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Journal articles on the topic 'Leupeptin'

Author: Grafiati

Published: 5 June 2025

Last updated: 1 August 2025

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1

Yoshinari, Mototaka, and Alvin Taurog. "Physiological role of thiol proteases in thyroid hormone secretion." Acta Endocrinologica 113, no. 2 (1986): 261–67. http://dx.doi.org/10.1530/acta.0.1130261.

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Abstract. To determine the physiological role of the thiol proteases in T4 and T3 release from thyroglobulin, experiments were performed with 131I-prelabelled rat thyroid lobes incubated in vitro in the presence and absence of leupeptin, an inhibitor of thiol proteases. Basal secretion of [131I]T4 and [131I]T3 from rat thyroid lobes prelabelled in vivo was quite low, but in the presence of 10 mU/ml bovine TSH a marked stimulatory effect was observed. The stimulatory effect of TSH was completely abolished by leupeptin. This was associated with marked inhibition of lysosomal proteolytic activity

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2

KIM, In Seop, Young Bae KIM, and Kye Joon LEE. "Characterization of the leupeptin-inactivating enzyme from Streptomyces exfoliatus SMF13 which produces leupeptin." Biochemical Journal 331, no. 2 (1998): 539–45. http://dx.doi.org/10.1042/bj3310539.

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Leupeptin-inactivating enzyme (LIE) was purified from Streptomyces exfoliatusSMF13 by ammoniumm sulphate fractionation of cell-free culture broth, ultrafiltration, anion-exchange chromatography on DEAE–Sephadex A-50 and gel filtration chromatography on Sephadex G-75. The molecular mass of the purified enzyme was measured as 34700 Da and the N-terminal amino acid sequence was APTPPDIPLANVPA. Acetyl-leucine, leucine and argininal were identified as the products of leupeptin inactivated by the LIE, indicating that leupeptin is inactivated by hydrolysis of peptide bond between leucine and leucine

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3

BADALAMENTE, MARIE A., L. C. HURST, S. B. PAUL, and A. STRACHER. "Enhancement of Neuromuscular Recovery after Nerve Repair in Primates." Journal of Hand Surgery 12, no. 2 (1987): 211–17. http://dx.doi.org/10.1016/0266-7681_87_90015-5.

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This investigation describes the use of the calcium-activated protease inhibitor, leupeptin, as an adjunctive therapy to the microsurgical repair of median nerves in a primate model. Our results indicate that leupeptin facilitates morphological recovery in denervated thenar muscles and in distal sensory and mixed motor-sensory nerve trunks and functional recovery measured by motor nerve conduction velocity. Toxicological testing of leupeptin showed that, when administered at a dose of 12mg/kg, intramuscularly, once daily, haematological and clotting profiles were not adversely affected.

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Noda, Toru, Mary L. Bronson, Shang-Ming Yu, and Marilyn G. Farquhar. "The 215 KD mannose-6-phosphate receptor is involved in crinophagy but not in autophagy." Proceedings, annual meeting, Electron Microscopy Society of America 48, no. 3 (1990): 932–33. http://dx.doi.org/10.1017/s0424820100162223.

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Autophagy and crinophagy represent the two major pathways for digestion of intracellular material via lysosomes have been described. Though both phenomena involve in corporation of cell organelles into lysosomes and thus degradation by lysosomal enzymes, the process by which autophagic and crinophagic vacuoles acquire lysosomal enzymes remains to be clarified. The aim of this work is to find out if mannose-6-phosphate (M6P) receptors are involved in this process. As a typical working model, we used hepatocytes of leupeptin-treated rats for autophagy (Fig. 1) and mammotrophs of female rats trea

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Zachgo, S., B. Dobberstein, and G. Griffiths. "A block in degradation of MHC class II-associated invariant chain correlates with a reduction in transport from endosome carrier vesicles to the prelysosome compartment." Journal of Cell Science 103, no. 3 (1992): 811–22. http://dx.doi.org/10.1242/jcs.103.3.811.

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Invariant chain (Ii) associated with MHC class II molecule is processed proteolytically via several distinct intermediates during its intracellular transport through endosomal compartments. Leupeptin added to the culture medium blocks processing of Ii, prevents its dissociation from the class II molecules and leads to an intracellular accumulation of a 22 kDa intermediate form of Ii. We show here that leupeptin has a very general effect on protein transport in the endocytic pathway. When added to Mel Juso cells leupeptin reduces the transport of endocytosed material from multivesicular body-li

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Subramanyam, Sarvepalli B., Aparna Tipirneni, Nazih Youssef, Generoso G. Gascon, and Pinar T. Ozand. "Biochemical Heterogeneity of Infantile Central Nervous System Spongy Degeneration." Journal of Child Neurology 7, no. 1_suppl (1992): S22—S25. http://dx.doi.org/10.1177/08830738920070010411.

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Aspartoacylase, the enzyme whose activity is deficient in infantile central nervous system spongy degeneration (Canavan-Van Bogaert-Bertrand disease), is detected as an approximately 59-kD protein in the Sephadex G-200 filtration of normal fibroblast extracts. The enzyme activity in homogenates of fibroblasts is protected by leupeptin, a protease inhibitor. In the absence of leupeptin, 90% of aspartoacylase activity is lost. In some patients with infantile spongy degeneration, no activity (less than 2%) can be detected. In some other patients with residual activity in fibroblasts, two separate

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7

Yamashita, Kouwa, Keiko Watanabe, Hideki Takayama, et al. "Assay of plasma leupeptin using the reversible binding of leupeptin to bovine pancreatic trypsin." Analytical Biochemistry 156, no. 2 (1986): 503–7. http://dx.doi.org/10.1016/0003-2697(86)90285-x.

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8

Freeman, Stuart J., and Nigel A. Brown. "Comparative effects of cathepsin inhibitors on rat embryonic development in vitro. Evidence that cathepsin D is unimportant in the proteolytic function of yolk sac." Development 86, no. 1 (1985): 271–81. http://dx.doi.org/10.1242/dev.86.1.271.

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The effects of two proteinase inhibitors, leupeptin and pepstatin on the development of 9·5-day rat conceptuses in vitro has been studied. All cultures were of 48 h duration and the inhibitors were present throughout the entire period. When pepstatin was added to the culture medium (5–25 μg/ml) conceptuses developed and grew to an extent that did not differ from untreated controls. However, leupeptin (l–4 μg/ml) caused severe growth retardation and abnormal development of conceptuses. The effects of the two inhibitors on the hydrolysis of 125I-labelled BSA and haemoglobin by homogenates of 10·

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9

Selsby, Joshua, Klara Pendrak, Monica Zadel, et al. "Leupeptin-based inhibitors do not improve the mdx phenotype." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 299, no. 5 (2010): R1192—R1201. http://dx.doi.org/10.1152/ajpregu.00586.2009.

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Calpain activation has been implicated in the disease pathology of Duchenne muscular dystrophy. Inhibition of calpain has been proposed as a promising therapeutic target, which could lessen the protein degradation and prevent progressive fibrosis. At the same time, there are conflicting reports as to whether elevation of calpastatin, an endogenous calpain inhibitor, alters pathology. We compared the effects of pharmacological calpain inhibition in the mdx mouse using leupeptin and a proprietary compound (C101) that linked the inhibitory portion of leupeptin to carnitine (to increase uptake int

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10

Al, Z., and C. M. Cohen. "Phorbol 12-myristate 13-acetate-stimulated phosphorylation of erythrocyte membrane skeletal proteins is blocked by calpain inhibitors: possible role of protein kinase M." Biochemical Journal 296, no. 3 (1993): 675–83. http://dx.doi.org/10.1042/bj2960675.

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Human erythrocytes contain cytosolic protein kinase C (PKC) which, when activated by phorbol 12-myristate 13-acetate (PMA), induces the phosphorylation of the membrane skeletal proteins band 4.1, band 4.9 and adducin. We found that brief treatments of erythrocytes with PMA resulted in a decrease in cytosolic PKC content and in the transient appearance in the cytosol of a Ca(2+)- and phospholipid-independent 55 kDa fragment of PKC, called PKM. Prolonged treatment with PMA resulted in the complete and irreversible loss of erythrocyte PKC. To investigate the possible role of calpain in this proce

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11

Lisk, Godfrey, Margaret Pain, Ilya Y. Gluzman, et al. "Changes in the Plasmodial Surface Anion Channel Reduce Leupeptin Uptake and Can Confer Drug Resistance in Plasmodium falciparum-Infected Erythrocytes." Antimicrobial Agents and Chemotherapy 52, no. 7 (2008): 2346–54. http://dx.doi.org/10.1128/aac.00057-08.

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ABSTRACT Cysteine protease inhibitors kill malaria parasites and are being pursued for development as antimalarial agents. Because they have multiple targets within bloodstream-stage parasites, workers have assumed that resistance to these inhibitors would not be acquired easily. In the present study, we used in vitro selection to generate a parasite resistant to growth inhibition by leupeptin, a broad-profile cysteine and serine protease inhibitor. Resistance was not associated with upregulation of cysteine protease activity, reduced leupeptin sensitivity of this activity, or expression level

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Elden, T. C. "Influence of a Cysteine Proteinase Inhibitor on Alfalfa Weevil (Coleoptera: Curculionidae) Growth and Development Over Successive Generations." Journal of Entomological Science 35, no. 1 (2000): 70–76. http://dx.doi.org/10.18474/0749-8004-35.1.70.

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The influence of leupeptin, a cysteine and serine proteinase inhibitor, on alfalfa weevil, Hypera postica (Gyllenhal), growth and development was investigated over nine successive generations. Concern that ingestion of proteinase inhibitors by phytophagous insects could induce production of inhibitor-insensitive proteinase activity initiated this investigation. The percent alfalfa weevil larval, pupal and adult survival, and defoliation was significantly lower on alfalfa foliage treated with leupeptin than on untreated foliage in all nine generations tested. Main effects for generations and tr

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13

Vidard, L., K. L. Rock, and B. Benacerraf. "The generation of immunogenic peptides can be selectively increased or decreased by proteolytic enzyme inhibitors." Journal of Immunology 147, no. 6 (1991): 1786–91. http://dx.doi.org/10.4049/jimmunol.147.6.1786.

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Abstract The ability of splenic APC and a B cell hybridoma (LS.102.9) to process and present OVA to a panel of T-T hybridomas with different fine specificities was investigated. Splenic APC process and present OVA to all the T-T hybrids. The B cell hybridoma could similarly process and present OVA to some T-T hybrids but was very inefficient in stimulating two of the T cell hybridomas. The presentation of native OVA to these two T-T hybrids was significantly increased by leupeptin. Pulsing experiments demonstrated that leupeptin acted on the APC at a step before the processed Ag was displayed

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14

SAINO, TETSUSHI, TETSUYA SOMENO, SHIN-ICHI ISHII, TAKAAKI AOYAGI, and HAMAO UMEZAWA. "Protease-inhibitory activities of leupeptin analogues." Journal of Antibiotics 41, no. 2 (1988): 220–25. http://dx.doi.org/10.7164/antibiotics.41.220.

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15

Kim, In Seop, and Kye Joon Lee. "Regulation of production of leupeptin, leupeptin-inactivating enzyme, and trypsin-like protease in Streptomyces exfoliatus SMF13." Journal of Fermentation and Bioengineering 80, no. 5 (1995): 434–39. http://dx.doi.org/10.1016/0922-338x(96)80916-0.

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16

Knowles, S. E., M. F. Hopgood, and F. J. Ballard. "Effects of inhibitors on aldolase breakdown after its microinjection into HeLa cells." Biochemical Journal 259, no. 1 (1989): 27–33. http://dx.doi.org/10.1042/bj2590027.

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1. The regulation of protein breakdown as well as the generation of intermediates in the pathway from intact protein to amino acids was investigated by using 3H-labelled N-ethylmaleimide-modified aldolase (NEM-aldolase) as an indicator protein after its microinjection into HeLa cells. 2. NEM-aldolase degradation to acid-soluble products proceeded at a slower rate than that of endogenously labelled total cell protein, and was inhibited to a greater extent by 3-methyladenine, leupeptin and NH4Cl. The combination of leupeptin plus NH4Cl was particularly effective, decreasing the NEM-aldolase brea

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17

Musil, L. S., and J. U. Baenziger. "Cleavage of membrane secretory component to soluble secretory component occurs on the cell surface of rat hepatocyte monolayers." Journal of Cell Biology 104, no. 6 (1987): 1725–33. http://dx.doi.org/10.1083/jcb.104.6.1725.

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Rat liver secretory component is synthesized as an integral membrane protein (mSC) and cleaved to an 80-kD soluble form (fSC) sometime during transcellular transport from the sinusoidal to the bile canalicular plasma membrane domain of hepatocytes. We have used 24-h monolayer cultures of rat hepatocytes to characterize the conversion of mSC to fSC. Cleavage of mSC in cultured hepatocytes is inhibited by the thiol protease inhibitors leupeptin, antipain, and E-64, but not by other inhibitors, including disopropylfluorophosphate, pepstatin, N-ethylmalemide, p-chloromercuribenzoic acid, and chlor

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18

Gavriel, Haim, Abraham Shulman, Alfred Stracher, and Haim Sohmer. "Leupeptin reduces impulse noise induced hearing loss." Journal of Occupational Medicine and Toxicology 6, no. 1 (2011): 38. http://dx.doi.org/10.1186/1745-6673-6-38.

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19

Dennis, Patricia A., and Nathan N. Aronson. "Metabolism of [3H]leupeptin by rat liver." Archives of Biochemistry and Biophysics 240, no. 2 (1985): 768–76. http://dx.doi.org/10.1016/0003-9861(85)90085-2.

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20

McConnell, Rose M., George E. Barnes, Charles F. Hoyng, and J. Martin Gunn. "New leupeptin analogs: synthesis and inhibition data." Journal of Medicinal Chemistry 33, no. 1 (1990): 86–93. http://dx.doi.org/10.1021/jm00163a014.

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21

Soji, Kasayama, Noma Keizo, Sato Bunzo, et al. "Leupeptin inhibits the transformation of glucocorticoid receptor." Journal of Steroid Biochemistry 28, no. 3 (1987): 273–77. http://dx.doi.org/10.1016/0022-4731(87)91018-1.

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22

Moore, R. H., A. Tuffaha, E. E. Millman, et al. "Agonist-induced sorting of human beta2-adrenergic receptors to lysosomes during downregulation." Journal of Cell Science 112, no. 3 (1999): 329–38. http://dx.doi.org/10.1242/jcs.112.3.329.

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During prolonged exposure to agonist, beta2-adrenergic receptors undergo downregulation, defined by the loss of radioligand binding sites. To determine the cellular basis for beta2-adrenergic receptor downregulation, we examined HEK293 cells stably expressing beta2-adrenergic receptors with an N-terminal epitope tag. Downregulation was blocked by leupeptin, a cysteine protease inhibitor, but not by pepstatin, an inhibitor of aspartate proteases. Immunofluorescence microscopy of cells treated with agonist for 3–6 hours in the presence of leupeptin showed beta2-adrenergic receptors, but not tran

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23

Samarel, A. M., A. G. Ferguson, R. S. Decker, and M. Lesch. "Effects of cysteine protease inhibitors on rabbit cathepsin D maturation." American Journal of Physiology-Cell Physiology 257, no. 6 (1989): C1069—C1079. http://dx.doi.org/10.1152/ajpcell.1989.257.6.c1069.

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To examine the effects of cysteine protease inhibitors on cathepsin D intracellular transport, proteolytic processing, and secretion, primary cultures of rabbit cardiac fibroblasts were grown to confluence and exposed (24 h) to media containing leupeptin (0-10 mM), E 64 (0-10 mM), or chloroquine (0-50 microM). Cathepsin D maturation was then evaluated in pulse-chase biosynthetic labeling experiments. None of the three agents affected the charge modification of procathepsin D (Mr 53,000) within the Golgi apparatus. However, all three agents interfered with the subsequent proteolytic processing

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Yamamoto, A., R. Masaki, Y. Fukui, and Y. Tashiro. "Absence of cytochrome P-450 and presence of autolysosomal membrane antigens on the isolation membranes and autophagosomal membranes in rat hepatocytes." Journal of Histochemistry & Cytochemistry 38, no. 11 (1990): 1571–81. http://dx.doi.org/10.1177/38.11.2212617.

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We wished to determine if phenobarbital (PB)-inducible cytochrome P-450 [P-450(PB)] and autolysosomal membrane antigens could be localized immunocytochemically on the isolation membranes and the limiting membranes of autophagosomes in rat hepatocytes by the post-embedding protein A-gold method. P-450(PB) was maximally induced by PB treatment; then formation of autophagosomes and accumulation of autolysosomes were induced by cessation of PB treatment and by injection of leupeptin, respectively. P-450(PB) was detected neither on the isolation membranes nor on the limiting membranes of autophagos

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McNicol, Archibald, Jon M. Gerrard, and D. Euan MacIntyre. "Evidence for two mechanisms of thrombin-induced platelet activation: one proteolytic, one receptor mediated." Biochemistry and Cell Biology 67, no. 7 (1989): 332–36. http://dx.doi.org/10.1139/o89-052.

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The possibility that thrombin-induced platelet reactivity could occur via both a receptor-related and a proteolytic process was examined. Thrombin elicited the formation of considerably more [32P)phosphatidic acid (an index of phospholipase C catalysed phosphoinositide metabolism) than did platelet activating factor, 5-hydroxytryptamine, ADP, and the thromboxane A2 analogue EP171, when these agents were added either alone or in combination. Co-addition of thrombin and EP171 did not evoke significantly more [32P]phosphatidic acid than did thrombin alone. The protease inhibitor leupeptin, decrea

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Iizuka, Hideaki, Yuzo Iwasaki, Teiji Yamamoto, and Satoru Kadoya. "Morphometric assessment of drug effects in experimental spinal cord injury." Journal of Neurosurgery 65, no. 1 (1986): 92–98. http://dx.doi.org/10.3171/jns.1986.65.1.0092.

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✓ The effect of large doses of methylprednisolone sodium succinate (MPSS) and two protease inhibitors, leupeptin and bestatin, on experimental acute spinal cord injury was evaluated by morphometric analysis of degenerating axons with the aid of an automated image analyzer. Spinal cord injury was produced by epidural compression with a surgical clip on the T-11 segment in rats. The extent of axonal damage was assessed in Rexed's lamina VIII in the L-6 segment by measuring the amount of silver grains, representing degenerating axons and their terminals, using the Fink-Heimer method. The severity

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Sharma, Paresh, Kempaiah Rayavara, Daisuke Ito, Katherine Basore, and Sanjay A. Desai. "A CLAG3 Mutation in an Amphipathic Transmembrane Domain Alters Malaria Parasite Nutrient Channels and Confers Leupeptin Resistance." Infection and Immunity 83, no. 6 (2015): 2566–74. http://dx.doi.org/10.1128/iai.02966-14.

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Erythrocytes infected with malaria parasites have increased permeability to ions and nutrients, as mediated by the plasmodial surface anion channel (PSAC) and recently linked to parasiteclag3genes. Although the encoded protein is integral to the host membrane, its precise contribution to solute transport remains unclear because it lacks conventional transmembrane domains and does not have homology to ion channel proteins in other organisms. Here, we identified a probable CLAG3 transmembrane domain adjacent to a variant extracellular motif. Helical-wheel analysis revealed strict segregation of

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Richardson, J. M., N. A. Woychik, D. L. Ebert, R. L. Dimond, and J. A. Cardelli. "Inhibition of early but not late proteolytic processing events leads to the missorting and oversecretion of precursor forms of lysosomal enzymes in Dictyostelium discoideum." Journal of Cell Biology 107, no. 6 (1988): 2097–107. http://dx.doi.org/10.1083/jcb.107.6.2097.

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Lysosomal enzymes are initially synthesized as precursor polypeptides which are proteolytically cleaved to generate mature forms of the enzymatically active protein. The identification of the proteinases involved in this process and their intracellular location will be important initial steps in determining the role of proteolysis in the function and targeting of lysosomal enzymes. Toward this end, axenically growing Dictyostelium discoideum cells were pulse radiolabeled with [35S]methionine and chased in fresh growth medium containing inhibitors of aspartic, metallo, serine, or cysteine prote

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Maes, Karen, Dries Testelmans, Scott Powers, Marc Decramer, and Ghislaine Gayan-Ramirez. "Leupeptin Inhibits Ventilator-induced Diaphragm Dysfunction in Rats." American Journal of Respiratory and Critical Care Medicine 175, no. 11 (2007): 1134–38. http://dx.doi.org/10.1164/rccm.200609-1342oc.

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Wang, Jian, Dalian Ding, Abraham Shulman, Alfred Stracher, and Richard J. Salvi. "Leupeptin protects sensory hair cells from acoustic trauma." NeuroReport 10, no. 4 (1999): 811–16. http://dx.doi.org/10.1097/00001756-199903170-00027.

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Thornton, S., JM Davison, and PH Baylis. "Leupeptin Does not Prevent Oxytocin Degradation by Oxytocinase." Clinical Science 74, s18 (1988): 23P. http://dx.doi.org/10.1042/cs074023pb.

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Billinger, Erika, Johan Viljanen, Sara Bergström Lind, and Gunnar Johansson. "Inhibition properties of free and conjugated leupeptin analogues." FEBS Open Bio 10, no. 12 (2020): 2605–15. http://dx.doi.org/10.1002/2211-5463.12994.

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33

Kurinov, I. V., and R. W. Harrison. "Two crystal structures of the leupeptin-trypsin complex." Protein Science 5, no. 4 (1996): 752–58. http://dx.doi.org/10.1002/pro.5560050420.

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Veeraragavan, Kannappan, and Claude Gagnon. "Leupeptin and chymostatin inhibit mammalian protein methylesterase activity." Biochemical and Biophysical Research Communications 142, no. 2 (1987): 603–8. http://dx.doi.org/10.1016/0006-291x(87)90316-0.

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CARTWRIGHT, Ian J., and Joan A. HIGGINS. "Intracellular degradation in the regulation of secretion of apolipoprotein B-100 by rabbit hepatocytes." Biochemical Journal 314, no. 3 (1996): 977–84. http://dx.doi.org/10.1042/bj3140977.

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Isolated rabbit hepatocytes were incubated with [35S]methionine to label intracellular pools of apolipoprotein B (apo-B). The cells were then reincubated with an excess of unlabelled methionine in the presence of oleate or protease inhibitors and the intracellular sites of accumulation of radiolabelled apo-B and the mass of apo-B were determined by isolation and analysis of subcellular fractions. Oleate or inhibitors of metalloproteases (o-phenanthroline), serine proteases (aprotinin), serine/cysteine proteases (leupeptin) or cysteine proteases (calpain inhibitor I; ALLN) but not aspartate pro

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Hariri, Mehrdad, Ghania Millane, Marie-Pierre Guimond, Ginette Guay, James W. Dennis, and Ivan R. Nabi. "Biogenesis of Multilamellar Bodies via Autophagy." Molecular Biology of the Cell 11, no. 1 (2000): 255–68. http://dx.doi.org/10.1091/mbc.11.1.255.

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Transfection of Mv1Lu mink lung type II alveolar cells with β1–6-N-acetylglucosaminyl transferase V is associated with the expression of large lysosomal vacuoles, which are immunofluorescently labeled for the lysosomal glycoprotein lysosomal-associated membrane protein-2 and the β1–6-branchedN-glycan-specific lectin phaseolis vulgaris leucoagglutinin. By electron microscopy, the vacuoles present the morphology of multilamellar bodies (MLBs). Treatment of the cells with the lysosomal protease inhibitor leupeptin results in the progressive transformation of the MLBs into electron-dense autophagi

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OKAMURA-OHO, Yuko, Sunqu ZHANG, William HILSON, Aleksander HINEK та John W. CALLAHAN. "Early proteolytic cleavage with loss of a C-terminal fragment underlies altered processing of the β-galactosidase precursor in galactosialidosis". Biochemical Journal 313, № 3 (1996): 787–94. http://dx.doi.org/10.1042/bj3130787.

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Processing of human β-galactosidase (β-GAL) was studied in permanently transfected Chinese hamster ovary (CHO) cells and compared with that in normal cells and in cells from subjects with GM1-gangliosidosis, galactosialidosis and I-cell disease. Biosynthesis of β-GAL in CHO cells results in the synthesis of an 88 kDa glycosylated and phosphorylated monomer precursor which is enzymically active and is secreted into the medium. Post-translational processing begins at the C-terminal end of the protein and gives rise to structurally related 67 and 64 kDa mature forms. These are subsequently degrad

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Kopitz, J., G. O. Kisen, P. B. Gordon, P. Bohley, and P. O. Seglen. "Nonselective autophagy of cytosolic enzymes by isolated rat hepatocytes." Journal of Cell Biology 111, no. 3 (1990): 941–53. http://dx.doi.org/10.1083/jcb.111.3.941.

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Seven cytosolic enzymes with varying half-lives (ornithine decarboxylase, 0.9 h; tyrosine aminotransferase, 3.1 h; tryptophan oxygenase, 3.3 h; serine dehydratase, 10.3 h; glucokinase, 12.7 h; lactate dehydrogenase, 17.0 h; aldolase, 17.4 h) were found to be autophagically sequestered at the same rate (3.5%/h) in isolated rat hepatocytes. Autophagy was measured as the accumulation of enzyme activity in the sedimentable organelles (mostly lysosomes) of electrodisrupted cells in the presence of the proteinase inhibitor leupeptin. Inhibitors of lysosomal fusion processes (vinblastine and asparagi

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Manoury-Schwartz, B. "Selective increased presentation of type II collagen by leupeptin." International Immunology 9, no. 4 (1997): 581–89. http://dx.doi.org/10.1093/intimm/9.4.581.

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BADALAMENTE, MARIE A., LAWRENCE C. HURST, ALFRED STRACHER, SETH PAUL, and JILL MAKOWSKI. "The Effects of Leupeptin on Nerve Repair in Primates." Annals of the New York Academy of Sciences 463, no. 1 Second Colloq (1986): 253–55. http://dx.doi.org/10.1111/j.1749-6632.1986.tb21562.x.

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MIYATA, Koichiro, Akihiko KODAMA, Shen-Fang CHEN, et al. "Induction of Cardiovascular Malformations by Leupeptin in the Rat." Congenital Anomalies 31, no. 1 (1991): 41–45. http://dx.doi.org/10.1111/j.1741-4520.1991.tb00357.x.

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Schröder, Ewald, Christopher Phillips, Elspeth Garman, Karl Harlos, and Catherine Crawford. "X-ray crystallographic structure of a papain-leupeptin complex." FEBS Letters 315, no. 1 (1993): 38–42. http://dx.doi.org/10.1016/0014-5793(93)81128-m.

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Nakajima, T., S. Takauchi, K. Ohara та ін. "α-Synuclein-positive structures induced in leupeptin-infused rats". Brain Research 1040, № 1-2 (2005): 73–80. http://dx.doi.org/10.1016/j.brainres.2005.01.099.

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Li, Jhe‐Hao, Joonseok Oh, Sabine Kienesberger, et al. "Making and Breaking Leupeptin Protease Inhibitors in Pathogenic Gammaproteobacteria." Angewandte Chemie 132, no. 41 (2020): 18028–36. http://dx.doi.org/10.1002/ange.202005506.

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Li, Jhe‐Hao, Joonseok Oh, Sabine Kienesberger, et al. "Making and Breaking Leupeptin Protease Inhibitors in Pathogenic Gammaproteobacteria." Angewandte Chemie International Edition 59, no. 41 (2020): 17872–80. http://dx.doi.org/10.1002/anie.202005506.

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Schönborn, Christina, H. D. Grimmecke, and H. Wand. "Hemmung extrazellulärer Sproßpilzproteinasen durch Pepstatin A und Leupeptin im Plattentest: Inhibition of Extracellular Proteinases from Yeasts by Pepstatin A and Leupeptin in vitro." Mycoses 28, no. 3 (2009): 117–26. http://dx.doi.org/10.1111/j.1439-0507.1985.tb02104.x.

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Singh, Raja B., and Naranjan S. Dhalla. "Ischemia–reperfusion-induced changes in sarcolemmal Na+/K+-ATPase are due to the activation of calpain in the heartThis article is one of a selection of papers published in a Special Issue on Oxidative Stress in Health and Disease." Canadian Journal of Physiology and Pharmacology 88, no. 3 (2010): 388–97. http://dx.doi.org/10.1139/y10-012.

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Depression in cardiac performance due to ischemia–reperfusion (I/R) injury is associated with the development of oxidative stress and decreased sarcolemmal (SL) Na+/K+-ATPase activity. Since both I/R and oxidative stress have been reported to promote the occurrence of intracellular Ca2+ overload and activate proteases such as calpain, this study was undertaken to investigate whether the activation of calpain in I/R hearts is associated with alterations in the SL Na+/K+-ATPase activity and its isoform content. For this purpose, isolated rat hearts treated with and without 2 different calpain in

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Clarke, B. L., and P. H. Weigel. "Differential effects of leupeptin, monensin and colchicine on ligand degradation mediated by the two asialoglycoprotein receptor pathways in isolated rat hepatocytes." Biochemical Journal 262, no. 1 (1989): 277–84. http://dx.doi.org/10.1042/bj2620277.

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We have shown that degradation of asialo-orosomucoid (ASOR) in isolated rat hepatocytes occurs by two different intracellular pathways [Clarke, Oka & Weigel (1987) J. Biol. Chem. 262, 17384-17392] mediated by two subpopulations of cell surface galactosyl (Gal) receptors, designated State 1 or State 2 receptors. In the present study, several inhibitors were tested for their effects on ligand degradation by the State 1 or State 2 pathway. Leupeptin, monensin and chloroquine completely inhibited degradation of 125I-labelled ASOR in both pathways. Dose-response studies showed, however, that th

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Brachet, Valérie, Graça Raposo, Sebastian Amigorena, and Ira Mellman. "Ii Chain Controls the Transport of Major Histocompatibility Complex Class II Molecules to and from Lysosomes." Journal of Cell Biology 137, no. 1 (1997): 51–65. http://dx.doi.org/10.1083/jcb.137.1.51.

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Major histocompatibility complex class II molecules are synthesized as a nonameric complex consisting of three αβ dimers associated with a trimer of invariant (Ii) chains. After exiting the TGN, a targeting signal in the Ii chain cytoplasmic domain directs the complex to endosomes where Ii chain is proteolytically processed and removed, allowing class II molecules to bind antigenic peptides before reaching the cell surface. Ii chain dissociation and peptide binding are thought to occur in one or more postendosomal sites related either to endosomes (designated CIIV) or to lysosomes (designated

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Curtis, A. S., and H. McMurray. "Conditions for fibroblast adhesion without fibronectin." Journal of Cell Science 86, no. 1 (1986): 25–33. http://dx.doi.org/10.1242/jcs.86.1.25.

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Conditions that permit the adhesion of BHK fibroblasts to a variety of surfaces after inhibition of protein synthesis and competition of any adsorbed fibronectin or vitronectin with the fibronectin cell-binding tetrapeptide, Arg-Gly-Asp-Ser (RGDS), are defined. Exposure of the cells to serum components at any stage in the preparation prevents cell attachment if cycloheximide or fibronectin tetrapeptide is present. If leupeptin is used cell adhesion and spreading occur even when all fibronectin synthesis is suppressed by cycloheximide inhibition, or fibronectin binding by tetrapeptide competiti

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