorporation into low-mol.-wt. components.

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Section: Methodsmentioning

confidence: 99%

Radioiodination studies of tumour cell-surface proteins after different disaggregation procedures

Droogmans¹,

Latner²,

Turner³

1977

Br J Cancer

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“…was determined in formate buffer at pH 2.8 using (methylu C)methemoglobin (NEN chemicals GmbH, Dreieich, FRG) as substrate similar to Hille at al. 16 After the addition of Ro 42-5892 in various concentrations, the samples were incubated for 1 hour at 37°C. Then, the nondigested proteinic material was precipitated by trichloroacetic acid (7.5%) and an aliquot of the supernatant counted in a liquid scintillation (0) counter.…”

Section: In Vitro Experimentsmentioning

confidence: 99%

Ro 42-5892 is a potent orally active renin inhibitor in primates.

et al. 1991

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The goal of the present study was to characterize the new renin inhibitor Ro 42-5892 in vitro and in vivo. In vitro, Ro 42-5892 inhibited purified human renin and human plasma renin specifically with an IC M of 0.7 nM and 0.8 nM, respectively. In vivo, Ro 42-5892 reduced mean arterial blood pressure in sodium-depleted marmosets and squirrel monkeys with as low a dose as 0.1 nig/kg orally. Higher doses reduced pressure by 30-35 mm Hg in both species. The duration of blood pressure decrease with 3 ing/kg orally was more than 24 hours. Maximal changes of plasma renin activity, immunoreactive angiotensin I, and immunoreactive angiotensin II were observed at 15 minutes. Renin was reduced by 74±31%, angiotensin I by 85±14%, angiotensin II by 89±17%, and immunoreactive active renin was increased by 70±39%. However, unlike pressure, these maximal effects were only transient with complete recovery of renin at 60 minutes under still reduced levels of angiotensin I (61 ±24%) and angiotensin II (71 ±38%) and increased concentrations of active renin (86±30%). The blood pressure lowering was due to specific renin inhibition as exemplified by the influence of the kidney, sodium status, species, or stereoselectivity. Moreover, the reduction of arterial blood pressure was similar to the action of the angiotensin converting enzyme inhibitor cilazapril and was not associated with reflex tachycardia in contrast to the pure vasodilator minoxidil. We conclude that Ro 42-5892 is a potent orally active renin inhibitor acting mainly by inhibition of renin in an extraplasmatic compartment (Hypertension 1991;18:22-31)

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“…Proteolysis of this substrate was measured essentially as described by Hille et a1 (16). Each incubation contained 60-pl aliquots of the tissue extracts and 10 pl of 0.05 M glycine/HCI, pH 2.8, 10 pl of unlabeled hemoglobin (10% w/v), and 20pl of 1251-hemoglobin containing lo4 cpm.…”

Section: Methodsmentioning

confidence: 99%

Carrageenin‐induced arthritis. III. Proteolytic enzymes present in rabbit knee joints after a single intraarticular injection of carrageenin

Lowther

Gillard

Baxter

et al. 1976

Arthritis & Rheumatism

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Microassay for cathepsin D shows an unexpected effect of cycloheximide on limb-bone rudiments in organ culture

Cited by 75 publications

References 9 publications

Radioiodination studies of tumour cell-surface proteins after different disaggregation procedures

Radioiodination studies of tumour cell-surface proteins after different disaggregation procedures

Ro 42-5892 is a potent orally active renin inhibitor in primates.

Carrageenin‐induced arthritis. III. Proteolytic enzymes present in rabbit knee joints after a single intraarticular injection of carrageenin

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