• Asian-Australasian Journal of Animal Sciences
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• 제19권8호
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• pp.1100-1105
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• 2006

During involution of the mammary gland after the lactation period, the gland undergoes an extensive epithelial cell death. In our previous study, overexpression of an extracellular proteinase inhibitor (Expi) gene accelerated apoptosis of mammary epithelial cells. Here we found that expression of the cathepsin D gene was induced in the Expi-overexpressed apoptotic cells. To understand the role of cathepsin D in apoptosis, we transfected cathepsin D gene into mammary epithelial HC11 cells and established the stable cell lines overexpressing the cathepsin D gene. We found that overexpression of the cathepsin D gene partially induced apoptosis of mammary epithelial cells. Expression patterns of the cathepsin D gene were examined in mouse mammary gland at various reproductive stages. Expression of the cathepsin D gene was increased during involution stages compared to lactation stages, and highest expression levels were shown at involution on day 4. We also examined expression of the cathepsin D gene in various mouse tissues. Mammary gland at involution on day 2 showed highest levels of cathepsin D mRNA of the mouse tissues that we examined. Liver tissues showed high levels of cathepsin D expression. These results demonstrate that cathepsin D may contribute to the apoptotic process of mammary epithelial cells.

• 대한세포병리학회지
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• 제11권2호
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• pp.75-81
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• 2000

Cathepsin D is a protease which is known to facilitate invasion and metastasis of breast carcinoma. Overexpression of cathepsin D is associated with poor clinical outcome and biologic aggressiveness of the breast cancer. We underwent immunocytochemical assay(ICA) for cathepsin D in fine needle aspiration cytology(FNAC) specimens from the breast carcinoma and benign breast diseases. In FNAC specimens cathepsin D was expressed in 21(42.9%) out of 49 cases of invasive ductal carcinoma, whereas negative result was observed in all 15 cases of benign breast diseases including 7 fibroadenomas, 6 fibrocystic diseases, and 2 benign ductal hyperplasias. Among the 11 FNAC specimens from ductal carcinoma in situ(DCIS), cathepsin D was expressed in 3 cases(27.3%). In FNAC specimens immunocytochemistry for cathepsin D showed positive result in 24 out of 60 carcinomas(sensitivity, 40%) and negative result in 15 out of all 15 benign breast diseases(specificity, 100%). No significant correlation was noted between cathepsin D expression in FNAC specimen and clinicohistological characteristics of the breast carcinoma, such as hormone receptors and cell differentiation. In conclusion, ICA of cathepsin D in FNAC specimens thought to be a good adjunct to differentiate malignancy from benign breast diseases.

• Tuberculosis and Respiratory Diseases
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• 제49권1호
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• pp.60-71
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• 2000

배경 및 목적 : Cathepsin D는 리소솜에 위치하는 단백분해효소로서 종양의 침윤, 전이, 증식에 관여할 것으로 생각되며, 이러한 작용을 통해 예후에도 중요한 역할을 할 것으로 추정된다. 폐암에서의 Cathepsin D의 예후인자로서의 역할은 아직 확립되지 않고 논란이 많은 실정이다. 이 연구의 목적은 비소세포폐암에서 Cathepsin D 발현의 예후적인 중요성을 알고자 하였다. 방법 : 비소세포 폐암환자 중 치료 목적으로 수술적 처치를 시행한 총 54명의 환자를 대상으로 하여 적출한 폐조직의 면역조직화학적 염색으로 Cathepsin D의 발현을 관찰하고 생존기간 및 TNM 병기와의 관계를 보았다. 결과 : 종양세포에서의 Cathepsin D의 발현은 총 54례 중 18례에서 관찰되어 33.3%의 발현율을 보였으나, 발현군과 비발현군 사이에 조직학적 분화도, 암의 크기. 영역 림프절 침범, 병리조직적 병기(surgical-pathologic stage, p-stage)는 통계적인 유의한 차이를 보이지 않았다. 간질세포에서는 29례(53.7%)에서 중둥도에서 다량(moderate to massive)의 Cathepsin D가 발현되는 것이 관찰되었고, 발현양상과 병리조직적 병기사이에 통계적으로 유의한 관련성이 있었으나(p=0.031), 각각의 조직학적 분화도, 암의 크기, 영역 림프절 침범과는 관계가 없었다. 종양세포와 세포에서의 Cathepsin D 의 발현은 생존율로 표현한 예후와의 유의한 관련성이 없었다. 예후와 관련된 변수를 사용한 다변량 분석결과 영역림프절 침범이 유일한 독립적 예후인자가 되었으며 Cathepsin D는 예후 인자로서의 의미는 없었다. 결론 : 비소세포폐암의 간질세포내 Cathepsin D 발현양상은 병리조직적 병기와 유의한 관련성을 나타내어 종양 진행과의 관련 가능성을 제사하였으나, 다른 임상병리인자들 및 예후와의 관련성은 없었다. 종양세포내에서의 Cathepsin D 발현은 병리조직적 병기를 포함한 임상병리 인자들 및 예후와 관계가 없었다.

• Advances in pediatric surgery
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• 제5권1호
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• pp.39-44
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• 1999

Diagnosing Hirschprung's disease is one of the clinical challenges of this disorder. In the stomach and the intestines, Cathepsin D was readily detected in cytoplasm of the rat gastric and in intestinal ganglion cells of the autonomic nervous system. The objectives of the present study were to examine cathepsin D expression in ganglion cells of the submucosal and myenteric plexuses of the intestine of children and to determine the utility of immunohistochemical staining of cathepsin D for detection of immature ganglion cells. Paraffin blocks of 35 intestinal segments were reviewed for immunohistochemical staining with polyclonal antibody to cathepsin D and hematoxylineosin stainings from the compatible specimens. There were 9 aganglionic segments and 9 ganglionic segments of neonates with Hirschsprung's disease, 8 intestinal segments with non-Hirschsprung's disease in neonates and 9 intestinal segments with non-Hirschsprung's disease infants over the age of 10 months. All ganglion cells showed intense granular cytoplasmic reactivity for cathepsin D regardless of maturity and all aganglionic segments had no expression for cathepsin D in the submucosal and myenteric plexuses of the intestine. However, histiocytes within the laminar propria and submucosa stained positively for cathepsin D. In conclusion, intestinal ganglion cells in children have reactivity for cathepsin D, threrfore immunohistochemical staining for cathepsin D can be used for identification of ganglion cells in neonates.

• 한국패류학회지
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• 제29권2호
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• pp.155-161
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• 2013

Cathepsins are lysosomal/cysteine proteases belong to papain family (C1 family) that is involved in intracellular protein degradation, antigen processing, hormone maturation, and immune responses. In this study, member of cathepsin family was identified from Manila clam (Mc-Cathepsin D) and investigated the immune response against brown ring disease (BRD) causing Vibrio tapetis challenge. The identified Mc-Cathepsin D gene encodes characteristic features typical for the cathepsin family including eukaryotic and viral aspartyl protease signature domain and two highly conserved active sites ($^{84}VVFDTGSSNLWV^{95}$ and $^{270}IADTGTSLLAG^{281}$). Moreover, MC-Cathepsin D shows higher identity values (-50-70%) and conserved amino acids with known cathepsin D members. Transcriptional results (by quantitative real-time RT-PCR) showed that Mc-Cathepsin D was expressed at higher levels in gills and hemocytes than mantle, adductor muscle, foot, and siphon. After the V. tapetis challenge under laboratory conditions, Mc-Cathepsin D mRNA was up-regulated in gills and hemocytes. Present study indicates that Mc-Cathepsin D is constitutively expressed in different tissues and potentially inducible when infecting BRD by V. tapetis. It is further suggesting that Mc-Cathepsin D may be involved in multiple role including immune response reactions against BRD.

• International Journal of Industrial Entomology and Biomaterials
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• 제3권2호
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• pp.121-126
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• 2001

A cDNA encoding a cathepsin D homologue was cloned from a cDNA library of the mulberry longicorn beetle, Apriona germari. Sequence analysis of the cDNA encoding the cathepsin D homologue of A. germari revealed that the 1,158 bp cDNA has an open reading frame of 386 amino acid residues. The deduced protein sequence of the A. germari cathepsin D homologue shows high homology with cathepsin D in insects, Aedes aegypti (68.2% amino acid similarity) and Drosophila melanogaster (67.2% amino acid similarity). Two aspartic residues and six cystein residues in the A. germari cathepsin D homologue are present at identical locations in all of the other catepsins D. Unlike cathepsins D in two insect species, A. gemari cathepsin D homologue appears to have two putative glycosylation sites, rather than one. Phylogenetic analysis revealed the A. germari cathepsin D homologue is more closely related to insect cathepsins D than to the other animal cathepsins D. Northern blot analysis suggests that A. germari cathepsin D homologue gene is expressed in most if not all, body tissues.

• Food Science and Biotechnology
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• 제18권1호
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• pp.84-88
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• 2009

Cathepsin S is a cysteine protease that affects extracellular matrix remodeling. Recently, several studies have reported that cathepsin S is involved in obesity. Both mouse and human adipose cells produce this enzyme in the early phase of adipocyte differentiation, where it degrades fibronectin. Cathepsin S gene expression is elevated in the adipose tissue of obese mice as compared to that of lean mice. Paecilomyces tenuipes water extracts (PTW) are shown to have an inhibitory effect on cathepsin S activity. In this study, Z-Val-Val-Arg-MCA was used as a cathepsin S-specific substrate in order to examine inhibitory effect of PTW. Supplementing 3T3-L1 cell media with PTW clearly reduced lipid droplet accumulation and cathepsin S-induced adipogenesis. Furthermore, PTW decreased weight gain, subcutaneous adipose tissue growth, the level of serum triglyceride, and total cholesterol in mice fed a high-fat diet. These data suggest that PTW work against adipose cathepsin S and presumably contribute to anti-obese activities.

• 대한의생명과학회지
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• 제10권4호
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• pp.429-434
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• 2004

The effects of intravenous administration of high concentration of taurocholic acid (TCA) on cathepsin B and D, and acid phosphatase activities in rat liver lysosome were studied. These liver lysosomal enzymes were determined from the experimental rats with choledocho-caval shunt (CCS). The activities of liver lysosomal cathepsin B and D, and acid phosphatase were found to be significantly increased in the CCS plus TCA injection group than in control group, such as group of CCS alone group. However, these hepatic enzyme activities did not change in the CCS plus tauroursodeoxycholic acid injection group. The above results suggest that TCA stimulates the biosynthesis of the lysosomal cathepsin B and D, and acid phosphatase in the liver.

• 한국미생물·생명공학회지
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• 제27권6호
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• pp.458-465
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• 1999

Streptomyces luteogriseus KT-10 isolated from Korean farm soil produced a strong cathepsin B inhibitor. Optimal conditions for the cathepsin B inhibitor production by s. luteogriseus KT-10 were evaluated. The cathepsin B inhibitor was produced with maximal yield in the cultural condition of pH 7.0 and $25^{\circ}C$ for 4 days. Optimal medium for the cathepsin B inhibitor production was determined to be a medium containing 20g, peptone 3g, yeast extract 1g, K2HPO4 0.5g, MgSO4.7H2O 0.5g, NaNO3 0.5g, NaCl 0.5g per l. The cathepsin B inhibitor produced by S. luteogriseus KT-10 could also inhibit the other proteinases such as trypsin, papain, and cathepsin D.

• International Journal of Industrial Entomology and Biomaterials
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• 제23권1호
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• pp.129-135
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• 2011

Cathepsins are well-characterized proteases that are ubiquitously expressed in lysosomes. Previous work revealed that $Bombyx$ $mori$ cathepsins B and D are expressed in the fat body and undergo decomposition during larval-pupal metamorphosis. Quantitative RT-PCR was performed to detect cathepsin gene expression at the transcription level when challenged by $B.$ $mori$ nuclear polyhedrosis virus (BmNPV), temperature and hormones (20-hydroxyecdysone (20E) and juvenile hormone analogue (JHA)). mRNAs encoding cathepsins B and D were significantly enhanced after the larvae were infected with BmNPV, and the peak of the induction appeared at 1 day before spinning. This attenuated the inducing effect on cathepsin expression caused by infection. Temperature shock induced cathepsin expression at the later stage of the $5^{th}$ instar, and transcription levels varied with development stage and temperature. Cathepsin B and D mRNA expression in the fat body were significantly induced by JHA at the day before spinning, and with 20E, the expression reached a peak at the last day of the $5^{th}$ instar. Cathepsin B and D mRNA expression exhibited detectable changes post-treatment, without significant differences between or among the hormone concentrations.