scholarly journals Lysosomal cysteine proteinases in rat epididymis.

1994 ◽  
Vol 42 (3) ◽  
pp. 417-425 ◽  
Author(s):  
H Tomomasa ◽  
S Waguri ◽  
T Umeda ◽  
K Koiso ◽  
E Kominami ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Enzyme Assay ◽  
Seminal Fluid ◽  
Specific Activity ◽  
Cathepsin L ◽  
The Body ◽  
Similar Distribution ◽  
Cysteine Proteinases ◽  
Intracellular Degradation ◽  
Cathepsin H

To examine the precise localization of lysosomal cysteine proteinases, cathepsins B, H, and L in rat epididymal epithelial cells, immunohistochemistry and enzyme assay were applied to the epididymal tissue. Granular immunodeposits for cathepsins B and H were detected in epididymal epithelial cells, whereas faint or no immunoreactivity for cathepsin L was found. Moreover, immunoreactivity for cathepsin B appeared mainly in principal cells and was more intense in the head of the epididymis than in the tail, whereas that for cathepsin H appeared in both principal and clear cells and was more intense in the tail than the head. By enzyme assay, activities of cathepsins B and H showed a similar distribution to that of the immunoreactivity. The cathepsin L-specific activity was distributed evenly in each part of the epididymis and was also detected in epididymal fluids obtained from the body and tail parts. By immunoblotting, proforms of cathepsins B, H, and L were present in the seminal fluid. The results suggest that cathepsins B and H are involved in the intracellular degradation system of epididymal epithelial cells, and proforms of cathepsins B, H, and L may be secreted into the epididymal duct lumen.

scholarly journals A comparison of four cathepsins (B, L, N and S) with collagenolytic activity from rabbit spleen

1988 ◽  
Vol 256 (2) ◽  
pp. 433-440 ◽  
Author(s):  
R A Maciewicz ◽  
D J Etherington
Keyword(s):  
Cathepsin B ◽  
Specific Activity ◽  
Cathepsin L ◽  
Cross Reactivity ◽  
Enzymic Activity ◽  
Enzyme Linked Immunosorbent Assay ◽  
Collagenolytic Activity ◽  
Cysteine Proteinases ◽  
Isoelectric Points ◽  
Multiple Charge

We have separated four cathepsins (B, L, N and S) from rabbit spleen. They are all collagen-degrading cysteine proteinases, with Mr values of 25,250, 23,500, 34,000 and 30,000 for cathepsin B, L, N and S respectively. Cathepsins B, N and S have isoelectric points of 5.4, 6.2 and 6.8 respectively, whereas cathepsin L exhibited multiple charge forms in the range 5.0-5.7. A comparison of their specific activity against a variety of protein and synthetic substrates shows many differences. These differences can be visually illustrated through isoelectric focusing and detection of enzymic activity with protein and synthetic-substrate overlays. By using an enzyme-linked immunosorbent assay based on the binding to chicken cystatin and detection with polyclonal and monoclonal antibodies to native cathepsins B and L, no cross-reactivity of the four native enzymes was observed. Studies on the co-operative or synergistic effect in degrading collagen indicated that, of the different combinations tested, only the combination of cathepsin B and N exhibited enhanced collagenolysis.

scholarly journals Polarized epithelial cells secrete matriptase as a consequence of zymogen activation and HAI-1-mediated inhibition

2009 ◽  
Vol 297 (2) ◽  
pp. C459-C470 ◽  
Author(s):  
Jehng-Kang Wang ◽  
Ming-Shyue Lee ◽  
I-Chu Tseng ◽  
Feng-Pai Chou ◽  
Ya-Wen Chen ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cells ◽  
Seminal Fluid ◽  
Secretory Granules ◽  
Functional Divergence ◽  
The Body ◽  
In Vivo Studies ◽  
Apical Plasma Membrane ◽  
Zymogen Activation

Matriptase, a transmembrane serine protease, is broadly expressed by, and crucial for the integrity of, the epithelium. Matriptase is synthesized as a zymogen and undergoes autoactivation to become an active protease that is immediately inhibited by, and forms complexes with, hepatocyte growth factor activator inhibitor (HAI-1). To investigate where matriptase is activated and how it is secreted in vivo, we determined the expression and activation status of matriptase in seminal fluid and urine and the distribution and subcellular localization of the protease in the prostate and kidney. The in vivo studies revealed that while the latent matriptase is localized at the basolateral surface of the ductal epithelial cells of both organs, only matriptase-HAI-1 complexes and not latent matriptase are detected in the body fluids, suggesting that activation, inhibition, and transcytosis of matriptase would have to occur for the secretion of matriptase. These complicated processes involved in the in vivo secretion were also observed in polarized Caco-2 intestinal epithelial cells. The cells target latent matriptase to the basolateral plasma membrane where activation, inhibition, and secretion of matriptase appear to take place. However, a proportion of matriptase-HAI-1 complexes, but not the latent matriptase, appears to undergo transcytosis to the apical plasma membrane for secretion. When epithelial cells lose their polarity, they secrete both latent and activated matriptase. Although most epithelial cells retain very low levels of matriptase-HAI-1 complex by rapidly secreting the complex, gastric chief cells may activate matriptase and store matriptase-HAI-1 complexes in the pepsinogen-secretory granules, suggesting an intracellular activation and regulated secretion in these cells. Taken together, while zymogen activation and closely coupled HAI-1-mediated inhibition are common features for matriptase regulation, the cellular location of matriptase activation and inhibition, and the secretory route for matriptase-HAI-1 complex may vary along with the functional divergence of different epithelial cells.

scholarly journals Elastinolytic activity of human cathepsin L

1986 ◽  
Vol 233 (3) ◽  
pp. 925-927 ◽  
Author(s):  
R W Mason ◽  
D A Johnson ◽  
A J Barrett ◽  
H A Chapman
Keyword(s):  
Cathepsin B ◽  
Specific Activity ◽  
Cathepsin L ◽  
Cysteine Proteinases ◽  
Pancreatic Elastase ◽  
Optimum Ph ◽  
Human Cathepsin ◽  
Hydrolysis Of

The hydrolysis of a tritiated elastin substrate by the human cysteine proteinases cathepsins B and L has been studied. Cathepsin L was found to be at least 100-fold more active on this substrate than cathepsin B. The specific activity of cathepsin L at pH 5.5 for hydrolysis of elastin was about the same as that of pig pancreatic elastase at its optimum pH of 8.8.

Hypothetical Role of Growth Factors to Reduce Intervertebral Disc Degeneration Significantly through Trained Biological Transformations

2020 ◽  
Vol 26 ◽  
Author(s):  
Cristian Muresanu ◽  
Siva G. Somasundaram ◽  
Sergey V. Vissarionov ◽  
Liliya V. Gavryushova ◽  
Vladimir N. Nikolenko ◽  
...  
Keyword(s):  
Growth Factors ◽  
Blood Circulation ◽  
Seminal Fluid ◽  
Prostate Gland ◽  
The Body ◽  
Personal Experiences ◽  
Biological Transformation ◽  
The Mind

Background: From the evidence of failed injection-based growth factor therapies, it has been proposed that a naturally triggered uninterrupted blood circulation of the growth factors would be superior. Objective: We seek to stimulate discussions and more research about the possibility of using the already available growth factors found in the prostate gland and endometrium by starting a novel educable physiology, known as biological transformations controlled by the mind. Methods: We summarized the stretch-gated ion channel mechanism of the cell membrane, and offer several practical methods that can be applied by anyone, in order to stimulate and enhance the blood circulation of the growth factors from the seminal fluid to sites throughout the body. This details the practical application of our earlier published studies about biological transformations. Results: A previously reported single-patient case study has been extended, adding more from his personal experiences continually improving this novel physiological training and extending the ideas from our earlier findings in detail. Conclusion: The biological transformation findings demonstrate the need additional research to establish the benefits of these natural therapies to repair and rejuvenate tissues affected by various chronic diseases or aging processes.

scholarly journals CHANGES IN FINE STRUCTURE DURING SILK PROTEIN PRODUCTION IN THE AMPULLATE GLAND OF THE SPIDER ARANEUS SERICATUS

1969 ◽  
Vol 42 (1) ◽  
pp. 284-295 ◽  
Author(s):  
Allen L. Bell ◽  
David B. Peakall
Keyword(s):  
Fine Structure ◽  
Epithelial Cells ◽  
Protein Production ◽  
Distal Portion ◽  
Silk Gland ◽  
The Body ◽  
Single Type ◽  
Secretory Cells ◽  
The Web ◽  
Tunica Intima

The ampullate silk gland of the spider, Araneus sericatus, produces the silk fiber for the scaffolding of the web. The fine structure of the various parts of the gland is described. The distal portion of the duct consist of a tube of epithelial cells which appear to secrete a substance which forms the tunica intima of the duct wall. At the proximal end of the duct there is a region of secretory cells. The epithelium of the sac portion contains five morphologically distinct types of granules. The bulk of the synthesis of silk occurs in the tail of the gland, and in this region only a single type of secretory droplet is seen in the epithelium. Protein synthesis can be stimulated by the injection of 1 mg/kg acetylcholine into the body fluids. 10 min after injection, much of the protein stored in the cytoplasm of the epithelial cells has been secreted into the lumen. 20 min after stimulation, the ergastoplasmic sacs form large whorls in the cytoplasm. Protein, similar in electron-opacity to protein found in the lumen, begins to form in that portion of the cytoplasm which is enclosed by the whorls. The limiting membrane of these droplets is formed by ergastoplasmic membranes which lose their ribosomes. No Golgi material has been found in these cells. Protein appears to be manufactured in the cytoplasm of the tail cells in a form which is ready for secretion.

The cysteine proteinases of Schistosoma mansoni cercariae

Parasitology ◽  
1997 ◽  
Vol 114 (2) ◽  
pp. 105-112 ◽  
Author(s):  
J. P. DALTON ◽  
K. A. CLOUGH ◽  
M. K. JONES ◽  
P. J. BRINDLEY
Keyword(s):  
Schistosoma Mansoni ◽  
Cathepsin B ◽  
Cathepsin L ◽  
Serine Proteinase ◽  
Skin Penetration ◽  
Scanning Electron Micrographs ◽  
Cysteine Proteinases ◽  
Similar Function ◽  
Substrate Preferences ◽  
Serine Proteinase Activity

Based on substrate preferences, cercariae of Schistosoma mansoni were seen to express both cathepsin L and cathepsin B cysteine proteinases, although the former activity was many -fold greater. Two cathepsin L activities identified in cercarial extracts by zymography co-migrated with activities in extracts of 3 h and 24 h schisotosomula and in extracts of adult worms. Since these enzymes have been implicated in haemoglob in digestion by adult worms, they may perform a similar function in schistosomula. Immunolocalization using scanning electron micrographs showed that cathepsin L and cathepsin B proteinases were present in the cercarial post-acetabular glands. In addition, cercarial serine proteinase activities considered to facilitate skin penetration efficiently cleaved the substrates Z-Gly-Pro-Arg-NHMec and Z-Gly-Pro-Lys-NHMec. Cercariae release most of this serine proteinase activity when induced to secrete the contents of their acetabular glands. In contrast, newly transformed 3 h and 24 h schistosomula did not express this activity.

Epithelial cells and their importance in the body

1927 ◽  
Vol 23 (12) ◽  
pp. 1287-1287
Keyword(s):  
Epithelial Cells ◽  
The Body

With a number of new studies the author proves his earlier view that epithelial cells produce a hormone circulating in the blood and passing into milk during lactation. The switching off of this hormone when the epithelial cells are removed leads to a decrease of calcium in the blood and causes tetany.

Expression of a novel FGF in the Xenopus embryo. A new candidate inducing factor for mesoderm formation and anteroposterior specification

Development ◽  
1992 ◽  
Vol 114 (3) ◽  
pp. 711-720 ◽  
Author(s):  
H.V. Isaacs ◽  
D. Tannahill ◽  
J.M. Slack
Keyword(s):  
Specific Activity ◽  
Biological Properties ◽  
The Body ◽  
Mesoderm Induction ◽  
Gastrula Stage ◽  
Blastula Stage ◽  
Mesoderm Formation ◽  
Low Levels

We have cloned and sequenced a new member of the fibroblast growth factor family from Xenopus laevis embryo cDNA. It is most closely related to both mammalian kFGF (FGF-4) and FGF-6 but as it is not clear whether it is a true homologue of either of these genes we provisionally refer to it as XeFGF (Xenopus embryonic FGF). Two sequences were obtained, differing by 11% in derived amino acid sequence, which probably represent pseudotetraploid variants. Both the sequence and the behaviour of in vitro translated protein indicates that, unlike bFGF (FGF-2), XeFGF is a secreted molecule. Recombinant XeFGF protein has mesoderm-inducing activity with a specific activity similar to bFGF. XeFGF mRNA is expressed maternally and zygotically with a peak during the gastrula stage. Both probe protection and in situ hybridization showed that the zygotic expression is concentrated in the posterior of the body axis and later in the tailbud. Later domains of expression were found near the midbrain/hindbrain boundary and at low levels in the myotomes. Because of its biological properties and expression pattern, XeFGF is a good candidate for an inducing factor with possible roles both in mesoderm induction at the blastula stage and in the formation of the anteroposterior axis at the gastrula stage.

Temperature-sensitive forms of large and small invertase in a mutant derived from a SUC1 strain of Saccharomyces cerevisiae

1981 ◽  
Vol 1 (5) ◽  
pp. 460-468
Author(s):  
T Mizunaga ◽  
J S Tkacz ◽  
L Rodriguez ◽  
R A Hackel ◽  
J O Lampen
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Parent Strain ◽  
Specific Activity ◽  
Single Gene ◽  
Companion Paper ◽  
Cellular Level ◽  
Temperature Sensitive ◽  
Mutagenic Treatment ◽  
Intracellular Degradation ◽  
Subunit Molecular Weight

Mutagenesis of the sucrose-fermenting (SUC1) Saccharomyces cerevisiae strain 4059-358D yielded an invertase-negative mutant (D10). Subsequent mutagenic treatment of D10 gave a sucrose-fermenting revertant (D10-ER1) that contained the same amount of large (mannoprotein) invertase as strain 4059-358D but only trace amounts of the smaller intracellular nonglycosylated enzyme. Limited genetic evidence indicated that the mutations in D10 and D10-ER1 are allelic to the SUC1 gene. The large invertases from D10-ER1 and 4059-358D were purified and compared. The two enzymes have similar specific activity and Km for sucrose, cross-react immunologically, and show the same subunit molecular weight after removal of the carbohydrate with endo-beta-N-acetylglucosaminidae H. They differ in that the large enzyme from the revertant is rapidly inactivated at 55 degrees C, whereas that from the parent is relatively stable at 65 degrees C. The small invertase in extracts of D10-ER1 is also heat sensitive as compared to the small enzyme from the original parent strain. The low level of small invertase in mutant D10-ER1 may reflect increased intracellular degradation of this heat-labile form. In several crosses of D10-ER1 with strains carrying the SUC1 or SUC3 genes, the temperature sensitivity of the large and small invertases and the low cellular level of small invertase appeared to cosegregate. These findings are evidence that SUC1 is a structural gene for invertase and that both large and small forms are encoded by a single gene. A detailed genetic analysis is presented in a companion paper.

An ultrastructural and cytochemical study of microbodies in the genus Nitella (Characeae)

1973 ◽  
Vol 51 (11) ◽  
pp. 2025-2032 ◽  
Author(s):  
B. A. Silverberg ◽  
T. Sawa
Keyword(s):  
Enzyme Assay ◽  
The Body ◽  
Cytochemical Localization ◽  
Cytochemical Study ◽  
Spherical Inclusions ◽  
Complete Digestion ◽  
Assay Methods ◽  
Granular Matrix ◽  
Available Information

Electron microscopy of the cells of the characean alga Nitella flexilis revealed the presence of numerous spherical inclusions which morphologically resemble plant microbodies. The structures have a dense granular matrix and are bounded by a single membrane. Many of the microbodies contain very electron-dense nucleoids that were shown to be alpha-amylase sensitive. In cells of the young apex, microbodies are the most abundant cellular organelle and are intimately associated with dilated cisternae of the endoplasmic reticulum and Golgi complexes, and with large osmiophilic lipid bodies. Although the microbody population appears reduced in mature branchlet cells and internode cells of the main axis, they exhibit a characteristic and frequent association with the chloroplasts. Turnover of microbodies involves some autolytic degradation of the body matrix until complete digestion presumably occurs. Developmental changes of microbodies were monitored with the cytochemical localization of lysosomal aryl sulfatase and acid phosphatase activities. The current study is of interest since catalase, an enzyme marker of microbodies in a variety of tissues, could not be detected using both cytochemical and enzyme assay methods. The functional role of microbodies in Nitella cells is explored in relation to presently available information.

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